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Information on EC 2.7.7.48 - RNA-directed RNA polymerase
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2.7.7.48 RNA-directed RNA polymeraseIUBMB Comments
Catalyses RNA-template-directed extension of the 3'- end of an RNA strand by one nucleotide at a time. Can initiate a chain de novo. See also EC 2.7.7.6 DNA-directed RNA polymerase.
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Word Map
- 2.7.7.48
- viruses
- strand
-
rnaps
-
single-stranded
- bacteriophage
- chromatin
- vaccine
- infectious
-
holoenzyme
- rrna
- helicase
- dsrnas
- ribonucleoproteins
- virion
- coronavirus
-
dna-dependent
-
outbreak
- replicons
- covid-19
- polyproteins
-
footprint
-
polyadenylation
- fever
- dengue
- pandemic
- polya
- nucleocapsids
-
serotype
- ribavirin
-
sequence-specific
- pre-mrnas
-
virological
-
non-structural
- duplex
-
stem-loops
- nucleoprotein
-
virus-infected
-
supercoiled
- rifampicin
-
unwind
-
virus-like
-
nucleolar
-
non-nucleoside
- gastroenteritis
- encephalitis
-
stall
-
anti-hcv
- dicer
-
virus-specific
- rotavirus
- synthesis
- drug development
- pharmacology
- medicine
- analysis
- molecular biology
The enzyme appears in viruses and cellular organisms
Synonyms
rna polymerase, rna-binding protein, rna-dependent rna polymerase, rdrp, nonstructural protein, transcriptase, vp1 protein, pol iv, rna-dependent rna polymerases, ns5b polymerase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
111 kDa protein
-
-
-
-
180 kDa protein
-
-
-
-
182 kDa protein
-
-
-
-
183 kDa protein
-
-
-
-
186 kDa protein
-
-
-
-
216.5 kDa protein
-
-
-
-
2A protein
-
-
-
-
3CD protein
-
precursor of the RNA-dependent RNA polymerase, although 3CD is a fully functional protease, it lacks polymerase activity
3D pol
-
-
-
-
3D polymerase
3Dpol
3Dpol-like protein
-
the RNA-dependent RNA polymerase is associated with the 3Dpol-like protein
69.6 kDa protein
-
-
-
-
core protein
-
-
-
-
core protein VP1
-
-
-
-
HC-J4 NS5BDELTA21
-
a C-terminally truncated polymerase based on the consensus sequence of pCV-J4L6S
HCV NS5B polymerase
influenza polymerase PA
inner layer protein VP1
-
-
-
-
JEV NS5
-
nonstructural protein that carries both methyltransferase and RNA-dependent RNA polymerase (RdRp) domains
JEV NS5 protein
jRdRp
L protein
-
-
-
-
large structural protein
-
-
-
-
M1 phosphoprotein
-
-
-
-
NIB
-
-
-
-
nonstructural phosphoprotein
-
-
-
-
nonstructural protein
-
-
-
-
nonstructural protein 5B
NS5
NS5 protein
NS5 RdRp
NS5B
NS5B polymerase
NS5B protein
NS5B RdRp
NS5B RNA-dependent RNA polymerase
nsp12
nucleocapsid phosphoprotein
-
-
-
-
nucleotidyltransferase, ribonucleate, RNA-dependent
-
-
-
-
ORF1
-
-
-
-
ORF1A
-
-
-
-
ORF1B
-
-
-
-
P protein
-
-
-
-
P180
-
-
-
-
P3D
-
-
-
-
P66
-
-
-
-
P70
-
-
-
-
P88 protein
-
-
-
-
PB1
-
-
-
-
PB1 proteins
-
-
-
-
PB2
-
-
-
-
PB2 proteins
-
-
-
-
Phage f2 replicase
-
-
-
-
picornaviral 3D polymerase
Pol
-
-
-
-
polymerase acidic protein
-
-
-
-
polymerase basic 1 protein
-
-
-
-
polymerase L
-
-
-
-
proteins PB1
-
-
-
-
proteins, PB 2
-
-
-
-
proteins, specific or class, lambda3, of reovirus
-
-
-
-
proteins, specific or class, PB 1
-
-
-
-
proteins, specific or class, PB 2
-
-
-
-
Q-beta replicase
-
-
-
-
Qbeta replicase
Qbeta-replicase
-
-
-
-
RDR
RDR1
RDR2
RDR6
RDRP
replicase, phage f2
-
-
-
-
replicase, Qbeta
-
-
-
-
ribonucleic acid replicase
-
-
-
-
ribonucleic acid-dependent ribonucleate nucleotidyltransferase
-
-
-
-
ribonucleic acid-dependent ribonucleic acid polymerase
-
-
-
-
ribonucleic replicase
-
-
-
-
ribonucleic synthetase
-
-
-
-
RNA dependent RNA polymerase
RNA nucleotidyltransferase (RNA-directed)
-
-
-
-
RNA polymerase
RNA replicase
-
-
-
-
RNA synthetase
-
-
-
-
RNA transcriptase
-
-
-
-
RNA-binding protein
-
-
-
-
RNA-dependent ribonucleate nucleotidyltransferase
-
-
-
-
RNA-dependent RNA polymerase
RNA-dependent RNA polymerase 1
RNA-dependent RNA polymerase NIb
RNA-dependent RNA polymerases
RNA-dependent RNA replicase
-
-
-
-
RNA-dependent RNA-polymerase
RNA-directed RNA polymerase
-
-
-
-
RNA-directed RNA polymerase L
RRF-3
RrpC
sigma NS protein
-
-
-
-
transcriptase
VP1
VP1 protein
-
-
-
-
additional information
3D polymerase
-
-
-
-
nonstructural protein 5B
-
-
-
-
NS5
-
consists of a C-terminal RNA-dependent RNA polymerase domain and an N-terminal methyltransferase domain
NS5
-
consists of a C-terminal RNA-dependent RNA polymerase domain and an N-terminal methyltransferase domain
NS5
-
consists of a C-terminal RNA-dependent RNA polymerase domain and an N-terminal methyltransferase domain
NS5
-
consists of a C-terminal RNA-dependent RNA polymerase domain and an N-terminal methyltransferase domain
NS5
-
consists of a C-terminal RNA-dependent RNA polymerase domain and an N-terminal methyltransferase domain
NS5
-
consists of a C-terminal RNA-dependent RNA polymerase domain and an N-terminal methyltransferase domain
NS5
-
consists of a C-terminal RNA-dependent RNA polymerase domain and an N-terminal methyltransferase domain
NS5
-
consists of a C-terminal RNA-dependent RNA polymerase domain and an N-terminal methyltransferase domain
NS5
-
NS5 consists of an N-terminal methyltransferase domain and the C-terminal RNA-dependent RNA polymerase (RdRp) domain
NS5
-
NS5 consists of an N-terminal methyltransferase domain and the C-terminal RNA-dependent RNA polymerase (RdRp) domain
-
NS5 protein
-
bifunctional and contains 900 amino acids. The S-adenosyl methionine transferase activity resides within its N-terminal domain, and residues 270 to 900 form the RNA-dependent RNA polymerase (RdRp) catalytic domain
NS5 RdRp
-
NS5 is a viral nonstructural protein that carries both methyltransferase and RNA-dependent RNA polymerase domains, it is a key component of the viral RNA replicase complex that presumably includes other viral nonstructural and cellular proteins
NS5B
-
-
-
-
NS5B protein
-
-
-
-
Qbeta replicase
-
-
-
-
RDRP
-
-
-
-
RDRP
-
-
RDRP
-
RNA-dependent RNA polymerase
-
-
-
-
RNA-dependent RNA polymerase
-
-
RNA-dependent RNA polymerase
-
-
RNA-dependent RNA polymerase
-
RNA-dependent RNA polymerase
-
consists of three viral proteins, PB1, PB2, and PA
RNA-dependent RNA polymerase 1
-
transcriptase
-
-
-
-
VP1
-
-
-
-
additional information
-
the enzyme belongs to the supergroup I of RNA-dependent RNA polymerases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
nucleoside triphosphate + RNAn = diphosphate + RNAn+1
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
nucleoside-triphosphate:RNA nucleotidyltransferase (RNA-directed)
Catalyses RNA-template-directed extension of the 3'- end of an RNA strand by one nucleotide at a time. Can initiate a chain de novo. See also EC 2.7.7.6 DNA-directed RNA polymerase.
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CAS REGISTRY NUMBER
COMMENTARY
9026-28-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(dT)12 + UTP
diphosphate + ?
-
assay uses poly(A) as an RNA template and oligo(dT)12-18 as the primer. Enzyme is strictly dependent on the presence of primer
-
-
?
2'-C-methyl-ATP + RNAn
diphosphate + RNAn+1
-
-
-
ir
5-fluorouridine triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme incorporates 5-fluorouridine monophosphate during RNA elongation in place of UMP or CMP using homopolymeric and heteropolymeric templates. Incorporation of 5-fluorouridine monophosphate does not prevent chain elongation, and, in some sequence contexts, it favors misincorporations at downstream positions. 5-Fluorouridine monophosphate is incorporated into the nascent RNA and occupies the new 3'-end of the primer at the active site of the enzyme. 5-Fluorouridine monophosphate establishes a Watson and Crick pair with the corresponding acceptor AMP in the template strand and an additional hydrogen bond with Ser304 of the polymerase. Further interactions, similar to those observed with standard nucleotides, contribute also to stabilize 5-fluorouridine monophosphate in the 3'-terminus of the RNA. When present in the template, 5-fluorouridine monophosphate directs the incorporation of AMP and GMP, with ATP being a more effective substrate than GTP. The misincorporation of GMP is 17fold faster opposite 5-fluorouridine than opposite U in the template. But Incorporated 5-fluorouridine monophosphate is not a chain terminator during RNA elongation
RNA with incoporated 5-fluorouridine phosphate
-
?
ara-ATP + RNAn
diphosphate + RNAn+1
-
-
-
ir
dATP + RNAn
diphosphate + RNAn+1
-
-
-
ir
remdesivir triphosphate + RNAn
diphosphate + RNAn+1
remdesivir triphosphate is effective in combating COVID-19 because it is a better substrate than ATP for the viral RNA-dependent RNA polymerase
-
-
?
ribavirin triphosphate + RNAn
?
ribavirin is a guanosine analogue that can be a substrate for the viral RNA polymerase. HCV is genetically variable, and this genetic variation can affect the polymerase's use of ribavirin triphosphate, overview
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
ir
ATP + RNAn
diphosphate + RNAn+1
RNA template with the first 25 nucleotides from the TrC (Trailer complement) sequence
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
?
ATP + RNAn
diphosphate + RNAn+1
-
-
-
ir
CTP + RNAn
diphosphate + RNAn+1
RNA template with the first 25 nucleotides from the TrC (Trailer complement) sequence
-
-
?
CTP + RNAn
diphosphate + RNAn+1
-
-
-
ir
GTP + poly(C)
diphosphate + ?
-
use of poly(C) as template annealed with oligoG12 as primer
-
-
?
GTP + poly(C)
diphosphate + ?
-
use of poly(C) as template annealed with oligoG12 as primer
-
-
?
GTP + RNAn
diphosphate + RNAn+1
RNA template with the first 25 nucleotides from the TrC (Trailer complement) sequence
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme should be involved in the replication of BaMV
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
full-length negative strand BBV RNAs are synthesized
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme synthesizes single-stranded RNA transcripts of one polarity which are identical in size to the denatured parental double-stranded RNA segments
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme is active in an in vitro RNA polymerase assay using homopolymeric RNA or BVDV minigenomic RNA templates. The major product is a covalently linked double-stranded molecule. In addition, a nucleotide-nonspecific and template-independent terminal nucleotidyl transferase activity is observed
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
dependent on and specific for BMV RNA
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
RNAs of Brome mosaic virus and the closely related cowpea Chlorotic mottle virus are the most effective, but some activity is also shown by certain other viral nucleic acids and polyribonucleotides
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
using poly(rA)/(dT)15 as a template-primer system
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
using poly(rA)/(dT)15 as a template-primer system
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme is completely dependent on exogenous template. The enzyme utilizes a variety of viral RNAs and CMV satellite RNA as template for minus-strand synthesis. Cellular RNAs are not used as templates
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme copies CMV RNA and several other viral RNAs, Brome mosaic virus RNA, Alfalfa mosaic virus RNA and Tobacco mosaic virus RNA. Activity with poly(C) and poly(U) but not poly(A) or poly(G). The product with CMV RNA as template is heterogenous in size with a peak length of about 150 residues
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
GTP + CMV RNA, yeast RNA or poly(C)
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Cystovirus phi6
the polymerase structure is switchable, with a discrete set of contacts stabilizing the initiation-competent form of the enzyme so that relatively modest changes can have-range effects, controlling the switch from the initiation to elongation phase, with premature conformational switching producing a structure that preferentially initiates by back-priming
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Cystovirus phi6
-
template is RNA, the phi6 polymerase is highly processive and can use either single- or double-stranded RNA as a template and synthesizes a full-length complementary strand of an RNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Cystovirus phi6
-
NTPs are ATP, GTP, CTP, and UTP, roles of the negatively charged plough area on the polymerase surface, of the rim of the template tunnel and of the template specificity pocket that is key in the formation of the productive RNA-polymerase binary complex. The positively charged rim of the template tunnel has a significant role in the engagement of highly structured ssRNA molecules, whereas specific interactions further down in the template tunnel promote ssRNA entry to the catalytic site
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Q6DLV0
homopolymer C as the template and biotinoligo(G)20 as the primer
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Q6DLV0
using homopolymer C as the template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
enzyme initiates RNA synthesis in a primer- and poly(A)-dependent manner in vitro
product is double-stranded RNA
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme does not manifest strict specificity towards EMC RNA template. It can use also Qbeta RNA, rRNA of BHK cells or poly(C)
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
catalysis and translocation are uncoupled in the viral RNA-dependent RNA polymerase. A motif B loop may assist the movement of the template strand in late stages of transcription
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
poly(A)-dependent oligo(U)-primed poly(U) polymerase activity. In the presence of an oligo(U) primer, the enzyme catalyzes the synthesis of a full-length copy of either poliovirus or globin RNA templates. In the absence of added primer, RNA products up to twice the length of the template are synthesized
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
kinetic mechanism for single nucleotide incorporation catalyzed by poliovirus polymerase in presence of Mg2+
-
-
r
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
RdRP incorporation of incorrect nucleosides is inefficient, making precise determination of kinetic parameters experimentally challenging. The fidelity for poliovirus polymerase 3Dpol ranges from 12000 to 1000000 for transition mutations and 32000 to 43000000 for transversion mutations
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
VPg (a peptide comprising the 3B region of protein 3AB) is the 22-residue soluble product of 3AB cleavage and serves as the protein primer for RNA replication
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
substrate is HP1 RNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
purified recombinant FMDV 3D is active in polymerization assays using homopolymeric and heteropolymeric primer templates and in binding to RNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
inducible enzyme
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
ATP, the enzyme requires a single-stranded molecule of RNA or polyribonucleotide as template, initiates new chains with purine ribonucleoside triphosphates
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
661081, 662733, 673227, 690468, 690470, 690615, 691255, 691257, 691273, 692029, 693537, 695258, 737570, 738678, 738870, 759501
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
polyC/oligoG is more efficient in supporting the HCV NS5B polymerase activity than polyA/oligodT. PolyA/oligoU or polyI/oligodC
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme performs RNA- or DNA oligonucleotide primer-dependent RNA synthesis on templates with a blocked 3' end or on homopolymeric templates
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
ribonucleotide-incorporating activity on an in vitro transcribed RNA containing the 3' end of the HCV genome. It also possesses ribunucleotide incorporation activity, to a lesser extent, on in vitro transcribed foreign RNA templates when RNA or DNA primers are present. The activity is higher with DNA primers than with RNA primers
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
RNA-dependent RNA polymerase activity uses poly(C) most efficiently as a template but is inactive on poly(U) and poly(G). The enzyme is able to copy a full-length or nearly full-length genome in the absence of additional viral or cellular cofactors. Poly(C)-oligo(G)12 is the most efficient substrate
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
once synthesis has begun, the C-terminally truncated enzyme NS5B(DELTA21) does not dissociate from the template until a complete double strand copy of the RNA is made
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
replication of Hepatitits C virus is thought to proceed via the initial synthesis of a complementary (-)RNA strand, which serves, in turn, as a template for the production of progeny (+)-strand RNA molecules. An RNA-dependent RNA polymerase is postulated to be involved in these steps
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
essential catalytic enzyme for HCV replication. NS5A binds RNA-dependent RNA polymerase and modulates RNA-dependent RNA polymerase activity
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
NS5B RdRp is essential for viral replication
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
poly(C) RNA template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
nculeotides are GTP, CTP, ATP, and UTP, the RNA templates for the enzyme assay are transcribed from linearized murine inducible nitric oxide synthase, iNOS, clone having 400 nt insert in an in vitro transcription reaction using SP6 RNA polymerase
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
B2 RNA is a substrate for RNA dependent RNA polymerization by Pol II
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
B2 RNA is a substrate for RNA dependent RNA polymerization by Pol II. Extension of B2 RNA by Pol II occurs from the 3'-end and is internally templated and requires all four NTPs, mechanism, overview. No activity with B2 RNA mutated at C155 to G
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
in vitro transcription using the model RNA template, v84
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
various RNA substrates: Alu RNA, 110 nucleotides of the Alu domain of Pyrococcus horikoshii SRP RNA, Candida albicans tRNAAsn, U-rich RNA (59-GGCCAUCCUGU7 CCCU11CU19-39)29, ph-RNA of 81 nucleotides30, and short ph-RNA of 36 nucleotides comprising just the conserved 3' and 5' ends with a short linker and circular single stranded DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
various RNA substrates: Alu RNA, 110 nucleotides of the Alu domain of Pyrococcus horikoshii SRP RNA, Candida albicans tRNAAsn, U-rich RNA (59-GGCCAUCCUGU7 CCCU11CU19-39)29, ph-RNA of 81 nucleotides30, and short ph-RNA of 36 nucleotides comprising just the conserved 3' and 5' ends with a short linker and circular single stranded DNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
replication occurs through de novo initiation and involves a complementary RNA intermediate
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
JEV NS5 protein can initiate RNA synthesis through a de novo initiation mechanism. JEV NS5 protein is more efficient in using negative-strand RNA templates, indicating that the JEV NS5 protein is involved in regulating the ratio of positive strand RNA to negative strand RNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
JEV NS5 protein can initiate RNA synthesis through a de novo initiation mechanism. JEV NS5 protein is more efficient in using negative-strand RNA templates
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the NS5 protein is able to use both plus- and minus-strand 3'-untranslated regions of the JEV genome as templates in the absence of a primer, with the latter RNA being a better template. Analysis of the RNA synthesis initiation site using the 3'-end 83 nucleotides of the JEV genome as a minimal RNA template reveals that the NS5 protein specifically initiates RNA synthesis from an internal site, U81, at the two nucleotides upstream of the 3'-end of the template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
poly(A) RNA template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
uses JEV and dengue-2 virus 3' end plus- and minus-strand RNA templates, the incorporation of [32P]-UMP is much lower when using positive-strand RNA as template than when using negative-strand RNA - an almost 10fold difference in efficiency
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
primer-free initiation assay with 13-nt RNA template, and ATP, CTP, FAM-UTP, and GTP, and additionally with a primer (5'-GUUCACACAGAUAAACUUCU-3') with a 6-FAM-labeled at the 5'-end in the primer extension assay
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
JEV NS5 protein can initiate RNA synthesis through a de novo initiation mechanism. JEV NS5 protein is more efficient in using negative-strand RNA templates, indicating that the JEV NS5 protein is involved in regulating the ratio of positive strand RNA to negative strand RNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
JEV NS5 protein can initiate RNA synthesis through a de novo initiation mechanism. JEV NS5 protein is more efficient in using negative-strand RNA templates
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
uses JEV and dengue-2 virus 3' end plus- and minus-strand RNA templates, the incorporation of [32P]-UMP is much lower when using positive-strand RNA as template than when using negative-strand RNA - an almost 10fold difference in efficiency
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
primer-free initiation assay with 13-nt RNA template, and ATP, CTP, FAM-UTP, and GTP, and additionally with a primer (5'-GUUCACACAGAUAAACUUCU-3') with a 6-FAM-labeled at the 5'-end in the primer extension assay
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
incorporation is more dependent on exogenopus UTP and GTP than ATP or CTP
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
incorporation is more dependent on exogenopus UTP and GTP than ATP or CTP
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
La France isometric virus
-
the enzyme is probably a transcriptase engaged in the synthesis of ssRNA transcripts corresponding to each of the virion-associated dsRNAs
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the polymerase product anneals only to measles RNA and not to Vero cell RNA
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme catalyzes cap methylation of virus-specific mRNA as well as RNA synthesis
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
viral ribonucleoprotein complexes and purified recombinant L protein but not P protein exhibit mRNA (guanine-7-)methyl-transferase activity. mRNA synthesis in a reconstituted transcription system using purified N protein-genomic RNA complex as a template requires both the L and P proteins. Enzymatic properties of Senda virus mRNA (guanine-7-)methyl-transferase are different to that of cellular mRNA (guanine-7-)methyl-transferase. Unlike cellular enzyme, the SeV enzyme preferentially methylates capped RNA containing the viral mRNA 5'-end sequences (GpppApGpG-). The C-terminal part (amino acid residues 1,7562,228) of the L protein catalyzes cap methylation, whereas the N-terminal half (residues 11,120) containing putative RNA polymerase subdomains does not
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the random polymers poly(UG), poly(UC), poly(AG) and poly(AU) serve as more effective templates than homopolymers
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
NV 3Dpol yields two different products when incubated with synthetic RNA in vitro: (1) a double-stranded RNA consisting of two single strands of opposite polarity or (2) the single-stranded RNA template labelled at its 39 terminus by terminal transferase activity. Initiation of RNA synthesis by NV 3Dpol on heteromeric RNA template occurs de novo
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
rNTP substrate binding structure, multistep model of nucleotide incorporation, overview
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
when the nucleotide concentrations are low, C is incorporated at the fastest rate and G at the slowest. G-incorporation step largely limits the overall reaction rate
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
synthesis of RNA in response to RNA template. An RNA primer can substitute for GTP to allow initiation. Mn2+ might reduce the template specificity by forming a complex with GTP that is more efficiently incorporated than is Mg*GTP with unfavored template
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
GTP and polyC
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
GTP and polyC
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
composed of one phage-coded polypeptide and three host-supplied polypeptides which function in the biosynthesis of proteins in the uninfected host. Two of theses polypeptides, protein elongation factors EF-Tu and EF-Ts, are required for initiation of transcription by replicase with all templates
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
Qbeta replicase is an RNA-dependent RNA polymerase responsible for replicating the RNA genome of coliphage Qbeta and plays a key role in the life cycle of the Qbeta phage
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
kinetic model for the RNA replication reaction
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Qubevirus durum Qbetaam12
-
synthesis of RNA in response to RNA template. An RNA primer can substitute for GTP to allow initiation. Mn2+ might reduce the template specificity by forming a complex with GTP that is more efficiently incorporated than is Mg*GTP with unfavored template
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Qubevirus durum QbetaamB86
-
synthesis of RNA in response to RNA template. An RNA primer can substitute for GTP to allow initiation. Mn2+ might reduce the template specificity by forming a complex with GTP that is more efficiently incorporated than is Mg*GTP with unfavored template
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
the enzyme (RdRP) is essential for both transcription and replication of the viral RNA genome
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
in presence of Mg2+ significant activity is observed when poly(A) or poly(C) is used as template and the activity is template and primer-dependent. Poly(G) and poly(U) templates are not efficient substrates. Biotinylated oligoDNA primers appear to work slightly more efficiently than oligoRNA primers. In presence of Mn2+ activity is stimulated 2.5-5.6fold. RNA synthesis using poly(C) as template becomes primer-independent
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
RNA polymerase activity on homopolymeric templates poly(A) and poly(C) and heteropolymeric RNA templates primed with either RNA or DNA oligonucleotide primers or self-primed by a copy-back mechanism
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
required for replication of the HRV RNA genome
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
in addition to RNA-dependent RNA polymerase activity the enzyme also possesses cap-snatching capacity
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
in addition to RNA-dependent RNA polymerase activity the enzyme also possesses cap-snatching capacity
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
key enzyme of replication
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
in a synthetic RNA template-dependent reaction, sapovirus 3Dpol synthesizes a double-stranded RNA or labels the template 3' terminus by terminal transferase activity. Initiation of RNA synthesis occurs de novo on heteropolymeric templates or in a primer dependent manner on polyadenylated templates
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
essential enzyme for viral RNA replication
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
key enzyme responsible for the SARS-CoV-2 replication process, catalyzes the synthesis of complementary minus strand RNA and genomic plus strand RNA. Identification of potential key agents for targeting RNA-dependent RNA polymerase of SARS-CoV-2 by integrated analysis and virtual drug screening
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
RNA-dependent RNA polymerase is a key enzyme which regulates the viral replication of SARS-CoV-2
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
the enzyme plas a key role in the replication of SARS-CoV-2
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
the enzyme plays a crucial role in SARS-CoV-2 replication
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
the nsp12 (RdRp) is a central component of SARS-CoV-2 replication/transcription machinery. It catalyzes the synthesis of a complementary RNA strand using the virus RNA template with the assistance of nsp7 and nsp8 as cofactors
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
cryo-EM structures of the SARS-CoV-2 RNA polymerase in complexes with RNA, before and after RNA translocation, reveals structural rearrangements that the RNA-dependent RNA polymerase (RdRp) nsp12 and its co-factors (nsp7 and nsp8) undergo to accommodate nucleic acid binding
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
SARS-CoV-2 core polymerase complex has less efficient activity for RNA synthesis and lower thermostability of individual subunits compared with SARSCoV
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme synthesizes single-stranded RNA transcripts of one polarity which are identical in size to the denatured parental double-stranded RNA segments
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
nsP4 possesses the RNA-dependent RNA polymerase activity required for the replication of the SIN genome and transcription of a subgenomic mRNA during infection
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
in the absence of other viral proteins nsP4 is capable of copying SIN plus- and minus-strand templates, but does not transcribe subgenomic RNA. Mutations in the 3' conserved sequence element and poly(A) tail of the plus-strand template prevent nsP4-mediated de novo initiation of minus-strand RNA synthesis. nsP4-dependent terminal addition of nucleotides occurs on template RNA possessing certain mutations in the 3' conserved sequence element and polyadenylate tail. nsP4 is capable of minus-strand synthesis independent of the sequence at the 5' end of the template. An A-U rich sequence in the 3' conserved sequence element represents a binding site for a replicase component. Probably nsP4 plus-strand genomic RNA synthesis is dependent on the 3' end of the minus-strand template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme catalyzes in vitro the transcription of short single-stranded RNA and DNA molecules into precise complementary RNA copies up to the full length of these templates. The transcription of RNA-oligonicleotide templates and DNA-oligonucleotide templates is equally effective. Differences in transcription efficiency are found to depend on nucleotide sequence rather than on the RNA or DNA nature of the single-stranded nucleic acid. Double-stranded nucleic acids such as poly(A)*poly(U) and a double-stranded DNA 14-mer are not transcribed. The RdRP-directed transcription can be primed. The unprimed transcription starts preferentially at the 3'-terminal nucleotide of the template. The enzyme is capable of adding a single noncomplementary nucleotide to the 3'-terminus of about 50% of the runoff transcripts. AMP is preferred over GMP whereas CMP and UMP are terminally added at very low frequency
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
key step in the reproduction of plus-stranded RNA viruses pathogens is replication of their single-stranded RNA genomes occuring in the cytosol of host cells in association with membranes and requiring a virally-encoded RNA-dependent RNA polymerase
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme is able to synthesize or finish full-length TNV-RNA on an endogenous template, the minus strand of TNV-RNA
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
both 5'- and 3'-terminal regions of the (+)-strand RNA template including the wild type cyclization motifs are important for RNA synthesis. However, the 3'-terminal region of the (-)-strand RNA template alone is sufficient for RNA synthesis. The (+)-strand 5'-cyclization motif is critical for (-)-strand RNA synthesis but neither the (-)-strand 5'- nor 3'-cyclization motif is important for the (+)-strand RNA synthesis. Cyclization of the viral RNA play a role for (-)-strand RNA synthesis but not for (+)-strand RNA synthesis
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
DNA can serve as a template for ZIKV NS5 with an efficiency similar to that of an RNA template. The enzyme (NS5) can utilize single-stranded DNA but not double-stranded DNA as a template or a primer to synthesize RNA. Both full-length NS5 and a truncated NS5 containing the polymerase domain can carry out in vitro RNA-dependent RNA synthesis
-
-
?
remdesivir triphosphate + RNAn
diphosphate + RNAn 3'-remdesivir
-
-
-
ir
remdesivir triphosphate + RNAn
diphosphate + RNAn 3'-remdesivir
-
-
-
ir
remdesivir triphosphate + RNAn
diphosphate + RNAn 3'-remdesivir
-
-
-
ir
remdesivir triphosphate + RNAn
diphosphate + RNAn 3'-remdesivir
-
-
-
ir
UTP + RNAn
diphosphate + RNAn+1
RNA template with the first 25 nucleotides from the TrC (Trailer complement) sequence
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
?
UTP + RNAn
diphosphate + RNAn+1
-
-
-
ir
additional information
?
-
-
the central polymerase domain (PD) shows nucleotide binding properties, but neither the N-terminal domain (NTD) nor the C-terminal domain (CTD). Isolated PD does not exhibit RdRp activity but this activity can be reconstituted when all three domains are included in the reaction mixture. Molecular dynamics simulation suggests that the isolated PD has increased internal motions in comparison to when it is associated with the NTD and CTD. The motions of the separated PD may lead to the formation of a less accessible RNA template-binding channel and, thus, impair RdRp activity
-
-
?
additional information
?
-
-
introns called mirtrons and sirtrons might serve as the single-stranded RNA precursors for the generation of microRNA and small interfering RNA (siRNA), respectively, through an RDR (RNA-dependent RNA polymerase)-dependent pathway. sRNA high-throughput sequencing in wild-type and RDR-deficient mutant plants, overview
-
-
?
additional information
?
-
-
introns called mirtrons and sirtrons might serve as the single-stranded RNA precursors for the generation of microRNA and small interfering RNA (siRNA), respectively, through an RDR (RNA-dependent RNA polymerase)-dependent pathway. sRNA high-throughput sequencing in wild-type and RDR-deficient mutant plants, overview
-
-
?
additional information
?
-
-
the conservative lysine residue K369 in motif D is a dynamic element whose position inside the polymerase molecule may determine the velocity of the enzymatic reaction
-
-
?
additional information
?
-
-
systemic necrotic spotting induced by ORMV in tobacco maps to the RdRp polymerase domain, comparison of necrotic lesions of wild-type and chimeric mutant virusses
-
-
?
additional information
?
-
Cystovirus phi6
-
construction of a Coxsackie virus B3-specific GFP siRNA pool
-
-
?
additional information
?
-
Cystovirus phi6
-
In silico template RNA modelling, overview
-
-
?
additional information
?
-
-
NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
-
-
?
additional information
?
-
-
formation of an RNA-RNA complex between the 5' and 3' terminal nucleotides of the viral genome is necessary for polymerase activity, template specificity for a flavivirus RdRp, analysis and mechanism, overview. Viral protein NS5 has the ability to bind RNA with high affinity
-
-
?
additional information
?
-
-
NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
-
-
?
additional information
?
-
-
formation of an RNA-RNA complex between the 5' and 3' terminal nucleotides of the viral genome is necessary for polymerase activity, template specificity for a flavivirus RdRp, analysis and mechanism, overview. Viral protein NS5 has the ability to bind RNA with high affinity
-
-
?
additional information
?
-
-
D-elp1, corresponding to the largest of the three subunits in the RNA polymerase II core elongator complex, has RNA-dependent RNA polymerase activity. RdRP activity is associated with the amino terminal 96-kD fragment, DELTAC, CDS 1-2528. D-elp1 is a noncanonical RdRP that can synthesize dsRNA from different ssRNA templates using either a primer-dependent or primer-independent initiation mechanism, overview. D-elp1 associates tightly with Dcr-2
-
-
?
additional information
?
-
cytoplasmic viral RNA-dependent RNA polymerase disrupts the intracellular splicing machinery by entering the nucleus and interfering with pre-mRNA processing factor 8, Prp8. Identification of potential protein targets of EV71 3Dpol by MALDI-TOF MS analysis, overview
-
-
?
additional information
?
-
interaction of EV71 3Dpol and the nuclear protein U5 snRNPs. ENzyme 3Dpol enters the cellular nucleus and colocalizes with pre-mRNA processing factor 8, Prp8, 3Dpol associates with the C-terminal domain of Prp8 containing the Jab1/MPN region. RIP-seq of the pre-mRNA are trapped by the Prp8-3Dpol complexes
-
-
?
additional information
?
-
-
viral RdRP elongation nucleotide addition cycle (NAC), structure-function analysis, overview
-
-
?
additional information
?
-
cytoplasmic viral RNA-dependent RNA polymerase disrupts the intracellular splicing machinery by entering the nucleus and interfering with pre-mRNA processing factor 8, Prp8. Identification of potential protein targets of EV71 3Dpol by MALDI-TOF MS analysis, overview
-
-
?
additional information
?
-
interaction of EV71 3Dpol and the nuclear protein U5 snRNPs. ENzyme 3Dpol enters the cellular nucleus and colocalizes with pre-mRNA processing factor 8, Prp8, 3Dpol associates with the C-terminal domain of Prp8 containing the Jab1/MPN region. RIP-seq of the pre-mRNA are trapped by the Prp8-3Dpol complexes
-
-
?
additional information
?
-
-
the conservative lysine residue K359 in motif D is a dynamic element whose position inside the polymerase molecule may determine the velocity of the enzymatic reaction
-
-
?
additional information
?
-
-
in vitro, protein nsp9 of equine arteritis virus shows weak de novo polymerase activity on homopolymeric RNA templates. The RNA-synthesizing activities observed in de novo and primer-dependent polymerase and terminal transferase assays cannot be attributed to recombinant EAV nsp9-RdRp. The polymerase assay employing 32P-labeled NTPs is sensitive enough to detect the activity of trace amounts of contaminating T7 RNA polymerase. This polymerase is also able to act on templates lacking the established T7 promoter requirements
-
-
?
additional information
?
-
-
enzyme-host membrane interactions are an initial step of FHV RNA replication complex assembly, overview
-
-
?
additional information
?
-
-
the enzyme translates in vitro rapidly. It specifically associates with mitochondria isolated from yeast, insect, and mammalian cells, temperature-dependently but independent of protease-sensitive mitochondrial outer membrane components or the host mitochondrial import machinery. The enzyme preferentially binds to specific anionic phospholipids, in particular the mitochondrion-specific phospholipid cardiolipin
-
-
?
additional information
?
-
-
the initiation of FMDV RNA synthesis is strongly inhibited by 5-fluorouridine triphosphate, and it is also an inhibitor of FMDV RNA elongation, overview
-
-
?
additional information
?
-
-
the conservative lysine residue K369 in motif D is a dynamic element whose position inside the polymerase molecule may determine the velocity of the enzymatic reaction
-
-
?
additional information
?
-
-
the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
-
-
?
additional information
?
-
-
the viral enzyme binds to its coding region RNA stem-loop structure, 5BSL3.2, and its negative strand, enzyme and RNA interaction is an important step in viral RNA replication, overview
-
-
?
additional information
?
-
-
presence of motif G is important for primer-dependent RNA synthesis but not to affect the binding of the enzyme to the template
-
-
?
additional information
?
-
-
the viral enzyme binds to its coding region RNA stem-loop structure, 5BSL3.2, and its negative strand, enzyme and RNA interaction is an important step in viral RNA replication, overview
-
-
?
additional information
?
-
-
RNA polymerase II (PolII) acts as an RNA-dependent RNA polymerase to extend and destabilize a non-coding RNA. Pol II extends B2 RNA by 18 nt on its 3'-end in an internally templated reaction. The RNA product resulting from extension of B2 RNA by the Pol II RdRP can be removed from Pol II by a factor present in nuclear extracts
-
-
?
additional information
?
-
-
the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
-
-
?
additional information
?
-
-
the RNA polymerase complex consists of three subunits, PB1, PB2, and PA. These polymerase subunits and nucleoprotein, together with the viral RNA, form the viral ribonucleoprotein complex, which is the minimum component for viral RNA replication and transcription
-
-
?
additional information
?
-
-
the heterotrimeric complex of PB1, PB2 and PA subunits cooperate in the transcription and replication of the viral genome, the N-terminal region of the PA subunit of two recent H5N1 strains can influence promoter binding and RNA polymerase activity as well as virulence of the strains, overview
-
-
?
additional information
?
-
the polymerase protein also harbors an intrinsic RNA and DNA endonuclease activity that cleaves host mRNAs during cap-snatching, inhibited by 2,4-dioxo-4-phenylbutanoic and activated by Mn2+, with the amino-terminal 209 residues of the PA subunit containing the endonuclease active site, structure-function analysis, overview
-
-
?
additional information
?
-
-
the RdRp catalyzes all the biochemical reactions of influenza virus transcription and replication in vitro, dinucleotide ApG and globin mRNA-primed transcription, de novo initiation/replication, and polyadenylation
-
-
?
additional information
?
-
the polymerase protein also harbors an intrinsic RNA and DNA endonuclease activity that cleaves host mRNAs during cap-snatching, inhibited by 2,4-dioxo-4-phenylbutanoic and activated by Mn2+, with the amino-terminal 209 residues of the PA subunit containing the endonuclease active site, structure-function analysis, overview
-
-
?
additional information
?
-
-
NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
-
-
?
additional information
?
-
-
formation of an RNA-RNA complex between the 5' and 3' terminal nucleotides of the viral genome is necessary for polymerase activity, template specificity for a flavivirus RdRp, analysis and mechanism, overview. Viral protein NS5 has the ability to bind RNA with high affinity
-
-
?
additional information
?
-
flaviviral RNA-dependent RNA polymerases initiate replication of the single-stranded RNA genome in the absence of a primer. The template sequence 5'-CU-3' at the 3'-end of the flaviviral genome is highly conserved. Flaviviral RdRps require high concentrations of the second incoming nucleotide GTP to catalyze de novo template-dependent RNA synthesis. the conserved motif F of jRdRp occupies multiple conformations in absence of GTP. Motif F becomes ordered on GTP binding and occludes the nucleotide triphosphate entry tunnel
-
-
?
additional information
?
-
-
flaviviral RNA-dependent RNA polymerases initiate replication of the single-stranded RNA genome in the absence of a primer. The template sequence 5'-CU-3' at the 3'-end of the flaviviral genome is highly conserved. Flaviviral RdRps require high concentrations of the second incoming nucleotide GTP to catalyze de novo template-dependent RNA synthesis. the conserved motif F of jRdRp occupies multiple conformations in absence of GTP. Motif F becomes ordered on GTP binding and occludes the nucleotide triphosphate entry tunnel
-
-
?
additional information
?
-
ATP and GTP enzyme binding structures, detailed overview. The triphosphate moiety of GTP interacts with the side chains of basic residues from motif F (R460, K463, K471 and R474) and from motif E (R734 and R742)
-
-
?
additional information
?
-
-
ATP and GTP enzyme binding structures, detailed overview. The triphosphate moiety of GTP interacts with the side chains of basic residues from motif F (R460, K463, K471 and R474) and from motif E (R734 and R742)
-
-
?
additional information
?
-
-
NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
-
-
?
additional information
?
-
-
formation of an RNA-RNA complex between the 5' and 3' terminal nucleotides of the viral genome is necessary for polymerase activity, template specificity for a flavivirus RdRp, analysis and mechanism, overview. Viral protein NS5 has the ability to bind RNA with high affinity
-
-
?
additional information
?
-
flaviviral RNA-dependent RNA polymerases initiate replication of the single-stranded RNA genome in the absence of a primer. The template sequence 5'-CU-3' at the 3'-end of the flaviviral genome is highly conserved. Flaviviral RdRps require high concentrations of the second incoming nucleotide GTP to catalyze de novo template-dependent RNA synthesis. the conserved motif F of jRdRp occupies multiple conformations in absence of GTP. Motif F becomes ordered on GTP binding and occludes the nucleotide triphosphate entry tunnel
-
-
?
additional information
?
-
ATP and GTP enzyme binding structures, detailed overview. The triphosphate moiety of GTP interacts with the side chains of basic residues from motif F (R460, K463, K471 and R474) and from motif E (R734 and R742)
-
-
?
additional information
?
-
-
the RNA-dependent RNA polymerase of arenaviruses is an integral part of the L protein, a 200-kDa multifunctional and multidomain protein, structure and function of the Lassa virus RdRp domain, folding model of thedomain, overview
-
-
?
additional information
?
-
-
residues K1127, R1134, E1135, L1136, D1140, and K1144, D1193, G1298, S1333, D1334, D1335, and K1376 from different subunits might be involved in catalysis
-
-
?
additional information
?
-
-
the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
-
-
?
additional information
?
-
-
the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
-
-
?
additional information
?
-
-
the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
-
-
?
additional information
?
-
-
pseudogene-derived antisense siRNAs can be produced in specific rice developmental stages or physiological growth conditions, suggesting their potentially important roles in normal rice development involving RDR2, or small RNAs from rice pseudogenes might also function as natural antisense siRNAs either by interacting with the complementary sense RNAs from functional parental genes or by forming double-strand RNAs with transcripts of adjacent paralogous pseudogenes, function classification of rice pseudogenes, overview
-
-
?
additional information
?
-
-
Potato spindle tuber viroid replication in the nucleoplasm generates (-)-PSTVd intermediates and (+)-PSTVd copies. The Nicotiana benthamiana canonical 9-zinc finger (ZF) transcription factor IIIA (TFIIIA-9ZF) as well as its variant TFIIIA-7ZF both interact with (+)-PSTVd, but only TFIIIA-7ZF interacts with (-)-PSTVd. TFIIIA-7ZF is found in the nucleoplasm and nucleolus, in contrast to the strictly nucleolar localization of TFIIIA-9ZF. The DNA-dependent RNA polymerase II interacts with the (+)- and (2)-PSTVd RNA in vivo
-
-
?
additional information
?
-
template ssRNA accesses the active site through a tunnel. The phi12 P2 conformation does not favor RNA binding
-
-
?
additional information
?
-
RHDV polyprotein cleavage product p58 is an active RNA-dependent RNA polymerase, that has no DNA-dependent RNA polymerase activity
-
-
?
additional information
?
-
-
RHDV polyprotein cleavage product p58 is an active RNA-dependent RNA polymerase, that has no DNA-dependent RNA polymerase activity
-
-
?
additional information
?
-
RHDV polyprotein cleavage product p58 is an active RNA-dependent RNA polymerase, that has no DNA-dependent RNA polymerase activity
-
-
?
additional information
?
-
-
the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
-
-
?
additional information
?
-
-
the C-terminal fragment can interact with the viral nucleocapsid protein, the N-terminal 50 amino acids of nucleocapsid protein are responsible for the NP-RdRp interaction
-
-
?
additional information
?
-
-
NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
-
-
?
additional information
?
-
-
formation of an RNA-RNA complex between the 5' and 3' terminal nucleotides of the viral genome is necessary for polymerase activity, template specificity for a flavivirus RdRp, analysis and mechanism, overview. Viral protein NS5 has the ability to bind RNA with high affinity
-
-
?
additional information
?
-
-
NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
-
-
?
additional information
?
-
-
formation of an RNA-RNA complex between the 5' and 3' terminal nucleotides of the viral genome is necessary for polymerase activity, template specificity for a flavivirus RdRp, analysis and mechanism, overview. Viral protein NS5 has the ability to bind RNA with high affinity
-
-
?
additional information
?
-
enzyme shows both primer-dependent and primer-independent RNA synthesis activities using homopolymeric RNA templates. It preferentially copies homopolymeric pyrimidine RNA templates in the absence of an added oligonucleotide primer and is also able to initiate de novo RNA synthesis from the 3'-ends of both the plus- and minus-strand genome of human SARS coronavirus, using the 3'-terminal 36- and 37-nt RNA, respectively
-
-
?
additional information
?
-
-
enzyme shows both primer-dependent and primer-independent RNA synthesis activities using homopolymeric RNA templates. It preferentially copies homopolymeric pyrimidine RNA templates in the absence of an added oligonucleotide primer and is also able to initiate de novo RNA synthesis from the 3'-ends of both the plus- and minus-strand genome of human SARS coronavirus, using the 3'-terminal 36- and 37-nt RNA, respectively
-
-
?
additional information
?
-
-
comparison of necrotic lesions of wild-type and chimeric mutant virusses
-
-
?
additional information
?
-
-
The single-stranded RNA genomes of the plus-stranded RNA viruses serve as templates for translation of viral proteins and perform other essential functions that generally involve local RNA structures, such as RNA hairpins. Viral RNA replication also requires a long-range RNA-RNA interaction
-
-
?
additional information
?
-
NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
-
-
?
additional information
?
-
formation of an RNA-RNA complex between the 5' and 3' terminal nucleotides of the viral genome is necessary for polymerase activity, template specificity for a flavivirus RdRp, analysis and mechanism, overview. Viral protein NS5 has the ability to bind RNA with high affinity
-
-
?
additional information
?
-
NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
-
-
?
additional information
?
-
formation of an RNA-RNA complex between the 5' and 3' terminal nucleotides of the viral genome is necessary for polymerase activity, template specificity for a flavivirus RdRp, analysis and mechanism, overview. Viral protein NS5 has the ability to bind RNA with high affinity
-
-
?
additional information
?
-
-
NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
-
-
?
additional information
?
-
-
formation of an RNA-RNA complex between the 5' and 3' terminal nucleotides of the viral genome is necessary for polymerase activity, template specificity for a flavivirus RdRp, analysis and mechanism, overview. Viral protein NS5 has the ability to bind RNA with high affinity
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme should be involved in the replication of BaMV
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
Cystovirus phi6
-
template is RNA, the phi6 polymerase is highly processive and can use either single- or double-stranded RNA as a template and synthesizes a full-length complementary strand of an RNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
inducible enzyme
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
replication of Hepatitits C virus is thought to proceed via the initial synthesis of a complementary (-)RNA strand, which serves, in turn, as a template for the production of progeny (+)-strand RNA molecules. An RNA-dependent RNA polymerase is postulated to be involved in these steps
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
essential catalytic enzyme for HCV replication. NS5A binds RNA-dependent RNA polymerase and modulates RNA-dependent RNA polymerase activity
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
NS5B RdRp is essential for viral replication
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
B2 RNA is a substrate for RNA dependent RNA polymerization by Pol II
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
JEV NS5 protein can initiate RNA synthesis through a de novo initiation mechanism. JEV NS5 protein is more efficient in using negative-strand RNA templates, indicating that the JEV NS5 protein is involved in regulating the ratio of positive strand RNA to negative strand RNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
JEV NS5 protein can initiate RNA synthesis through a de novo initiation mechanism. JEV NS5 protein is more efficient in using negative-strand RNA templates, indicating that the JEV NS5 protein is involved in regulating the ratio of positive strand RNA to negative strand RNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
La France isometric virus
-
the enzyme is probably a transcriptase engaged in the synthesis of ssRNA transcripts corresponding to each of the virion-associated dsRNAs
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
the enzyme catalyzes cap methylation of virus-specific mRNA as well as RNA synthesis
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
composed of one phage-coded polypeptide and three host-supplied polypeptides which function in the biosynthesis of proteins in the uninfected host. Two of theses polypeptides, protein elongation factors EF-Tu and EF-Ts, are required for initiation of transcription by replicase with all templates
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
Qbeta replicase is an RNA-dependent RNA polymerase responsible for replicating the RNA genome of coliphage Qbeta and plays a key role in the life cycle of the Qbeta phage
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
the enzyme (RdRP) is essential for both transcription and replication of the viral RNA genome
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
required for replication of the HRV RNA genome
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
key enzyme of replication
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
essential enzyme for viral RNA replication
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
key enzyme responsible for the SARS-CoV-2 replication process, catalyzes the synthesis of complementary minus strand RNA and genomic plus strand RNA. Identification of potential key agents for targeting RNA-dependent RNA polymerase of SARS-CoV-2 by integrated analysis and virtual drug screening
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
RNA-dependent RNA polymerase is a key enzyme which regulates the viral replication of SARS-CoV-2
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
the enzyme plas a key role in the replication of SARS-CoV-2
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
the enzyme plays a crucial role in SARS-CoV-2 replication
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
the nsp12 (RdRp) is a central component of SARS-CoV-2 replication/transcription machinery. It catalyzes the synthesis of a complementary RNA strand using the virus RNA template with the assistance of nsp7 and nsp8 as cofactors
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
nsP4 possesses the RNA-dependent RNA polymerase activity required for the replication of the SIN genome and transcription of a subgenomic mRNA during infection
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
-
key step in the reproduction of plus-stranded RNA viruses pathogens is replication of their single-stranded RNA genomes occuring in the cytosol of host cells in association with membranes and requiring a virally-encoded RNA-dependent RNA polymerase
-
-
?
additional information
?
-
-
systemic necrotic spotting induced by ORMV in tobacco maps to the RdRp polymerase domain, comparison of necrotic lesions of wild-type and chimeric mutant virusses
-
-
?
additional information
?
-
-
NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
-
-
?
additional information
?
-
-
NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
-
-
?
additional information
?
-
-
D-elp1, corresponding to the largest of the three subunits in the RNA polymerase II core elongator complex, has RNA-dependent RNA polymerase activity. RdRP activity is associated with the amino terminal 96-kD fragment, DELTAC, CDS 1-2528. D-elp1 is a noncanonical RdRP that can synthesize dsRNA from different ssRNA templates using either a primer-dependent or primer-independent initiation mechanism, overview. D-elp1 associates tightly with Dcr-2
-
-
?
additional information
?
-
cytoplasmic viral RNA-dependent RNA polymerase disrupts the intracellular splicing machinery by entering the nucleus and interfering with pre-mRNA processing factor 8, Prp8. Identification of potential protein targets of EV71 3Dpol by MALDI-TOF MS analysis, overview
-
-
?
additional information
?
-
cytoplasmic viral RNA-dependent RNA polymerase disrupts the intracellular splicing machinery by entering the nucleus and interfering with pre-mRNA processing factor 8, Prp8. Identification of potential protein targets of EV71 3Dpol by MALDI-TOF MS analysis, overview
-
-
?
additional information
?
-
-
enzyme-host membrane interactions are an initial step of FHV RNA replication complex assembly, overview
-
-
?
additional information
?
-
-
the initiation of FMDV RNA synthesis is strongly inhibited by 5-fluorouridine triphosphate, and it is also an inhibitor of FMDV RNA elongation, overview
-
-
?
additional information
?
-
-
the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
-
-
?
additional information
?
-
-
RNA polymerase II (PolII) acts as an RNA-dependent RNA polymerase to extend and destabilize a non-coding RNA. Pol II extends B2 RNA by 18 nt on its 3'-end in an internally templated reaction. The RNA product resulting from extension of B2 RNA by the Pol II RdRP can be removed from Pol II by a factor present in nuclear extracts
-
-
?
additional information
?
-
-
the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
-
-
?
additional information
?
-
-
the RNA polymerase complex consists of three subunits, PB1, PB2, and PA. These polymerase subunits and nucleoprotein, together with the viral RNA, form the viral ribonucleoprotein complex, which is the minimum component for viral RNA replication and transcription
-
-
?
additional information
?
-
-
NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
-
-
?
additional information
?
-
flaviviral RNA-dependent RNA polymerases initiate replication of the single-stranded RNA genome in the absence of a primer. The template sequence 5'-CU-3' at the 3'-end of the flaviviral genome is highly conserved. Flaviviral RdRps require high concentrations of the second incoming nucleotide GTP to catalyze de novo template-dependent RNA synthesis. the conserved motif F of jRdRp occupies multiple conformations in absence of GTP. Motif F becomes ordered on GTP binding and occludes the nucleotide triphosphate entry tunnel
-
-
?
additional information
?
-
-
flaviviral RNA-dependent RNA polymerases initiate replication of the single-stranded RNA genome in the absence of a primer. The template sequence 5'-CU-3' at the 3'-end of the flaviviral genome is highly conserved. Flaviviral RdRps require high concentrations of the second incoming nucleotide GTP to catalyze de novo template-dependent RNA synthesis. the conserved motif F of jRdRp occupies multiple conformations in absence of GTP. Motif F becomes ordered on GTP binding and occludes the nucleotide triphosphate entry tunnel
-
-
?
additional information
?
-
-
NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
-
-
?
additional information
?
-
flaviviral RNA-dependent RNA polymerases initiate replication of the single-stranded RNA genome in the absence of a primer. The template sequence 5'-CU-3' at the 3'-end of the flaviviral genome is highly conserved. Flaviviral RdRps require high concentrations of the second incoming nucleotide GTP to catalyze de novo template-dependent RNA synthesis. the conserved motif F of jRdRp occupies multiple conformations in absence of GTP. Motif F becomes ordered on GTP binding and occludes the nucleotide triphosphate entry tunnel
-
-
?
additional information
?
-
-
the RNA-dependent RNA polymerase of arenaviruses is an integral part of the L protein, a 200-kDa multifunctional and multidomain protein, structure and function of the Lassa virus RdRp domain, folding model of thedomain, overview
-
-
?
additional information
?
-
-
the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
-
-
?
additional information
?
-
-
the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
-
-
?
additional information
?
-
-
the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
-
-
?
additional information
?
-
-
pseudogene-derived antisense siRNAs can be produced in specific rice developmental stages or physiological growth conditions, suggesting their potentially important roles in normal rice development involving RDR2, or small RNAs from rice pseudogenes might also function as natural antisense siRNAs either by interacting with the complementary sense RNAs from functional parental genes or by forming double-strand RNAs with transcripts of adjacent paralogous pseudogenes, function classification of rice pseudogenes, overview
-
-
?
additional information
?
-
-
Potato spindle tuber viroid replication in the nucleoplasm generates (-)-PSTVd intermediates and (+)-PSTVd copies. The Nicotiana benthamiana canonical 9-zinc finger (ZF) transcription factor IIIA (TFIIIA-9ZF) as well as its variant TFIIIA-7ZF both interact with (+)-PSTVd, but only TFIIIA-7ZF interacts with (-)-PSTVd. TFIIIA-7ZF is found in the nucleoplasm and nucleolus, in contrast to the strictly nucleolar localization of TFIIIA-9ZF. The DNA-dependent RNA polymerase II interacts with the (+)- and (2)-PSTVd RNA in vivo
-
-
?
additional information
?
-
RHDV polyprotein cleavage product p58 is an active RNA-dependent RNA polymerase, that has no DNA-dependent RNA polymerase activity
-
-
?
additional information
?
-
-
RHDV polyprotein cleavage product p58 is an active RNA-dependent RNA polymerase, that has no DNA-dependent RNA polymerase activity
-
-
?
additional information
?
-
RHDV polyprotein cleavage product p58 is an active RNA-dependent RNA polymerase, that has no DNA-dependent RNA polymerase activity
-
-
?
additional information
?
-
-
the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
-
-
?
additional information
?
-
-
the C-terminal fragment can interact with the viral nucleocapsid protein, the N-terminal 50 amino acids of nucleocapsid protein are responsible for the NP-RdRp interaction
-
-
?
additional information
?
-
-
NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
-
-
?
additional information
?
-
-
NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
-
-
?
additional information
?
-
-
comparison of necrotic lesions of wild-type and chimeric mutant virusses
-
-
?
additional information
?
-
-
The single-stranded RNA genomes of the plus-stranded RNA viruses serve as templates for translation of viral proteins and perform other essential functions that generally involve local RNA structures, such as RNA hairpins. Viral RNA replication also requires a long-range RNA-RNA interaction
-
-
?
additional information
?
-
NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
-
-
?
additional information
?
-
NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
-
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additional information
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NS5 is the largest and the most conserved of the flavivirus proteins. It contains an N-terminal methyl transferase domain and a C-terminal RdRp domain. The main enzymatic activity observed in extracts of infected cells with endogenous templates is the elongation of already initiated RNA synthesis
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
GTP
GTP is crucial for the formation of the initiation complex during RNA replication. The 3D structure of the RdRp (RNA-dependent RNA polymerase) of SARS-CoV2 is modelled its probable GTP binding pocket in the active site is predicted
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
divalent cation required, Ca2+ shows about 20% of the activity with Mg2+ at about 1 mM
K+
Mg2+
Mn2+
NaCl
NH4Cl
-
activity is increased by a factor of about 1.2-1.5 when the final salt concentration is raised to 60 mM by the addition of NaCl, KCl or NH4Cl
Zn2+
additional information
K+
-
K+ exhibits a stimulatory effect at 25 mM, while the stimulatory effect decreases when the concentration of K+ is higher than 25 mM
K+
-
KCl, activity is increased by a factor of about 1.2-1.5 when the final salt concentration is raised to 60 mM by the addition of NaCl, KCl or NH4Cl
Mg2+
Cystovirus phi6
activation of the RNA/polymerase complex by the addition of substrate and Mg2+ initiates a single round of reaction within the crystal to form a dead-end complex that partially collapses within the enzyme active site
Mg2+
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and Mn2+, both required. Maximum activity in presence of 5.0 mM Mg2+ and 1.0-2.0 mM Mn2+
Mg2+
-
kinetic mechanism for single nucleotide incorporation catalyzed by poliovirus polymerase in presence of Mg2+
Mg2+
-
using Mg2+ as the divalent cation cofactor, the enzyme can use both the first conformational-change step and the phosphoryl-transfer step to distinguish between correct and incorrect nucleotides
Mg2+
Foxtail mosaic potexvirus
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the enzyme is strictly dependent on presence of Mg2+, optimal activity in presence of 5 mM MgCl2
Mg2+
the enzyme requires either Mn2+ or Mg2+ for RNA-dependent RNA polymerase activity. NS5B undergoes conformational changes upon the binding of metal ions. This process does not significantly stimulate the binding to the RNA or NTP substrates
Mg2+
-
absolute requirement for divalent cation, effective concentration range is 5-10 mM
Mg2+
-
the enzyme directs incoming nucleotides to its active site through Mg2+-dependent dynamics within its F motif. Mg2+-bound nucleotide first binds next to the tunnel entry of the RNA-dependent RNA polymerase(RdRp)-specific entry tunnel. Interactions with the triphosphate moiety orient the nucleotide such that its base moiety enters first. Dynamics of RdRp motifs F1 + F3 then allow the nucleotide to interrogate the RNA template base prior to nucleotide insertion into the active site. These dynamics are finely regulated by a second magnesium dication, thus coordinating the entry of a magnesium-bound nucleotide with shuttling of the second magnesium necessary for the two-metal ion catalysis
Mg2+
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activates optimally at 8 mM, recombinant viral enzyme purified from insect cells
Mg2+
-
dependent on divalent cations, Mn2+ is 20times more effective than Mg2+ at optimal concentration (3 mM)
Mg2+
-
Mg2+ is 20 times less effective than Mn2+ in coordinating the catalytic reaction of RdRp
Mg2+
-
in presence of Mg2+ significant activity is observed when poly(A) or poly(C) is used as template and the activity is template and primer-dependent. Poly(G) and poly(U) templates are not efficient substrates. Biotinylated oligoDNA primers appear to work slightly more efficiently than oligoRNA primers. Divalent cation required, optimal concentration for Mg2+ is 1 mM
Mg2+
-
over a concentration range from 0.5 to 5 mM, sapovirus 3Dpol displays a clear preference for Mn2+ over Mg2+
Mg2+
-
the activity of the enzyme bound to membrane of infected Nicotiana tabacum is sharply increased with Mg2+ up to 10 mM and then levels off up to 50 mM
Mn2+
-
optimum concentration at 0.1 mM, RdRp is twice as active at the Mn2+ concentration optimum compared to that of Mg2+
Mn2+
-
and Mg2+, both required. Maximum activity in presence of 5.0 mM Mg2+ and 1.0-2.0 mM Mn2+
Mn2+
-
stimulates to a higher extent than Mg2+, poly(rU) polymerase activity using dT15/rA30
Mn2+
-
using Mn2+ as the cofactor, the ability to diminish the rate of phosphoryl transfer for incorrect nucleotides relative to correct nucleotides is lost completely, leaving only the conformational-change step for selection of the correct nucleotide
Mn2+
the enzyme requires either Mn2+ or Mg2+ for RNA-dependent RNA polymerase activity. NS5B undergoes conformational changes upon the binding of metal ions. This process does not significantly stimulate the binding to the RNA or NTP substrates
Mn2+
-
absolute requirement for divalent cation, effective concentration is about 1 mM
Mn2+
-
optimal polymerase activity at 0.25 mM MnCl2, activity is lower than in presence of MgCl2
Mn2+
-
likely helps to stabilize the interaction between the active site and the NTPi
Mn2+
-
dependent on divalent cations, Mn2+ is 20times more effective than Mg2+ at optimal concentration (3 mM)
Mn2+
-
Mn2+ is 20 times more effective than Mg2+ in coordinating the catalytic reaction of RdRp
Mn2+
required, GTP binding reduces the affinity of jRdRp for RNA in the absence of Mn2+, binding affinity of jRdRp toward RNA in the presence of GTP/ATP is restored when Mn2+ ion is included in the reaction buffer
Mn2+
-
Mn2+ might reduce the template specificity by forming a complex with GTP that is more efficiently incorporated than is Mg*GTP with unfavored template
Mn2+
-
in presence of Mn2+ activity is stimulates by 2.5-5.6fold. RNA synthesis using poly(C) as template becomes primer-independent, about 2.5fold stimulation at 1 mM
Mn2+
-
over a concentration range from 0.5 to 5 mM, sapovirus 3Dpol displays a clear preference for Mn2+ over Mg2+
Mn2+
-
0.05 mM, 40% of the activity compared to reaction with 3 mM Mg2+. 5.0 mM, 70% of the activity compared to the reaction with 3 mM Mg2+, Mn2+ is present as the sole divalent cation
NaCl
-
activity is increased by a factor of about 1.2-1.5 when the final salt concentration is raised to 60 mM by the addition of NaCl, KCl or NH4Cl
Zn2+
Q6DLV0
contains zinc, Zn2+ likely contributes to the structural stability of the region near motif E of the DENV 3 polymerase
Zn2+
the study models potential Zn2+ binding to study models potential Zn binding to the enzyme (RdRp) and the 3CLpro. The Zn binding site is conserved between severe acute respiratory syndrome (SARS)-coronavirus (CoV) and SARS-CoV-2. The location of these sites may influence the enzymatic activity of the enzyme in COVID-19
additional information
recombinant non-tagged RdRp does not require manganese ions to activate RNA polymerization
additional information
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recombinant non-tagged RdRp does not require manganese ions to activate RNA polymerization
additional information
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no detectable level of RdRp activity is observed in the presence of 0.5 to 10 mM Mg2+
additional information
-
computational study of metal-binding preferences. When he calculated metal hydration energies are used, the proteination energies for the structures indicate that the binding preference for the metal is Cu2+ > Mn2+, Fe2+ > Zn2+ > Ni2+ > Co2+ > Mg2+, Ca2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(1S)-1-(4-aminothieno[3,2-d]pyrimidin-7-yl)-1,4-anhydro-2-C-methyl-D-ribitol
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(2E)-3-(4-[[(1-[[(1-cyclohexyl-2-furan-3-yl-1H-benzimidazol-5-yl)carbonyl]amino]cyclobutyl)carbonyl]amino]phenyl)prop-2-enoic acid
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(2E)-3-(4-[[(2-cyclohexyl-3-phenylquinoxalin-6-yl)carbonyl]amino]phenyl)prop-2-enoic acid
-
(2E)-3-[4-([[1-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
-
(2E)-3-[4-([[1-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclopentyl]carbonyl]amino)phenyl]prop-2-enoic acid
-
(2E)-3-[4-([[1-([[2-cyclohexyl-3-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
-
(2E)-3-[4-([[1-([[3-cyclohexyl-2-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
-
(2E)-3-[4-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)phenyl]prop-2-enoic acid
-
(2E)-3-[4-([[2-cyclohexyl-3-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)phenyl]prop-2-enoic acid
-
(2E)-3-[4-([[3-cyclohexyl-2-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)phenyl]prop-2-enoic acid
-
(2R,3S,4R,5R)-5-(4-amino-2-oxopyrimidin-1(2H)-yl)-2-azido-2-[[(2-methylpropanoyl)oxy]methyl]tetrahydrofuran-3,4-diyl bis(2-methylpropanoate)
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(2R,3S,5S)-5-(methoxycarbonyl)-5-(2-methylpropyl)-2-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]pyrrolidine-3-carboxylic acid
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(2R,3S,5S)-5-[(aminooxy)carbonyl]-5-(2-methylpropyl)-2-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]pyrrolidine-3-carboxylic acid
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-
(2S)-(((5Z)-5-[(5-ethyl-2-furyl)methylene]-4-oxo-4,5-dihydro-1,3-thiazol-2-yl)amino)(4-fluorophenyl)acetic acid
-
-
(2S)-1-[(2-amino-4-chloro-5-methylphenyl)sulfonyl]pyrrolidine-2-carboxylic acid
-
-
(2S)-1-[(3,4,5-trichloro-2-hydroxyphenyl)sulfonyl]pyrrolidine-2-carboxylic acid
-
-
(2S)-1-[(3,5-dichloro-2-hydroxyphenyl)sulfonyl]pyrrolidine-2-carboxylic acid
-
-
(2S)-1-[[4-([[1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]carbonyl]amino)phenyl]sulfonyl]pyrrolidine-2-carboxylic acid
-
-
(2S,4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)pyrrolidine-2,4-dicarboxylic acid
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-
(2S,4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-5-thiophen-2-ylpyrrolidine-2,4-dicarboxylic acid
-
-
(2S,4S,5R)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-1-[[4-(trifluoromethyl)phenyl]carbonyl]pyrrolidine-2,4-dicarboxylic acid
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(2S,4S,5R)-2-(2-methylpropyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]pyrrolidine-2,4-dicarboxylic acid
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-
(2S,4S,5R)-2-isobutyl-4-(2-phenylacetyl)-5-(thiophen-2-yl)-1-(4-(trifluoromethyl)benzoyl)pyrrolidine-2-carboxylic acid
-
-
(2S,4S,5R)-2-isobutyl-5-(thiophen-2-yl)-1-(4-(trifluoromethyl)benzoyl)pyrrolidine-2,4-dicarboxylic acid
-
-
(2S,4S,5R)-4-acetyl-2-isobutyl-5-(thiophen-2-yl)-1-(4-(trifluoromethyl)benzoyl)pyrrolidine-2-carboxylic acid
-
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(2S,5R)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-2,5-dihydro-1H-pyrrole-2,4-dicarboxylic acid
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-
(2Z)-3-[4-([[1-([[2-cyclohexyl-3-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
-
(2Z)-3-[4-([[1-([[3-cyclohexyl-2-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
-
(4E)-1-(3,4-dimethylphenyl)-4-(hydroxyimino)pyrazolidine-3,5-dione
-
(4R,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(ethoxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
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(4R,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(hydroxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
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(4S,5R)-1-[(3-bromo-4-tert-butylphenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
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-
(4S,5R)-1-[(4-tert-butyl-3-chlorophenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
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(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(ethoxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
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(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(hydroxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
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(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(methoxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
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(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
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(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-methoxy-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
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(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-4-(phenylcarbamoyl)-5-(1,3-thiazol-2-yl)-L-proline
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(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-4-[[(2-phenylethoxy)sulfinyl]carbamoyl]-5-(1,3-thiazol-2-yl)-L-proline
-
-
(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-4-(methylcarbamoyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-thiophen-2-yl-L-proline
-
-
(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-4-[(methoxysulfinyl)carbamoyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
(4S,5R)-2-(2-methylpropyl)-4-(phenylcarbamoyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]-L-proline
-
-
(4S,5R)-2-(2-methylpropyl)-4-[(2-phenylethyl)carbamoyl]-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]-L-proline
-
-
(4S,5R)-2-(2-methylpropyl)-5-thiophen-2-yl-4-[[(trifluoromethoxy)sulfinyl]carbamoyl]-1-[[4-(trifluoromethyl)phenyl]carbonyl]-L-proline
-
-
(4S,5R)-4-(benzylcarbamoyl)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
(4S,5R)-4-(ethylcarbamoyl)-2-(2-methylpropyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]-L-proline
-
-
(4S,5R)-4-(methylcarbamoyl)-2-(2-methylpropyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]-L-proline
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-
(4S,5R)-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-1-[[4-(trifluoromethyl)phenyl]carbonyl]-L-proline
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-
(4S,5R)-4-carbamoyl-2-(2-methylpropyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]-L-proline
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(4S,5R)-4-[(1-methylethyl)carbamoyl]-2-(2-methylpropyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]-L-proline
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(4S,5R)-4-[(methoxysulfinyl)carbamoyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-1-[[4-(trifluoromethyl)phenyl]carbonyl]-L-proline
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(4S,5R)-4-[(methoxysulfinyl)carbamoyl]-2-(2-methylpropyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]-L-proline
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(4S,5R)-4-[[(benzyloxy)sulfinyl]carbamoyl]-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
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(5-cyano-6-fluoro-8-methyl-1-propyl-3,4-dihydro-1H-[1]benzothieno[2,3-c]pyran-1-yl)acetic acid
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(5-cyano-8-methyl-1-propyl-1,3,4,9-tetrahydropyrano[3,4-b]indol-1-yl)acetic acid
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(5-cyano-8-methyl-1-propyl-2,3,4,9-tetrahydro-1H-carbazol-1-yl)acetic acid
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(5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(methoxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
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(5S)-5-tert-butyl-3-(1,1-dioxido-4H-1,2,4-benzothiadiazin-3-yl)-4-hydroxy-1-(3-methylbutyl)-1,5-dihydro-2H-pyrrol-2-one
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(6R,7R,8S,9R)-4-bromo-7,8-dihydroxy-7,8,9,10-tetrahydro-5H,6H-6,9-epoxy-1,2,5a,10a-tetraazacycloocta[1,2,3-cd]inden-5-one
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([[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]oxy]methyl)phosphonic acid
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1,3-bis-(4-chloro-1H(3H)-triazolo[4,5-g]quinoline)propan-2-one
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moderate antiproliferative activity for the cell lines tested
1,3-dimethyl-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-1H-pyrazole-5-carboxamide
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1-(1-methylethyl)-N-[4-[(2-methylpiperidin-1-yl)sulfonyl]phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
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1-(2-cyclopropylethyl)-3-(1,1-dioxido-4H-1,2,4-benzothiadiazin-3-yl)-6-fluoro-4-hydroxyquinolin-2(1H)-one
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1-(cyclobutylamino)-3-(1,1-dioxido-4H-1,2,4-benzothiadiazin-3-yl)-4-hydroxyquinolin-2(1H)-one
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1-benzyl-N-(2,3-dimethylphenyl)-3,5-dimethyl-1H-pyrazole-4-carboxamide
NIC04, in combination with NIC02, i.e. N-(3-cyano-5,6-dihydro-4H-cyclopenta[b]thiophen-2-yl)-4-methyl-2-phenyl-1,3-thiazole-5-carboximidic acid
1-benzyl-N-[4-[(2-methylpiperidin-1-yl)sulfonyl]phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
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1-cyclohexyl-2-(2-fluoro-4-[[2-(3-oxomorpholin-4-yl)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
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1-cyclohexyl-2-(2-fluoro-4-[[2-(4-hydroxypiperidin-1-yl)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
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1-cyclohexyl-2-(2-fluoro-4-[[2-(4-methylpiperazin-1-yl)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-2-(2-fluoro-4-[[2-methoxy-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-2-(2-fluoro-4-[[2-morpholin-4-yl-5-(2-oxopiperidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-2-(2-fluoro-4-[[2-morpholin-4-yl-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
-
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1-cyclohexyl-2-(2-fluoro-4-[[5-(2-oxopyrrolidin-1-yl)-2-piperidin-1-ylbenzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
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1-cyclohexyl-2-(4-[[2-morpholin-4-yl-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-indole-5-carboxylic acid
-
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1-cyclohexyl-2-(4-[[4-(dimethylcarbamoyl)phenyl](phenyl)methoxy]-2-fluorophenyl)-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-2-(4-[[5-(1,1-dioxidoisothiazolidin-2-yl)-2-morpholin-4-ylbenzyl]oxy]-2-fluorophenyl)-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-2-(4-[[5-(dimethylcarbamoyl)-2-morpholin-4-ylbenzyl]oxy]-2-fluorophenyl)-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-2-furan-3-yl-N-[(1S)-2-(5-hydroxy-1H-indol-3-yl)-1-(1,3-thiazol-4-yl)ethyl]-1H-benzimidazole-5-carboxamide
-
-
1-cyclohexyl-2-[2-fluoro-4-([5-[(1-methylethyl)carbamoyl]-2-morpholin-4-ylbenzyl]oxy)phenyl]-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-2-[2-fluoro-4-([5-[(methoxyacetyl)(methyl)amino]-2-morpholin-4-ylbenzyl]oxy)phenyl]-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-2-[2-fluoro-4-[(2-morpholin-4-ylbenzyl)oxy]phenyl]-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-N-[2-(3,4-dimethoxyphenyl)ethyl]-2-pyridin-2-yl-1H-benzimidazole-5-carboxamide
-
-
1-ethyl-N-[4-[(2-methylpiperidin-1-yl)sulfonyl]phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
-
1-methyl-3-(trifluoromethyl)-N-[4-(pyrrolidinylsulfonyl)-phenyl]-1H-pyrazole-5-carboxamide
-
specific inhibitor, inhibits RdRp complex activity
1-methyl-3-(trifluoromethyl)-N-[4-(pyrrolidinylsulfonyl)phenyl]-1H-pyrazole-5-carboxamide
-
-
1-methyl-3-(trifluoromethyl)-N-[4-pyrrolidinylsulfonylphenyl]-1H-pyrazole-5-carboxamide
-
-
1-methyl-4-(trifluoromethyl)-N-(4-[[4-(trifluoromethyl)piperidin-1-yl]sulfonyl]phenyl)-1H-pyrrole-2-carboxamide
-
-
1-methyl-5-[[4-(pyrrolidin-1-ylsulfonyl)phenoxy]methyl]-3-(trifluoromethyl)-1H-pyrazole
-
-
1-methyl-N-[4-(morpholin-4-ylsulfonyl)phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
-
1-methyl-N-[4-(morpholin-4-ylsulfonyl)phenyl]-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
1-methyl-N-[4-(piperazin-1-ylsulfonyl)phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
-
1-methyl-N-[4-(piperazin-1-ylsulfonyl)phenyl]-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
1-methyl-N-[4-(piperidin-1-ylsulfonyl)phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
-
1-methyl-N-[4-(piperidin-1-ylsulfonyl)phenyl]-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
1-methyl-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
first-in-class nonnucleoside inhibitor of RNA-dependent RNA polymerase complex activity, highly active against multiple primary isolates of diverse measles virus genotypes circulating worldwide, high developmental potential as a potent therapeutic against measles virus, active concentrations of 35-145 nM
1-methyl-N-[4-[(2-methylpiperidin-1-yl)sulfonyl]phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
-
1-methyl-N-[4-[(2-methylpiperidin-1-yl)sulfonyl]phenyl]-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
1-methyl-N-[4-[(4-methylpiperidin-1-yl)sulfonyl]phenyl]-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
1-phenyl-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
-
1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-[(2-chlorophenyl)carbamoyl]-2-(1,3-thiazol-4-ylmethyl)piperazine-2-carboxylic acid
-
-
1-[1-(2,5-difluorophenyl)-3-(3-trifluoromethylphenyl)-triazen-3-yl]-N,N-dimethyl-3-propanamine
1-[1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]-2-[4-(pyrrolidin-1-ylsulfonyl)phenyl]ethanol
-
-
1-[1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]-2-[4-(pyrrolidin-1-ylsulfonyl)phenyl]ethanone
-
-
1-[2-(diethylamino)ethyl]-6-(1H-imidazol-1-yl)-1,3-dihydro-2H-benzimidazol-2-one
-
1-[[4-([[1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]carbonyl]amino)phenyl]sulfonyl]piperidine-2-carboxylic acid
-
-
1-[[4-([[1-methyl-4-(trifluoromethyl)-1H-pyrrol-2-yl]carbonyl]amino)phenyl]sulfonyl]piperidine-3-carboxylic acid
-
-
1-[[4-([[1-methyl-4-(trifluoromethyl)-1H-pyrrol-2-yl]carbonyl]amino)phenyl]sulfonyl]proline
-
-
12-cyclohexylindolo[1,2-c][1,3]benzoxazine-9-carboxylic acid
-
dihedral angle between the C2-aryl group and the indole ring is 24°
13-cyclohexyl-3-[[2-morpholin-4-yl-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]-6,7-dihydroindolo[1,2-d][1,4]benzoxazepine-10-carboxylic acid
-
-
13-cyclohexyl-5-(2-piperidin-1-ylethyl)-6,7-dihydro-5H-indolo[1,2-d][1,4]benzodiazepine-10-carboxylic acid
-
-
13-cyclohexyl-6,7-dihydro-5H-indolo[1,2-d][1,4]benzodiazepine-10-carboxylic acid
-
dihedral angle between the C2-aryl group and the indole ring is 46°
13-cyclohexyl-6,7-dihydro-5H-indolo[2,1-a][2]benzazepine-10-carboxylic acid
-
dihedral angle between the C2-aryl group and the indole ring is 53°
13-cyclohexyl-6,7-dihydroindolo[1,2-d][1,4]benzothiazepine-10-carboxylate
-
dihedral angle between the C2-aryl group and the indole ring is 56°
13-cyclohexyl-6,7-dihydroindolo[1,2-d][1,4]benzoxazepine-10-carboxylic acid
-
dihedral angle between the C2-aryl group and the indole ring is 43°
14-cyclohexyl-7,8-dihydro-6H-indolo[1,2-e][1,5]benzoxazocine-11-carboxylate
-
dihedral angle between the C2-aryl group and the indole ring is 61°
1H-benzimidazole-5-carboxylic acid, 2-[4-[[4'-chloro-4-(2-oxo-1-pyrrolidinyl)[1,1'-biphenyl]-2-yl]methoxy]-2-fluorophenyl]-1-cyclohexyl hydrochloride
i.e. JTK-109
2',3'-dideoxycytidine triphosphate
-
inhibition is higher in presence of Mn2+ than in presence of Mg2+
2',3'-dideoxyguanosine triphosphate
-
inhibition is higher in presence of Mn2+ than in presence of Mg2+
2'-deoxycytidine triphosphate
-
inhibition is higher in presence of Mn2+ than in presence of Mg2+
2'-fluoro-2'C-methylcytidine-5'-triphosphate
-
acts as a chain terminator after incorporated during RNA synthesis. It is readily incorporated into a growing primer by NS5B but is also efficiently excised
2'-fluoro-2'C-methyluridine-5'-triphosphate
-
acts as a chain terminator after incorporated during RNA synthesis. It is readily incorporated into a growing primer by NS5B but is also efficiently excised. Although 2'C-modified CTP analogs are more efficiently incorporated compared with the UTP analog, the UTP analog is a better inhibitor because of its resistance to ATP-dependent excision
2'C-methylcytidine triphosphate
-
acts as a chain terminator after incorporated during RNA synthesis. It is readily incorporated into a growing primer by NS5B but is also efficiently excised
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-[(E)-phenyldiazenyl]aniline
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-{(E)-[3-(trifluoromethyl)phenyl]diazenyl}aniline
2-(2-C-methyl-b-D-ribofuranosyl)-2,6-dihydro-7H-2,3,5,6-tetraazabenzo[cd]azulen-7-one
-
-
2-(3-[[(2-chlorobenzyl)carbamoyl]amino]thiophen-2-yl)-5,6-dihydroxypyrimidine-4-carboxylic acid
-
-
2-(4-chlorophenyl)-3-cyclohexyl-1-[2-[4-(diethylamino)piperidin-1-yl]-2-oxoethyl]-1H-indole-6-carboxylic acid
-
-
2-(4-[[2-(4-acetylpiperazin-1-yl)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]-2-fluorophenyl)-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
-
-
2-(4-[[2-(4-carboxypiperidin-1-yl)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]-2-fluorophenyl)-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
-
-
2-(4-[[2-(4-chlorophenoxy)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]-2-fluorophenyl)-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
-
-
2-(4-[[4'-chloro-4-(2-oxopyrrolidin-1-yl)biphenyl-2-yl]methoxy]-2-fluorophenyl)-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
-
-
2-(4-[[5-(acetylamino)-2-morpholin-4-ylbenzyl]oxy]-2-fluorophenyl)-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
-
-
2-([3-[1-(2-cyclopropylethyl)-6-fluoro-4-hydroxy-2-oxo-1,2-dihydroquinolin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]oxy)acetamide
-
-
2-([3-[1-(cyclobutylamino)-4-hydroxy-2-oxo-1,2-dihydroquinolin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]oxy)acetamide
A-782759
2-([3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydro-1,8-naphthyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]oxy)acetamide
-
-
2-([5-(2,4-dichlorophenyl)-1,3,4-thiadiazol-2-yl]imino)-1,3-thiazolidin-4-one
-
-
2-([5-(2,6-dichlorophenyl)-1,3,4-thiadiazol-2-yl]imino)-1,3-thiazolidin-4-one
-
-
2-([5-(2-chloro-6-fluorophenyl)-1,3,4-thiadiazol-2-yl]-imino)-1,3-thiazolidin-4-one
-
-
2-([[1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]carbonyl]amino)-5-(pyrrolidin-1-ylsulfonyl)phenyl 1-methyl-3-(trifluoromethyl)-1H-pyrazole-5-carboxylate
-
-
2-amino-7-(2-C-methyl-beta-D-ribofuranosyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
-
2-fluoro-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-5-(trifluoromethyl)benzamide
-
-
2-methyl-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-6-(trifluoromethyl)pyridine-3-carboxamide
-
-
2-nitro-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-4-(trifluoromethyl)benzamide
-
-
2-[2-chloro-4-(2-[2-cyclopentyl-5-[(5,7-dimethyl[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)methyl]-4-hydroxy-6-oxo-3,6-dihydro-2H-pyran-2-yl]ethyl)phenyl]-2-methylpropanenitrile
-
-
2-[4-(2-[(2R)-2-cyclopentyl-4-hydroxy-5-[(6-methyl[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)methyl]-6-oxo-3,6-dihydro-2H-pyran-2-yl]ethyl)-2-fluorophenyl]-2-methylpropanenitrile
-
-
2-[4-(2-[2-cyclopentyl-5-[(5,7-dimethyl[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)methyl]-4-hydroxy-6-oxo-3,6-dihydro-2H-pyran-2-yl]ethyl)-2-fluorophenyl]-2-methylpropanenitrile
-
-
2-[4-(benzyloxy)phenyl]-3-cyclohexyl-1-[2-(dimethylamino)-2-oxoethyl]-1H-indole-6-carboxylic acid
-
-
2-[4-([4'-chloro-4-[(4-hydroxypiperidin-1-yl)carbonyl]biphenyl-2-yl]methoxy)-2-fluorophenyl]-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
-
-
2-[4-([5-[acetyl(1-methylethyl)amino]-2-morpholin-4-ylbenzyl]oxy)-2-fluorophenyl]-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
-
-
2-[4-([5-[acetyl(methyl)amino]-2-morpholin-4-ylbenzyl]oxy)-2-fluorophenyl]-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
-
-
2-[4-[(5-chloro-2-morpholin-4-ylbenzyl)oxy]-2-fluorophenyl]-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
-
-
2-[5-[[4-(pyrrolidin-1-ylsulfonyl)phenyl]carbamoyl]-3-(trifluoromethyl)-1H-pyrazol-1-yl]benzoic acid
-
-
3'-azido-3'-deoxythymidine triphosphate
incorporated by SARS-CoV RNA-dependent RNA polymerase (RdRp), and blocks further incorporation by the polymerase
3'-dATP
incorporation of the 3'-deoxynucleotide triphosphate fully prevents extension of a product in the presence of the next correct ribonucleotide
3'-dCTP
incorporation of the 3'-deoxynucleotide triphosphate fully prevents extension of a product in the presence of the next correct ribonucleotide
3'-deoxy-5'-O-([2-[(2,2-dimethyl-1-methylidenepropyl)sulfanyl]ethoxy][2-[(2,2-dimethylpropanoyl)sulfanyl]ethoxy]phosphoryl)cytidine
-
-
3'-fluoro-3'-deoxythymidine triphosphate
incorporated by SARS-CoV RNA-dependent RNA polymerase (RdRp), and blocks further incorporation by the polymerase
3-(1,1-dioxido-4H-1,2,4-benzothiadiazin-3-yl)-4-hydroxy-1-(3-methylbutyl)quinolin-2(1H)-one
-
-
3-(benzyloxy)-13-cyclohexyl-6,7-dihydroindolo[1,2-d][1,4]benzoxazepine-10-carboxylic acid
-
-
3-(isopropyl[(4-methylphenyl)sulfonyl]amino)-5-phenylthiophene-2-carboxylic acid
-
-
3-([(2,4-dimethylphenyl)sulfonyl]amino)-5-phenylthiophene-2-carboxylic acid
-
-
3-([(4-chloro-2,5-dimethylphenyl)sulfonyl]amino)-5-phenylthiophene-2-carboxamide
-
-
3-allyl-5,8-dichloro-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
3-allyl-8-cyano-5-fluoro-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
3-allyl-8-cyano-5-methyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
3-allyl-8-cyano-7-fluoro-5-methyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
3-benzyl-5-chloropyrido[3,2-g]quinoxalin-2(1H)-one
-
moderate antiproliferative activity for the cell lines tested
3-butyl-5,8-dichloro-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
3-butyl-8-cyano-5-fluoro-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
3-butyl-8-cyano-5-methyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
3-butyl-8-cyano-7-fluoro-5-methyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
3-cyclohexyl-1-(2-oxo-2-piperidin-1-ylethyl)-2-phenyl-1H-indole-6-carboxylic acid
-
-
3-cyclohexyl-1-(2-[methyl[(1-methylpiperidin-3-yl)methyl]amino]-2-oxoethyl)-2-phenyl-1H-indole-6-carboxylic acid
-
-
3-cyclohexyl-1-methyl-2-(4-[[2-morpholin-4-yl-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-indole-6-carboxylic acid
-
-
3-cyclohexyl-1-[2-(dimethylamino)-2-oxoethyl]-2-(4-methoxyphenyl)-1H-indole-6-carboxylic acid
-
-
3-cyclohexyl-1-[2-(dimethylamino)-2-oxoethyl]-2-phenyl-1H-indole-6-carboxylic acid
-
-
3-cyclohexyl-1-[2-(dimethylamino)-2-oxoethyl]-2-phenyl-1H-pyrrolo[2,3-b]pyridine-6-carboxylic acid
-
-
3-cyclohexyl-2-furan-3-yl-1-[2-oxo-2-(4-pyrrolidin-1-ylpiperidin-1-yl)ethyl]-1H-indole-6-carboxylic acid
-
-
3-cyclohexyl-2-furan-3-yl-N-[(1S)-2-(5-hydroxy-1H-indol-3-yl)-1-(1,3-thiazol-4-yl)ethyl]-1-methyl-1H-indole-6-carboxamide
-
-
3-tert-butyl-1-methyl-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-1H-pyrazole-5-carboxamide
-
-
3-[(1S,9aR)-octahydro-2H-quinolizin-1-ylmethyl]-1-phenyl-3-(trifluoromethylphenyl)triazene
3-[(4-amino-2-tert-butyl-5-methylphenyl)sulfanyl]-6-cyclopentyl-4-hydroxy-6-[2-(4-hydroxyphenyl)ethyl]-5,6-dihydro-2H-pyran-2-one
-
-
3-[[(trans-4-methylcyclohexyl)carbonyl](1-methylethyl)amino]-5-phenylthiophene-2-carboxylic acid
-
-
3-[[(trans-4-methylcyclohexyl)carbonyl](1-methylpiperidin-4-yl)amino]-5-phenylthiophene-2-carboxylic acid
-
-
3-[[4'-chloro-4-(2-oxopyrrolidin-1-yl)biphenyl-2-yl]methoxy]-13-cyclohexyl-6,7-dihydroindolo[1,2-d][1,4]benzoxazepine-10-carboxylic acid
-
-
4'-azido-cytidine triphosphate
-
acts as a chain terminator after incorporated during RNA synthesis. It is readily incorporated into a growing primer by NS5B but is also efficiently excised
4'-C-azidocytidine-5'-triphosphate
causes only partial chain termination
4-bromo-1-methyl-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
-
4-methyl-N-((5Z)-5-[(5-methyl-2-furyl)methylene]-4-oxo-4,5-dihydro-1,3-thiazol-2-yl)benzenesulfonamide
-
-
4-[(E)-(2,4-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
4-[(E)-(2,5-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
5'-O-([2-[(2,2-dimethyl-1-methylidenepropyl)sulfanyl]ethoxy][2-[(2,2-dimethylpropanoyl)sulfanyl]ethoxy]phosphoryl)-2'-O-methylcytidine
-
-
5,6-dihydroxy-2-[4-(([(1-naphthylsulfonyl)amino]carbonyl)amino)-3-thienyl]pyrimidine-4-carboxylic acid
-
-
5,8-dichloro-3-propyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
5-(2,6-dichlorobenzylidene)-2-[[5-(2,4-dichlorophenyl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(2,6-dichlorobenzylidene)-2-[[5-(2,6-dichlorophenyl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(2,6-dichlorobenzylidene)-2-[[5-(2-chloro-6-fluorophenyl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(2,6-dichlorobenzylidene)-2-[[5-(2-chlorophenyl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(2,6-dichlorobenzylidene)-2-[[5-(2-fluorophenyl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(2,6-dichlorobenzylidene)-2-[[5-(3-fluorophenyl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(2,6-dichlorobenzylidene)-2-[[5-(pyridin-3-yl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(2-amino-2-oxoethoxy)-N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
-
5-(3-fluorobenzylidene)-2-[[5-(2,4-dichlorophenyl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(3-fluorobenzylidene)-2-[[5-(2,6-dichlorophenyl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(3-fluorobenzylidene)-2-[[5-(2-chloro-6-fluorophenyl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(3-fluorobenzylidene)-2-[[5-(2-chlorophenyl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(3-fluorobenzylidene)-2-[[5-(2-fluorophenyl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(3-fluorobenzylidene)-2-[[5-(3-fluorophenyl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(3-fluorobenzylidene)-2-[[5-(pyridin-3-yl)-1,3,4-thiadiazol-2-yl]imino]-1,3-thiazolidin-4-one
-
-
5-(4-bromophenylmethylene)-3-(benzenesulfonylamino)-4-oxo-2-thionothiazolidine
-
reversible and non-competitive with nucleotides. Inhibitor appear to form a reversible covalent bond with the NS5B cysteine 366
5-(4-chlorophenylmethylene)-3-(benzenesulfonylamino)-4-oxo-2-thionothiazolidine
-
reversible and non-competitive with nucleotides. Inhibitor appear to form a reversible covalent bond with the NS5B cysteine 366
5-(4-cyanophenyl)-3-([(2-methylphenyl)sulfonyl]amino)thiophene-2-carboxylic acid
-
-
5-(4-[[(2-cyclohexyl-3-phenylquinoxalin-6-yl)carbonyl]amino]phenyl)furan-2-carboxylic acid
-
5-(4-[[(3-cyclohexyl-2-phenylquinoxalin-6-yl)carbonyl]amino]phenyl)furan-2-carboxylic acid
-
5-(carboxymethoxy)-N-[(1-cyclohexyl-2-furan-3-yl-1H-benzimidazol-5-yl)carbonyl]-L-tryptophan
-
-
5-([3,5-bis(trifluoromethyl)phenyl]amino)-3-hydroxyisothiazole-4-carbonitrile
-
-
5-azidomethyl-3-hydroxy-4-hydroxymethyl-pyridine-2-carboxylic acid hydroxyamide
-
i.e. DMB213. Competitive with natural nucleoside triphosphate substrates
5-chloro-3-phenylpyrido[3,2-g]quinoxalin-2(1H)-one
-
compound is equally cytotoxic for all cell lines tested
5-cyano-8-fluoro-1-propyl-2,3,4,9-tetrahydro-1H-carbazole-1-carboxylic acid
-
-
5-cyano-8-methyl-1-propyl-2,3,4,9-tetrahydro-1H-carbazole-1-carboxylic acid
-
-
5-cyclopropyl-2-(4-fluorophenyl)-6-[(2-hydroxyethyl)(methylsulfonyl)amino]-N-methyl-1-benzofuran-3-carboxamide
-
-
5-ethyl-1-(2-C-methyl-b-D-ribofuranosyl)-1,5-dihydro-1,4,5,6,8-pentaazaacenaphthylen-3-amine
-
-
5-fluoro-7-(2-C-methyl-beta-D-ribofuranosyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine
-
-
5-fluorouridine triphosphate
-
5-fluorouridine triphosphate is a strong competitive inhibitor of VPg uridylylation by FMDV 3D in vitro, versus UTP, FUTP, dTTP, ATP, CTP, or GTP, uridylylation at VPg Tyr3, which is located near the active site of 3D, at the RNA binding cleft of 3D, binding structure from crystal structure, overview. No inhibition with oligoT primers
5-hydroxy-N-[[3-(3-methoxyphenyl)-2-(4-methoxyphenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
-
5-[(4-bromophenyl)methyl]-2-phenyl-5H-imidazo[4,5-c]pyridine
-
5-[[(4-chlorophenyl)sulfonyl]amino]-2-methyl-1-benzofuran-3-carboxylic acid
Q6DLV0
crystallization data, the inhibitor binds to the protein as a dimer and causes conformational changes in the protein
5BSL3.2N
-
the complementary strand of 5BSL3.2 inhibits the enzyme, the bulge structure is indispensable for enzyme binding
-
6-(2-amino-2-oxoethoxy)-N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
-
6-cyclohexyl-4-methyl-5-(4-[[2-morpholin-4-yl-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-4H-thieno[3,2-b]pyrrole-2-carboxylic acid
-
-
6-cyclohexyl-4-[2-(dimethylamino)-2-oxoethyl]-5-phenyl-4H-thieno[3,2-b]pyrrole-2-carboxylic acid
-
-
6-[2-(3-chloro-4-methoxyphenyl)ethyl]-6-cyclopentyl-4-hydroxy-3-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]-5,6-dihydro-2H-pyran-2-one
-
-
6-[2-(5-chloro-2,4-dimethoxyphenyl)ethyl]-6-cyclopentyl-3-[(5,7-dimethyl[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)sulfanyl]-4-hydroxy-5,6-dihydro-2H-pyran-2-one
-
AG-021541
6-[2-(methoxysulfinyl)hydrazino]-9-(2-C-methyl-b-D-ribofuranosyl)-9H-purine
-
-
7-(2-C-methyl-b-D-ribofuranosyl)-5-nitro-7H-pyrrolo[2,3-d]pyrimidin-4-amine
-
-
8,8'-[carbonylbis(imino-3,1-phenylene carbonylimino)]bis(1,3,5-naphthalene-trisulfonic acid)
i.e. NF023
8,8'-[carbonylbis(iminobenzene-3,1-diylcarbonylimino)]dinaphthalene-1,3,5-trisulfonic acid
8-chloro-1-propyl-5-(trifluoromethyl)-2,3,4,9-tetrahydro-1H-carbazole-1-carboxylic acid
-
-
8-cyano-5-fluoro-3-propyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
8-cyano-5-methyl-3-propyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
8-cyano-7-fluoro-5-methyl-3-propyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
9-(5,6-dideoxy-2-C-methyl-6-phosphono-b-D-ribo-hexofuranosyl)-9H-purin-6-amine
-
-
9-(5-O-[bis[2-(acetylsulfanyl)ethoxy]phosphoryl]-2-C-methyl-b-D-ribofuranosyl)-6-ethoxy-9H-purine
-
-
afzelin
strong binding affinity to the enzyme (RdRp)
aptamer F38
-
identification and characterization of aptamers to the 3Dpol enzyme (serotype C). Three of these RNA molecules display inhibitory activity in an in vitro UTP incorporation assay
-
aptamer F47
-
identification and characterization of aptamers to the 3Dpol enzyme (serotype C). Three of these RNA molecules display inhibitory activity in an in vitro UTP incorporation assay
-
aptamer F52
-
identification and characterization of aptamers to the 3Dpol enzyme (serotype C). Three of these RNA molecules display inhibitory activity in an in vitro UTP incorporation assay
-
Astragalin
strong binding affinity to the enzyme (RdRp)
benzyl 1-[[4-([[1-methyl-4-(trifluoromethyl)-1H-pyrrol-2-yl]carbonyl]amino)phenyl]sulfonyl]prolinate
-
-
beta-D-2'-beta-C-ethynyl-7-deaza-adenosine-5'-triphosphate
causes chain termination after incorporation into nascent RNA
beta-D-2'-beta-C-methyladenosine-5'-triphosphate
causes chain termination after incorporation into nascent RNA
beta-D-2'-beta-C-methylcytidine-5'-triphosphate
causes chain termination after incorporation into nascent RNA
beta-D-2'-beta-C-methylguanosine-5'-triphosphate
causes chain termination after incorporation into nascent RNA
beta-D-2'-deoxy-2'-alpha-fluoro-2'-beta-C-methylcytidine-5'-triphosphate
causes chain termination after incorporation into nascent RNA
beta-D-2'-deoxy-2'-alpha-fluoro-2'-beta-C-methylguanosine-5'-triphosphate
causes chain termination after incorporation into nascent RNA
beta-D-2'-deoxy-2'-fluoro-2'-C-methylcytidine
i.e. PSI-6130, a selective inhibitor of hepatitis C virus replication that targets the NS5B polymerase
beta-D-2'-deoxy-2'-fluoro-2'-C-methylcytidine 5'-triphosphate
-
PSI-6130-TP, potent inhibitor
beta-D-2'-deoxy-2'-fluoro-2'-C-methyluridine 5'-triphosphate
-
also named RO2433-TP or PSI-6206, potent inhibitor
biorobin
strong binding affinity to the enzyme (RdRp)
conivaptan
binds to RNA-dependent RNA polymerase with high affinity
cyclohexyl 4-([[1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]carbonyl]amino)benzenesulfonate
-
-
delvomycin
-
the protein synthetic activity of the EF-Tu in the replicase complex is eliminated but the Qbeta RNA replicase activity is only slightly affected
dihydropyranone inhibitor
binding of non-nucleoside inhibitors induces significant fluctuations at the atomic level which are critical for enzymatic activity, with minimalglobal structural alterations. Residue-wise mapping of interactions of non-nucleoside inhibitors at different sites exhibits some conserved interaction patterns of key amino acids and water molecules
dimethyl (2S,4S,5R)-2-(2-methylpropyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]pyrrolidine-2,4-dicarboxylate
-
-
eltrombopag
binds to RNA-dependent RNA polymerase with high affinity
ErbB3-binding protein 1
-
specifically interacts with the catalytic subunit PB1 of influenza virus RNA polymerase near the catalytic site for RNA polymerization
-
ergotamine
binds to RNA-dependent RNA polymerase with high affinity
ethyl (2E)-3-[4-([[1-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoate
-
ethyl (2E)-3-[4-([[1-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclopentyl]carbonyl]amino)phenyl]prop-2-enoate
-
ethyl (2E)-3-[4-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)phenyl]prop-2-enoate
-
ethyl 2-methylimidazo[1,2-a]pyrrolo[2,3-c]pyridin-8-carboxylate
AG110, potent inhibitor of pestivirus replication, does not inhibit the in vitro activity of recombinant bovine viral diarrhea virus RdRp but inhibits the activity of bovine viral diarrhea virus replication complexes
fisetin
high affinities with the RNA-polymerase active site
Fructus Ligustri Lucidi aqueous extract
-
0.005 mg/ml, inhibits intracellular NS5B-catalyzed RNA synthesis
-
HA1077
-
i.e. fasudil, reduces the levels of intracellular viral RNA by 70% at 0.02 mM, the RdRp activity of HCV NS5B is not inhibited by the PRK2 inhibitor, but its activation by phosphorylation through PRK2
HgCl2
-
inhibition is reversed by incubation with an excess amount of dithiothreitol and 2-mercaptoethanol
IDX-184
high potential to fight the SARS-CoV-2 strain specifically
imidazole
tolerable at low concentrations, but inhibits at concentrations higher than 25 mM
kaempferol
strong binding affinity to the enzyme (RdRp)
methyl 1-[[4-([[1-methyl-4-(trifluoromethyl)-1H-pyrrol-2-yl]carbonyl]amino)phenyl]sulfonyl]piperidine-2-carboxylate
-
-
methyl 2-[5-[[4-(pyrrolidin-1-ylsulfonyl)phenyl]carbamoyl]-3-(trifluoromethyl)-1H-pyrazol-1-yl]benzoate
-
-
methyl 5-(2-amino-2-oxoethoxy)-N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophanate
-
methyl 6-(2-amino-2-oxoethoxy)-N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophanate
-
methyl N-[(2,3-difuran-2-ylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophanate
-
methyl N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophanate
-
methyl N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-6-hydroxy-L-tryptophanate
-
methyl N-[(2,3-dipyridin-2-ylquinoxalin-6-yl)carbonyl]-L-tryptophanate
-
methyl N-[(2,3-ditetrahydrofuran-2-ylquinoxalin-6-yl)carbonyl]-6-hydroxy-L-tryptophanate
-
methyl N-[(2,3-ditetrahydrofuran-2-ylquinoxalin-6-yl)carbonyl]-L-tryptophanate
-
methyl N-[[2,3-bis(3-methoxyphenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophanate
-
methyl N-[[2,3-bis(3-methoxyphenyl)quinoxalin-6-yl]carbonyl]-L-tryptophanate
-
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-(2-methoxy-2-oxoethoxy)-L-tryptophanate
-
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophanate
-
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-[[(2E)-4-methoxy-4-oxobut-2-en-1-yl]oxy]-L-tryptophanate
-
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-(2-methoxy-2-oxoethoxy)-L-tryptophanate
-
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophanate
-
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-[[(2E)-4-methoxy-4-oxobut-2-en-1-yl]oxy]-L-tryptophanate
-
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophanate
-
methyl N-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophanate
-
methyl N-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophanate
-
methyl N-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-L-tryptophanate
-
Myricitrin
strong binding affinity to the enzyme (RdRp)
N,1-dimethyl-N-[4-(piperidin-1-ylsulfonyl)phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
-
N,N'-[4-(pyrrolidin-1-ylsulfonyl)benzene-1,2-diyl]bis[1-methyl-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide]
-
-
N-(3-cyano-5,6-dihydro-4H-cyclopenta[b]thiophen-2-yl)-4-methyl-2-phenyl-1,3-thiazole-5-carboxamide
a non-nucleoside inhibitor
N-(3-cyano-5,6-dihydro-4H-cyclopenta[b]thiophen-2-yl)-4-methyl-2-phenyl-1,3-thiazole-5-carboximidic acid
NIC02, in combination with NIC04, i.e. 1-benzyl-N-(2,3-dimethylphenyl)-3,5-dimethyl-1H-pyrazole-4-carboxamide
N-(3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-5-[(1E)-pent-1-en-1-yl]-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl)methanesulfonamide
-
-
N-(3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-5-[(1E)-prop-1-en-1-yl]-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl)methanesulfonamide
-
-
N-(3-[4-hydroxy-5-[(E)-2-(4-methoxyphenyl)ethenyl]-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl)methanesulfonamide
-
-
N-(3-[5-[(1E)-3,3-dimethylbut-1-en-1-yl]-4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl)methanesulfonamide
-
-
N-(4-[[2-(hydroxymethyl)piperidin-1-yl]sulfonyl]phenyl)-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
N-(4-[[4-(methoxymethylidene)piperidin-1-yl]sulfonyl]phenyl)-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
N-(4-[[4-(tert-butoxyamino)piperazin-1-yl]sulfonyl]phenyl)-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
N-propyl-N-[2-(2H-1,2,4-triazino[5,6-b]indol-3-ylthio)ethyl]-1-propanamine
VP32947
N-[(13-cyclohexyl-6,7-dihydroindolo[1,2-d][1,4]benzoxazepin-10-yl)carbonyl]-2-methylalanine
-
-
N-[(1R)-6-chloro-2,3,4,9-tetrahydro-1H-carbazol-1-yl]pyridine-2-carboxamide
-
-
N-[(2,3-ditetrahydrofuran-2-ylquinoxalin-6-yl)carbonyl]-6-hydroxy-L-tryptophan
-
N-[(2,4-dichlorophenyl)carbonyl]-N-[3-(trifluoromethyl)benzyl]-L-phenylalanine
-
-
N-[(2-cyclohexyl-3-phenylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophan
-
N-[(3-cyclohexyl-2-phenylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophan
-
N-[(5Z)-5-((5-[2-chloro-5-(trifluoromethyl)phenyl]-2-furyl)methylene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]benzenesulfonamide
-
-
N-[(5Z)-5-(3,4-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]benzenesulfonamide
-
-
N-[(5Z)-5-(4-bromobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]benzenesulfonamide
-
-
N-[(Z)-2-[4-(2-bromophenoxy)phenyl]-1-[(2-hydroxyethyl)carbamoyl]ethenyl]benzamide
-
-
N-[2-amino-4-(pyrrolidin-1-ylsulfonyl)phenyl]-1-methyl-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
-
N-[2-hydroxy-4-(pyrrolidin-1-ylsulfonyl)phenyl]-1-methyl-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
-
N-[3-[(4aR,7aS)-1-(4-fluorobenzyl)-4-hydroxy-2-oxo-2,4a,5,6,7,7a-hexahydro-1H-cyclopenta[b]pyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(4R)-1-hydroxy-4-methyl-4-(3-methylbutyl)-3-oxo-3,4-dihydronaphthalen-2-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
A-837093
N-[3-[(4R)-5-(4-fluorobenzyl)-8-hydroxy-4-methyl-6-oxo-5-azaspiro[2.5]oct-7-en-7-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5R)-1-cyclobutyl-4-hydroxy-5-methyl-2-oxo-5-propyl-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5R)-1-cyclobutyl-4-hydroxy-5-methyl-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5R)-1-cyclobutyl-5-(2-cyclopropylethyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5R)-1-cyclobutyl-5-(3,3-dimethylbutyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5R)-1-cyclohexyl-4-hydroxy-5-methyl-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5R)-1-cyclohexyl-5-(3,3-dimethylbutyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5R)-1-cyclohexyl-5-(4-fluorobenzyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5R)-1-cyclopentyl-4-hydroxy-5-(3-methylbut-2-en-1-yl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5R)-1-cyclopentyl-4-hydroxy-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5R)-1-cyclopentyl-4-hydroxy-5-methyl-2-oxo-5-prop-2-yn-1-yl-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5R)-1-cyclopentyl-4-hydroxy-5-methyl-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5R)-1-cyclopentyl-5-(2-cyclopropylethyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5R)-1-cyclopentyl-5-(3,3-dimethylbutyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5R)-1-cyclopentyl-5-(4-fluorobenzyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5R)-1-cyclopentyl-5-ethyl-4-hydroxy-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5R)-1-cyclopropyl-4-hydroxy-5-methyl-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5R)-1-cyclopropyl-5-(3,3-dimethylbutyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5R)-1-cyclopropyl-5-(4-fluorobenzyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5R)-4-hydroxy-5-methyl-5-(3-methylbutyl)-2-oxo-1-phenyl-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5R)-5-butyl-1-cyclobutyl-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5R)-6-(4-fluorobenzyl)-9-hydroxy-5-methyl-7-oxo-6-azaspiro[3.5]non-8-en-8-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5S)-1,5-bis(4-fluorobenzyl)-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5S)-1-(4-fluorobenzyl)-4-hydroxy-5-(3-methylbut-2-en-1-yl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5S)-1-(4-fluorobenzyl)-4-hydroxy-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5S)-1-(4-fluorobenzyl)-4-hydroxy-5-methyl-2-oxo-5-phenyl-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5S)-1-(4-fluorobenzyl)-4-hydroxy-5-methyl-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5S)-5-ethyl-1-(4-fluorobenzyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(5S)-5-tert-butyl-1-(3-chloro-4-fluorobenzyl)-4-hydroxy-2-oxo-2,5-dihydro-1H-pyrrol-3-yl]-1,1-dioxido-4H-1,2-benzothiazin-7-yl]methanesulfonamide
-
-
N-[3-[(5S)-5-tert-butyl-1-(4-fluorobenzyl)-4-hydroxy-2-oxo-2,5-dihydro-1H-pyrrol-3-yl]-1,1-dioxido-1,2-benzisothiazol-6-yl]methanesulfonamide
-
-
N-[3-[(6R)-1-(4-fluorobenzyl)-4-hydroxy-2-oxo-6-phenyl-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(6R)-1-(4-fluorobenzyl)-4-hydroxy-6-(1-methylethyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(6R)-1-(4-fluorobenzyl)-4-hydroxy-6-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(6R)-6-ethyl-1-(4-fluorobenzyl)-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(6R)-6-tert-butyl-1-(4-fluorobenzyl)-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(6S)-1-(4-fluorobenzyl)-4-hydroxy-6-(1-methylethyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(6S)-1-(4-fluorobenzyl)-6-(4-fluorophenyl)-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(6S)-6-(1-ethylpropyl)-1-(4-fluorobenzyl)-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[(6S)-6-ethyl-1-(4-fluorobenzyl)-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[1-(4-fluorobenzyl)-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[1-(4-fluorobenzyl)-4-hydroxy-5,5-dimethyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[1-(cyclobutylamino)-4-hydroxy-2-oxo-1,2-dihydroquinolin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]sulfamide
-
-
N-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydro-1,8-naphthyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
-
N-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
-
N-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-5-phenyl-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
-
N-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-5-thiophen-2-yl-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
-
N-[3-[5-acetyl-4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
-
N-[3-[5-bromo-4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
-
N-[3-[5-ethenyl-4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
-
N-[3-[5-furan-2-yl-4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
-
N-[3-[6-(4-fluorobenzyl)-9-hydroxy-7-oxo-6-azaspiro[4.5]dec-8-en-8-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[3-[7-(4-fluorobenzyl)-10-hydroxy-8-oxo-7-azaspiro[4.5]dec-9-en-9-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
-
N-[4-(1H-indol-1-ylsulfonyl)phenyl]-1-methyl-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
-
N-[4-(1H-indol-1-ylsulfonyl)phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
N-[4-(azepan-1-ylsulfonyl)phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
N-[4-(azocan-1-ylsulfonyl)phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
N-[4-(cyclohexylsulfamoyl)phenyl]-1-methyl-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
-
N-[4-(diethylsulfamoyl)phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
N-[4-(dimethylsulfamoyl)phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
N-[4-(diprop-2-en-1-ylsulfamoyl)phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
N-[4-(dipropylsulfamoyl)phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-1,3-benzothiazole-2-carboxamide
-
-
N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-1-[2-(trifluoromethyl)phenyl]-1H-imidazole-2-carboxamide
-
-
N-[4-([4-[2-(2-hydroxyethoxy)ethyl]piperazin-1-yl]sulfonyl)phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
N-[4-[(2,6-dimethylpiperidin-1-yl)sulfonyl]phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
N-[4-[(2-ethylpiperidin-1-yl)sulfonyl]phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
N-[4-[(4-aminopiperidin-1-yl)sulfonyl]phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
N-[4-[(4-hydroxypiperidin-1-yl)sulfonyl]phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
N-[4-[(4-tert-butoxypiperazin-1-yl)sulfonyl]phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
N-[4-[bis(1-methylethyl)sulfamoyl]phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
N-[4-[bis(2-methylpropyl)sulfamoyl]phenyl]-1-methyl-4-(trifluoromethyl)-1H-pyrrole-2-carboxamide
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-phenyldiazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-[3-(trifluoromethyl)phenyl]diazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
N-[[1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]methyl]-4-(pyrrolidin-1-ylsulfonyl)aniline
-
-
N-[[2,3-bis(3-methoxyphenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophan
-
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-(carboxymethoxy)-L-tryptophan
-
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophan
-
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-[[(2E)-3-carboxyprop-2-en-1-yl]oxy]-L-tryptophan
-
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-(carboxymethoxy)-L-tryptophan
-
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophan
-
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-[[(2E)-3-carboxyprop-2-en-1-yl]oxy]-L-tryptophan
-
N-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophan
-
N-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophan
-
N-[[2-cyclohexyl-3-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophan
-
N-[[2-cyclohexyl-3-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
-
N-[[3-cyclohexyl-2-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophan
-
N-[[3-cyclohexyl-2-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
-
N2-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydro-1,8-naphthyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]glycinamide
-
-
p-Hydroxymercuriphenylsulfonate
-
0.1 mM, reduces the transcription activity down to 10%
PCMB
-
inhibition is reversed by incubation with an excess amount of dithiothreitol and 2-mercaptoethanol. PCMB-inhibited enzyme is unable to synthesize RNA, but still maintains template-binding ability
phenyl 1-[[4-([[1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]carbonyl]amino)phenyl]sulfonyl]-L-prolinate
-
-
phenylalanine
binding of non-nucleoside inhibitors induces significant fluctuations at the atomic level which are critical for enzymatic activity, with minimalglobal structural alterations. Residue-wise mapping of interactions of non-nucleoside inhibitors at different sites exhibits some conserved interaction patterns of key amino acids and water molecules
Poly(U)
-
inhibits by competing with the template for binding to the enzyme, does not inhibit the elongation of preinitiated RNA chains
Polyethylene sulfonate
-
inhibits by competing with the template for binding to the enzyme, does not inhibit the elongation of preinitiated RNA chains
-
propan-2-yl (2S)-2-([([(2R,3R,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxy-4-(prop-1-yn-1-yl)oxolan-2-yl]methoxy)(phenoxy)phosphoryl]amino)propanoate
-
-
propan-2-yl (2S)-2-([([(2R,3R,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxy-4-methyloxolan-2-yl]methoxy)(phenoxy)phosphoryl]amino)propanoate
-
-
propan-2-yl (2S)-2-([([(2R,3R,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-4-ethynyl-3,4-dihydroxyoxolan-2-yl]methoxy)(phenoxy)phosphoryl]amino)propanoate
-
-
propan-2-yl (2S)-2-([([(2S,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-fluoro-3,4-dihydroxy-4-(prop-1-yn-1-yl)oxolan-2-yl]methoxy)(phenoxy)phosphoryl]amino)propanoate
-
-
propan-2-yl (2S)-2-([([(2S,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-fluoro-3,4-dihydroxy-4-methyloxolan-2-yl]methoxy)(phenoxy)phosphoryl]amino)propanoate
-
-
propan-2-yl (2S)-2-([([(2S,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-4-ethynyl-2-fluoro-3,4-dihydroxyoxolan-2-yl]methoxy)(phenoxy)phosphoryl]amino)propanoate
-
the prodrug displays potent anti-dengue virus activity in the primary human peripheral blood mononuclear cell-based assay with no significant cytotoxicity in human hepatocellular liver carcinoma cell lines and no mitochondrial toxicity in the cell-based assay using human prostate cancer cell lines
quercetin
high affinities with the RNA-polymerase active site; strong binding affinity to the enzyme (RdRp)
quercetin-3'-O-glucuronide
better binding affinities than quercetin
quercetin-3'-O-sulfate
better binding affinities than quercetin
quercetin-3-O-glucoside
strong binding affinity to the enzyme (RdRp)
quercetin-3-O-glucuronide
better binding affinities than quercetin
quercetin-3-O-rutinoside
i.e. rutin, most active compared to all quercetin derivatives
quercetin-7-O-glucuronide
better binding affinities than quercetin
quercetin-7-O-sulfate
better binding affinities than quercetin
quercitrin
strong binding affinity to the enzyme (RdRp)
quinupristin
virtual screen identifies several drugs predicted to bind in the conserved RNA tunnel. Quinupristin is expected to bind across the RNA tunnel, blocking access from both sides and suggesting that it has the potential to arrest viral replication by preventing viral RNA synthesis. Quinupristin is an antibiotic that has been in clinical use for two decades and causes relatively minor side effects
R7128
is the prodrug of PSI-6130, inhibits the enzyme and viral replication
RNA
-
inhibited by high non-template RNA concentrations. This inhibition indicates feedback regulation of minus-strand synthesis
setrobuvir
high potential to fight the SARS-CoV-2 strain specifically
Tenofovir
binds to the enzyme (SARS-CoV-2 RdRp) with binding energies comparable to native nucleotides, potent drugs against SARS-CoV-2
tert-butyl 1-[[4-([[1-methyl-4-(trifluoromethyl)-1H-pyrrol-2-yl]carbonyl]amino)phenyl]sulfonyl]piperidine-2-carboperoxoate
-
-
thiophene
binding of non-nucleoside inhibitors induces significant fluctuations at the atomic level which are critical for enzymatic activity, with minimalglobal structural alterations. Residue-wise mapping of interactions of non-nucleoside inhibitors at different sites exhibits some conserved interaction patterns of key amino acids and water molecules
tipranavir
binds to RNA-dependent RNA polymerase with high affinity
Y27632
-
blocks HCV RdRp phosphorylation by suppressing PRK2 activation, reduces the levels of intracellular viral RNA by 92% at 0.02 mM, the RdRp activity of HCV NS5B is not inhibited by the PRK2 inhibitor, but its activation by phosphorylation through PRK2
YAK
high potential to fight the SARS-CoV-2 strain specifically
[(1R)-5-cyano-8-methyl-1-propyl-1,3,4,9-tetrahydropyrano[3,4-b]indol-1-yl]acetic acid
-
-
[(1R)-8-chloro-5-ethyl-1-propyl-1,3,4,9-tetrahydropyrano[3,4-b]indol-1-yl]acetic acid
-
-
[(1S)-5-cyano-8-methyl-1-(1-methylpropyl)-7-[2-(1H-pyrazol-1-yl)ethoxy]-1,3,4,9-tetrahydropyrano[3,4-b]indol-1-yl]acetic acid
-
-
1-(2,5-difluorophenyl)-3-(3'-trifluoromethylphenyl)triazene
-
1-[1-(2,5-difluorophenyl)-3-(3-trifluoromethylphenyl)-triazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-(3-trifluoromethylphenyl)-triazen-3-yl]-N,N-dimethyl-3-propanamine
-
1-[1-(2,5-difluorophenyl)-3-(3-trifluoromethylphenyl)-triazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-(3-trifluoromethylphenyl)-triazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-(3-trifluoromethylphenyl)-triazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-(3-trifluoromethylphenyl)-triazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-(3-trifluoromethylphenyl)-triazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-(3-trifluoromethylphenyl)-triazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-(3-trifluoromethylphenyl)-triazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-(3-trifluoromethylphenyl)-triazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
1-[1-(2,5-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,5-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,6-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
1-[1-(2,6-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,6-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,6-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,6-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,6-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(2,6-difluorophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(3-nitrophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
1-[1-(3-nitrophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(3-nitrophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
1-[1-(3-nitrophenyl)-3-phenyltriazen-3-yl]-N,N-dimethyl-3-propanamine
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-[(E)-phenyldiazenyl]aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-[(E)-phenyldiazenyl]aniline
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-[(E)-phenyldiazenyl]aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-[(E)-phenyldiazenyl]aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-[(E)-phenyldiazenyl]aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-[(E)-phenyldiazenyl]aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-[(E)-phenyldiazenyl]aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-[(E)-phenyldiazenyl]aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-[(E)-phenyldiazenyl]aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-[(E)-phenyldiazenyl]aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-{(E)-[3-(trifluoromethyl)phenyl]diazenyl}aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-{(E)-[3-(trifluoromethyl)phenyl]diazenyl}aniline
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-{(E)-[3-(trifluoromethyl)phenyl]diazenyl}aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-{(E)-[3-(trifluoromethyl)phenyl]diazenyl}aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-{(E)-[3-(trifluoromethyl)phenyl]diazenyl}aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-{(E)-[3-(trifluoromethyl)phenyl]diazenyl}aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-{(E)-[3-(trifluoromethyl)phenyl]diazenyl}aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-{(E)-[3-(trifluoromethyl)phenyl]diazenyl}aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-{(E)-[3-(trifluoromethyl)phenyl]diazenyl}aniline
-
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-{(E)-[3-(trifluoromethyl)phenyl]diazenyl}aniline
-
-
3'-dGTP
incorporation of the 3'-deoxynucleotide triphosphate fully prevents extension of a product in the presence of the next correct ribonucleotide
3'-dUTP
-
incorporation of the 3'-deoxynucleotide triphosphate fully preventes extension of a product in the presence of the next correct ribonucleotide
3'-dUTP
incorporation of the 3'-deoxynucleotide triphosphate fully prevents extension of a product in the presence of the next correct ribonucleotide
3-[(1S,9aR)-octahydro-2H-quinolizin-1-ylmethyl]-1-phenyl-3-(trifluoromethylphenyl)triazene
-
-
3-[(1S,9aR)-octahydro-2H-quinolizin-1-ylmethyl]-1-phenyl-3-(trifluoromethylphenyl)triazene
-
3-[(1S,9aR)-octahydro-2H-quinolizin-1-ylmethyl]-1-phenyl-3-(trifluoromethylphenyl)triazene
-
-
3-[(1S,9aR)-octahydro-2H-quinolizin-1-ylmethyl]-1-phenyl-3-(trifluoromethylphenyl)triazene
-
-
3-[(1S,9aR)-octahydro-2H-quinolizin-1-ylmethyl]-1-phenyl-3-(trifluoromethylphenyl)triazene
-
-
3-[(1S,9aR)-octahydro-2H-quinolizin-1-ylmethyl]-1-phenyl-3-(trifluoromethylphenyl)triazene
-
-
3-[(1S,9aR)-octahydro-2H-quinolizin-1-ylmethyl]-1-phenyl-3-(trifluoromethylphenyl)triazene
-
-
3-[(1S,9aR)-octahydro-2H-quinolizin-1-ylmethyl]-1-phenyl-3-(trifluoromethylphenyl)triazene
-
-
3-[(1S,9aR)-octahydro-2H-quinolizin-1-ylmethyl]-1-phenyl-3-(trifluoromethylphenyl)triazene
-
-
3-[(1S,9aR)-octahydro-2H-quinolizin-1-ylmethyl]-1-phenyl-3-(trifluoromethylphenyl)triazene
-
-
4-chloro-2-(4-nitrophenyl)-3H-imidazo[4,5-g]quinoline
-
in addition, inhibitory to the recombinant hepacivirus enzyme. Compound shows no cytotoxicity for the various cell lines tested, exception made for HepG-2 cells
4-chloro-2-(4-nitrophenyl)-3H-imidazo[4,5-g]quinoline
-
in addition, inhibitory to the recombinant bovine viral diarrhea virus enzyme. Compound shows no cytotoxicity for the various cell lines tested, exception made for HepG-2 cells
4-[(E)-(2,4-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,4-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
4-[(E)-(2,4-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,4-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,4-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,4-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,4-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,4-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,4-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,4-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,5-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,5-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
4-[(E)-(2,5-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,5-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,5-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,5-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,5-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,5-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,5-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
4-[(E)-(2,5-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
8,8'-[carbonylbis(iminobenzene-3,1-diylcarbonylimino)]dinaphthalene-1,3,5-trisulfonic acid
-
-
8,8'-[carbonylbis(iminobenzene-3,1-diylcarbonylimino)]dinaphthalene-1,3,5-trisulfonic acid
-
-
ATP
-
reaction at the U-incorporation site is inhibited with inhibition constant 1.09 mM, reaction at the G-incorporation site is inhibited with inhibition constant 1.25 mM, reaction at the C-incorporation site is inhibited with inhibition constant 1.48 mM
aurintricarboxylic acid
-
inhibits by competing with the template for binding to the enzyme, does not inhibit the elongation of preinitiated RNA chains
beta-D-2'-alpha-deoxy-2'-beta-fluoro-2'-C-methyluridine-5'-triphosphate
-
causes chain termination after incorporation into nascent RNA
beta-D-2'-alpha-deoxy-2'-beta-fluoro-2'-C-methyluridine-5'-triphosphate
causes chain termination after incorporation into nascent RNA
beta-D-2'-beta-C-ethynyluridine-5'-triphosphate
-
causes chain termination after incorporation into nascent RNA
beta-D-2'-beta-C-ethynyluridine-5'-triphosphate
causes chain termination after incorporation into nascent RNA
beta-D-2'-beta-C-methyluridine-5'-triphosphate
-
causes chain termination after incorporation into nascent RNA
beta-D-2'-beta-C-methyluridine-5'-triphosphate
causes chain termination after incorporation into nascent RNA
CTP
-
reaction at the A-incorporation site is inhibited with inhibition constants of 2.7 mM
favipiravir
unusually high nucleotide incorporation rates and high error rates of SARS-CoV RNA-dependent-RNA-polymerase allow facile insertion of Favipiravir into viral RNA, provoking C-to-U and G-to-A transitions in the already low cytosine content SARS-CoV-2 genome
galidesivir
binds to the enzyme (SARS-CoV-2 RdRp) with binding energies comparable to native nucleotides, potent drugs against SARS-CoV-2
gliotoxin
-
in presence of MnCl2 the IC50 value is 0.036 mM, in presence of Mn2+ the IC50 value is 0.202 mM
Mn2+
-
concentrations of 1.0 mM, 0.5 mM and 0.05 mM in the presence of Mg2+ inhibit activity by 75%, 50% and 25%, respectively
N'-[4-(2,5-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
N'-[4-(2,5-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
-
N'-[4-(2,5-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
-
N'-[4-(2,5-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
-
N'-[4-(2,6-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
N'-[4-(2,6-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
-
N'-[4-(2,6-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
-
N'-[4-(2,6-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
-
N,N-dimethyl-1-(1,3-diphenyltriazen-3-yl)-3-propanamine
-
N,N-dimethyl-1-[1-(4-nitrophenyl)-3-phenyltriazen-3-yl]-3-propanamine
-
N,N-dimethyl-1-[1-(4-nitrophenyl)-3-phenyltriazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-(4-nitrophenyl)-3-phenyltriazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-(4-nitrophenyl)-3-phenyltriazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-phenyl-3-(3-trifluoromethylphenyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-phenyl-3-(3-trifluoromethylphenyl)triazen-3-yl]-3-propanamine
-
N,N-dimethyl-1-[1-phenyl-3-(3-trifluoromethylphenyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-phenyl-3-(3-trifluoromethylphenyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-phenyl-3-(3-trifluoromethylphenyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-phenyl-3-(3-trifluoromethylphenyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-phenyl-3-(3-trifluoromethylphenyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-phenyl-3-(3-trifluoromethylphenyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-phenyl-3-(3-trifluoromethylphenyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[1-phenyl-3-(3-trifluoromethylphenyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-1-[3-phenyl-1-(p-tolyl)triazen-3-yl]-3-propanamine
-
N,N-dimethyl-1-[3-phenyl-1-(p-tolyl)triazen-3-yl]-3-propanamine
-
-
N,N-dimethyl-N'-4-(4'-tolylazo)phenylpropane-1,3-diamine
-
N,N-dimethyl-N'-[4-(3-nitrophenylazo)phenyl]propane-1,3-diamine
-
N,N-dimethyl-N'-[4-(3-nitrophenylazo)phenyl]propane-1,3-diamine
-
-
N,N-dimethyl-N'-[4-(4-nitrophenylazo)phenyl]propane-1,3-diamine
-
N,N-dimethyl-N'-[4-(4-nitrophenylazo)phenyl]propane-1,3-diamine
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-phenyldiazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-phenyldiazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-phenyldiazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-phenyldiazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-phenyldiazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-phenyldiazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-phenyldiazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-phenyldiazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-phenyldiazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-phenyldiazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-[3-(trifluoromethyl)phenyl]diazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-[3-(trifluoromethyl)phenyl]diazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-[3-(trifluoromethyl)phenyl]diazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-[3-(trifluoromethyl)phenyl]diazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-[3-(trifluoromethyl)phenyl]diazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-[3-(trifluoromethyl)phenyl]diazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-[3-(trifluoromethyl)phenyl]diazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-[3-(trifluoromethyl)phenyl]diazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-[3-(trifluoromethyl)phenyl]diazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-4-[(E)-[3-(trifluoromethyl)phenyl]diazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
NaCl
tolerable at low concentrations, but inhibits at concentrations higher than 25 mM
NADPH
-
the inhibitor occupies the RNA template binding channel of Human enterovirus D68 enzyme (RdRp) with a binding pocket. Residues involved in the NADPH binding pocket of EV-D68 RdRp are highly conserved in RdRps of enteroviruses. The enzyme activity decreases when titrated with NADPH in vitro
remdesivir
high-affinity and consistent molecular interactions with specific active site residues that anchor remdemsivir within the binding pocket for efficient binding. These residues are Asp452, Thr456, Arg555, Thr556, Val557, Arg624, Thr680, Ser681, and Ser682. Remdesivir binding induces minimal individual amino acid perturbations, subtly interferes with deviations of C-alpha atoms, and restricts the systematic transition of SARS-CoV-2 RNA-dependent RNA polymerase from the buried hydrophobic region to the surface-exposed hydrophilic region. A pharmacophore model based on the observed high-affinity interactions with SARSCoV-2 virus RNA-dependent RNA polymerase is mapped, which showcase the crucial functional moieties of remdesivir and is subsequently employed for virtual screening
remdesivir
binds to the enzyme (SARS-CoV-2 RdRp) with binding energies comparable to native nucleotides, potent drugs against SARS-CoV-2
remdesivir
cryo-electron microscopy structure of the SARS-CoV-2 RNA-dependent RNA polymerase, both in the apo form at 2.8 A resolution and in complex with a 50-base template-primer RNA and remdesivir at 2.5 A resolution. The complex structure reveals that the partial double-stranded RNA template is inserted into the central channel of the RNA-dependent RNA polymerase, where remdesivir is covalently incorporated into the primer strand at the first replicated base pair, and terminates chain elongation
remdesivir
cryo-electron microscopy structure of COVID-19 virus full-length nsp12 in complex with cofactors nsp7 and nsp8 at 2.9 A resolution. A comparative analysis model shows how remdesivir binds to this polymerase
remdesivir triphosphate
-
remdesivir or its derivatives have the potential to become broad-spectrum antiviral agent effective against many RNA viruses
remdesivir triphosphate
the inhibitor causes a delayed chain termination at position i+3
remdesivir triphosphate
the inhibitor causes a delayed chain termination at position i+5
remdesivir triphosphate
-
remdesivir or its derivatives have the potential to become broad-spectrum antiviral agent effective against many RNA viruses
remdesivir triphosphate
the inhibitor causes a delayed chain termination at position i+3
remdesivir triphosphate
the structures of the enzyme in complex with RNA helical strands and remdesivir provide the structure details of RdRp inhibition by remdesivir. The inhibitor competes with the incorporation of nucleotide counterparts and inhibits transcription of viral RNA. The inhibition mechanism of remdesivir is a delayed chain termination of nascent viral RNA at i+3 position
remdesivir triphosphate
the inhibition mechanism of remdesivir triphosphate is inestigated through structural and kinetic analyses
remdesivir triphosphate
using pharmacophore models, three natural product hits SN00166900, SN00303170 and SN00359915 are identified which have lower binding energies than that of remdesivir triphosphate
remdesivir triphosphate
effective in combating COVID-19 because it is a better substrate than ATP for the viral RNA-dependent RNA polymerase
remdesivir triphosphate
remdesivir or its derivatives have the potential to become broad-spectrum antiviral agent effective against many RNA viruses
remdesivir triphosphate
-
remdesivir or its derivatives have the potential to become broad-spectrum antiviral agent effective against many RNA viruses
remdesivir triphosphate
-
remdesivir or its derivatives have the potential to become broad-spectrum antiviral agent effective against many RNA viruses
remdesivir triphosphate
the inhibitor causes a delayed chain termination at position i+5
remdesivir triphosphate
remdesivir or its derivatives have the potential to become broad-spectrum antiviral agent effective against many RNA viruses
ribavirin
binds to the enzyme (SARS-CoV-2 RdRp) with binding energies comparable to native nucleotides, potent drugs against SARS-CoV-2
RNase
-
RNAse A, 0.01 mg/ml, or Rnase T1, 0.002 mg/ml, inhibit the reaction by 90-95%
-
sofosbuvir
-
the clinical effectiveness of sofosbuvir is largely a function of being intractable to nucleotide-mediated excision compared with similar nucleoside analogs
sofosbuvir
the enzyme (RdRp) of the SARS-CoV-2 RNA virus represents the most optimal target for an antiviral drug. Linear amino acid sequence as well as molecule structure show the highest homology to RdRps of other positive-sense RNA viruses. It is highly predictable that an antiviral developed for an RNA virus with a genome of the same polarity (i.e. sofosbuvir for HCV) could have a higher inhibitory efficacy against the SARS-CoV-2, compared to antiviral developed for negative-sense RNA viruses
sofosbuvir
binds to the enzyme (SARS-CoV-2 RdRp) with binding energies comparable to native nucleotides, potent drugs against SARS-CoV-2
sofosbuvir triphosphate
sofosbuvir triphosphate is incorporated by SARS-CoV RNA-dependent RNA polymerase (RdRp), and blocks further incorporation by the polymerase. Sofosbuvir triphosphate is not incorporated by a host-like high-fidelity DNA polymerase
UTP
-
reaction at the A-incorporation site is inhibited with inhibition constants of 3.2 mM
[N,N-dimethyl-N'-(4-phenylazophenyl)]propane-1,3-diamine
-
additional information
-
RdRp inhibition and antiviral potencies of the inhibitor compounds, overview
-
additional information
RdRp inhibition and antiviral potencies of the inhibitor compounds, overview
-
additional information
-
RdRp inhibition and antiviral potencies of the inhibitor compounds, overview
-
additional information
-
the CSFC analogues 2-(2-furanyl)-N-(6-methyl-2-benzothiazolyl)-4-quinolinecarboxamide and 2-phenyl-N-(1-phenyl-1H-pyrazol-3-yl)-4-quinolinecarboxamide do not inhibit the in vitro activity of recombinant Bovine viral diarrhea virus RNA-dependent RNA polymerase but inhibit the activity of Bovine viral diarrhea virus replication complexes
-
additional information
-
activity is depressed by increasing monovalent ion concentrations
-
additional information
-
RdRp inhibition and antiviral potencies of the inhibitor compounds, overview
-
additional information
-
RdRp inhibition and antiviral potencies of the inhibitor compounds, overview
-
additional information
-
RdRp inhibition and antiviral potencies of the inhibitor compounds, overview
-
additional information
-
structure-based drug design of potent non-nucleoside inhibitors of Dengue viral RNA-dependent RNA polymerase, -ray-based fragment screening, overview. A biphenyl acetic acid fragment 3 binds in the palm subdomain of RdRp, 1000fold improvement in potency in vitro and acquired antidengue activity against all four serotypes with low micromolar EC50 in cell-based assays
-
additional information
-
activity is lowered at ionic strength of 0.1
-
additional information
-
inhibition of NS5B activity by RNA template exhibits characteristics of substrate inhibition, suggesting the template binds to a secondary site on the enzyme forming an inactive complex, poly(A) behaves like a competitive inhibitor with respect to oligo (dT12) primer
-
additional information
mAbs 8B2 and 7G8 inhibit the primer-dependent RdRp activity, mAb 8B2 inhibits the elongation of RNA chains, while mAb 7G8 inhibitory effect is achieved through inhibition of multiple RNA synthesis initiations
-
additional information
-
mAbs 8B2 and 7G8 inhibit the primer-dependent RdRp activity, mAb 8B2 inhibits the elongation of RNA chains, while mAb 7G8 inhibitory effect is achieved through inhibition of multiple RNA synthesis initiations
-
additional information
inhibitor efficiency with wild-type and mutant enzymes, overview
-
additional information
-
inhibitor efficiency with wild-type and mutant enzymes, overview
-
additional information
5,5- and 6,6-dialkyl-5,6-dihydro-1H-pyridin-2-ones as potent inhibitors of HCV NS5B polymerase, overview
-
additional information
-
5,5- and 6,6-dialkyl-5,6-dihydro-1H-pyridin-2-ones as potent inhibitors of HCV NS5B polymerase, overview
-
additional information
reduction of NS5B activity by co-expression of an NS5B mRNA-cleaving DNAzyme in Hep-G2 cells
-
additional information
-
reduction of NS5B activity by co-expression of an NS5B mRNA-cleaving DNAzyme in Hep-G2 cells
-
additional information
-
PRK2 inhibitors can be antiviral drugs that act by suppressing HCV replication via inhibition of viral RNA polymerase phosphorylation
-
additional information
-
synthesis and evaluation of 4-thiazolidinones as non-nucleoside inhibitors of hepatitis C virus NS5B RNA-dependent RNA polymerase, docking study and molecular modelling, overview
-
additional information
-
non-nucleoside analogue inhibitors are being developed as part of a multidrug regiment to treat hepatitis C viral infections. Particularly promising are inhibitors that bind to the surface of the thumb domain of the viral RNA-dependent RNA polymerase. Kinetic analysis shows that non-nucleoside inhibitors binding to thumb site-2 (NNI2) do not block initiation or elongation of RNA synthesis, rather, they block the transition from the initiation to elongation, which is thought to proceed with significant structural rearrangement of the enzyme-RNA complex. Mapping of the effect of three NNI2 inhibitors on the conformational dynamics of the enzyme using hydrogen/deuterium exchange kinetics, overview. NNI2 inhibitors act through long range allosteric effects, revealing important conformational changes underlying normal polymerase function. Losses in conformational dynamics upon binding of NNI2s is correlated with inhibitor potency
-
additional information
-
RdRp inhibition and antiviral potencies of the inhibitor compounds, overview
-
additional information
-
RdRp inhibition and antiviral potencies of the inhibitor compounds, overview
-
additional information
-
inhibition of the assembly of the viral nucleoprotein, by RuvB-like protein 2, RBL2, and subsequent inhibition of the formation of the viral ribonucleoprotein complex inhibits viral RNA replication, overview
-
additional information
La France isometric virus
-
the enzyme is resistant to inhibitors of DNA-dependent RNA polymerase activity: actinomycin D, alpha-amanitin and rifampin
-
additional information
-
MNV-1 replication is insensitive to the fungal metabolite brefeldin A and consistently does not appear to recruit coatomer protein complex I, COPI, or COPII component proteins during replication
-
additional information
-
some pseudogene-derived siRNAs may be implicated in repressing pseudogene transcription involving RDR2
-
additional information
-
RdRp inhibition and antiviral potencies of the inhibitor compounds, overview
-
additional information
-
RdRp inhibition and antiviral potencies of the inhibitor compounds, overview
-
additional information
not sensitive to actinomycin D
-
additional information
MN908947
the high sequence conservation between SARS-CoV RNA-dependent RNA polymerase (RdRp) and SARS-CoV-2 RNA polymerase makes it very likely that any potent agents developed for the SARS-CoV RdRp will exhibit equal potency and efficacy on the SARS-CoV-2 enzyme
-
additional information
-
the high sequence conservation between SARS-CoV RNA-dependent RNA polymerase (RdRp) and SARS-CoV-2 RNA polymerase makes it very likely that any potent agents developed for the SARS-CoV RdRp will exhibit equal potency and efficacy on the SARS-CoV-2 enzyme
-
additional information
cryo-electron microscopy structure of COVID-19 virus full-length nsp12 in complex with cofactors nsp7 and nsp8 at 2.9 A resolution provides a basis for the design of new antiviral therapeutics that target viral RNA-dependent RNA polymerase
-
additional information
-
cryo-electron microscopy structure of COVID-19 virus full-length nsp12 in complex with cofactors nsp7 and nsp8 at 2.9 A resolution provides a basis for the design of new antiviral therapeutics that target viral RNA-dependent RNA polymerase
-
additional information
the high sequence conservation between SARS-CoV RNA-dependent RNA polymerase (RdRp) and SARS-CoV-2 RNA polymerase makes it very likely that any potent agents developed for the SARS-CoV RdRp will exhibit equal potency and efficacy on the SARS-CoV-2 enzyme
-
additional information
-
shRNAs expressing plasmids (pEGFP-U6/P1 and pEGFP-U6/P2) are capable of protecting cells against transmissible gastroenteritis virus invasion with very high specificity and efficiency against RdRp gene
-
additional information
-
the 5'-cap inhibits the (-)-strand RNA synthesis from the 3'-fold-back structure of (+)-strand RNA template without affecting the de novo synthesis of RNA
-
additional information
-
RdRp inhibition and antiviral potencies of the inhibitor compounds, overview
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Foot-and-Mouth disease virus 3B1
-
acts as primer for RNA synthesis by RNA-dependent RNA polymerase. To act as the primer for positive-strand RNA synthesis, the peptide has to be uridylated to form VpgpU(pU). This reaction is achieved by the RNA-dependent RNA polymerase in the presence of the 3CD precursor plus an internal RNA sequence termed a cis-acting replication element, cre
-
Foot-and-Mouth disease virus 3B2
-
acts as primer for RNA synthesis by RNA-dependent RNA polymerase. To act as the primer for positive-strand RNA synthesis, the peptide has to be uridylated to form VpgpU(pU). This reaction is achieved by the RNA-dependent RNA polymerase in the presence of the 3CD precursor plus an internal RNA sequence termed a cis-acting replication element, cre
-
Foot-and-Mouth disease virus 3B3
-
acts as primer for RNA synthesis by RNA-dependent RNA polymerase. To act as the primer for positive-strand RNA synthesis, the peptide has to be uridylated to form VpgpU(pU). This reaction is achieved by the RNA-dependent RNA polymerase in the presence of the 3CD precursor plus an internal RNA sequence termed a cis-acting replication element, cre
-
host factor
-
hexameric host-coded protein of 12500 Da subunits is required for in vitro Qbeta RNA replication
-
L-protein
the intact L protein is essential for enzyme (RdRP) activity and optimal RNA binding. In truncated L protein constructs, enzyme activity is abrogated due to their deficiency in RNA template binding
-
nsp7
the nsp12 (RdRp) catalyzes the synthesis of a complementary RNA strand using the virus RNA template with the assistance of nsp7 and nsp8 as cofactors
-
nsp8
the nsp12 (RdRp) catalyzes the synthesis of a complementary RNA strand using the virus RNA template with the assistance of nsp7 and nsp8 as cofactors
-
phosphoprotein P
-
P is essential for RNA-dependent RNA polymerase function as cofactor. The amino terminus of P is essential for its function in a minireplicon assay. It binds to STAT1 and inhibits interferon-induced Tyr phosphorylation of STAT1, which is not required for P polymerase cofactor function, since mutations in the STAT1 binding motif of P, e.g. G121E, do not affect RNA polymerase function, but abrogate STAT1 inhibition, overview. The gene for NiV P encodes functions that sequester inactive STAT1 in the nucleus, preventing its activation and suggest that the W protein is the dominant inhibitor of STAT1 in NiV-infected cells
-
polypeptide Vpg
-
serves as a primer for addition of the first nucleotide during synthesis of both positive and negative strands. Efficiency and specificity of Vpg uridylylation by picornavirus polymerases is greatly influenced by allosteric effects of ligand binding that are likely to be relevant during viral replicative cyle
-
RanBP5
-
a member of importin beta family, required for PB1/PA heterodimer import into the nucleus, where the active heterotrimer of the enzyme is formed
-
Sodium diethyldithiocarbamate
-
5 mM, great stimulation of template-dependent activity and to a lesser extent template-independent activity
viral protein P10
requirement of the interaction between RNA-dependent RNA polymerase (RdRp) and viral protein P10 via the intrinsically disordered C-terminal domain of RdRp in viral replication and progression of infection in vivo
-
VpgpU(pU)
-
Foot-and-Mouth disease virus 3B peptides acts as primers for RNA synthesis by RNA-dependent RNA polymerase. To act as the primer for positive-strand RNA synthesis, the peptides have to be uridylated to form VPgpU(pU). This reaction is achieved by the RNA-dependent RNA polymerase in the presence of the 3CD precursor plus an internal RNA sequence termed a cis-acting replication element, cre
-
GTP
required for de novo (primer-independent) initiation
GTP
flaviviral RdRps require high concentrations of the second incoming nucleotide GTP to catalyze de novo template-dependent RNA synthesis. GTP stimulates de novo RNA synthesis by RdRp from Japanese encephalitis virus
RNA
-
2-10fold stimulation with the addition of various RNA templates. CCMV and CPMV RNA produces the greatest stimulation. TMV RNA also acts as a template, but with much less efficiency
additional information
-
the HCV replication reaction in vitro is stimulated by the protein NS5A in a template-specific manner
-
additional information
RdRp is induced by fungal infection of Rhizoctonia solani
-
additional information
-
RdRp is induced by fungal infection of Rhizoctonia solani
-
additional information
-
RdRp phosphorylation by PRK2 is required for activation and RNA replication
-
additional information
-
the HCV replication reaction in vitro is stimulated by the protein NS5A in a template-specific manner
-
additional information
-
the HCV replication reaction in vitro is stimulated by the protein NS5A in a template-specific manner
-
additional information
the HCV replication reaction in vitro is stimulated by the protein NS5A in a template-specific manner
-
additional information
-
The Nicotiana benthamiana canonical 9-zinc finger (ZF) transcription factor IIIA (TFIIIA-9ZF) as well as its variant TFIIIA-7ZF both interact with (+)-PSTVd, but only TFIIIA-7ZF interacts with (-)-PSTVd. TFIIIA-7ZF is found in the nucleoplasm and nucleolus, in contrast to the strictly nucleolar localization of TFIIIA-9ZF. Overexpression of TFIIIA-7ZF enhances PSTVd replication in planta, the land plant-specific transcription factor directly enhances transcription of a pathogenic noncoding RNA template by DNA-dependent RNA polymerase II. TFIIIA-7ZF is a cellular transcription factor that acts in DdRP-catalyzed RNA-templated transcription, highlighting both the extraordinary evolutionary adaptation of viroids and the potential of DdRPs for a broader role in cellular processes. Subcellular localization of TFIIIA-7ZF and TFIIIA-9ZF in Nicotiana benthamiana leaves infected by PSTVd, overview
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0011
RNAn
30°C, pH 7.5, RNA template with the first 25 nucleotides from the TrC (Trailer complement) sequence
0.0029
ATP
-
pH 7.5, 23°C, reaction with heteropolymeric template T500, C-terminally truncated enzyme form NS5B(DELTA21)
0.0085
ATP
30°C, pH 7.5, cosubstrate: RNA template with the first 25 nucleotides from the TrC (Trailer complement) sequence
0.00018
CTP
30°C, pH 7.5, cosubstrate: RNA template with the first 25 nucleotides from the TrC (Trailer complement) sequence
0.0006
CTP
-
pH 7.5, 23°C, reaction with heteropolymeric template T500, C-terminally truncated enzyme form NS5B(DELTA21)
0.00019
GTP
-
pH 7.5, 23°C, deletion mutant DELTAC21, poly(C)-oligo(G)18 as template
0.0014
GTP
-
pH 7.5, 23°C, reaction with heteropolymeric template T500, C-terminally truncated enzyme form NS5B(DELTA21)
0.0027
GTP
30°C, pH 7.5, cosubstrate: RNA template with the first 25 nucleotides from the TrC (Trailer complement) sequence
0.0035
GTP
-
pH 8.2, 25°C, enzyme form DELTA21 that lacks the C-terminal 21 hydrophobic residues
0.0000089
remdesivir triphosphate
pH 8, 30°C
0.053
remdesivir triphosphate
pH 7.0, 37°C
14.6
rGTP
Michaelis-Menten kinetic model, pH 7.5, 30°C, recombinant enzyme
19.1
rGTP
substrate inhibition, pH 7.5, 30°C, recombinant enzyme
0.0006
UTP
-
pH 7.5, 23°C, reaction with heteropolymeric template T500, C-terminally truncated enzyme form NS5B(DELTA21)
0.0014
UTP
30°C, pH 7.5, cosubstrate: RNA template with the first 25 nucleotides from the TrC (Trailer complement) sequence
0.0054
UTP
-
pH 7.5, 23°C, deletion mutant DELTAC21, poly(A)-oligo(U)18 as template
0.0057
UTP
-
pH 7.5, 23°C, C-terminally truncated enzyme form NS5B(DELTA21), reaction with dT16/poly(rA)
additional information
additional information
-
the Km-value for the equimolar mixture of ATP, CTP and GTP in presence of 0.02 mM UTP is about 0.035 mM
-
additional information
additional information
-
effect of Mg2+ and Mn2+ on the Km-value for polyC/oligoG and polyA/oligodT
-
additional information
additional information
-
kinetic analysis of the recombinant enzyme complex
-
additional information
additional information
Michaelis-Menten kinetic analysis
-
additional information
additional information
-
Michaelis-Menten kinetic analysis
-
additional information
additional information
dissociation constants for the interaction of jRdRp with RNA in the presence/absence of NTPs and Mn2+
-
additional information
additional information
-
dissociation constants for the interaction of jRdRp with RNA in the presence/absence of NTPs and Mn2+
-
additional information
additional information
steady-state kinetics analysis of non-tagged DENV-2 RdRp in the presence of constant poly(rC) and Mg2+ concentrations
-
additional information
additional information
-
steady-state kinetics analysis of non-tagged DENV-2 RdRp in the presence of constant poly(rC) and Mg2+ concentrations
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
680
remdesivir triphosphate
pH 7.0, 37°C
additional information
additional information
-
the enzyme is able to copy long heteropolymeric templates with an elongation rate of 150-200 nucleotides per min at 22°C
-
0.000105
ATP
-
pH 7.5, 23°C, reaction with heteropolymeric template T500, C-terminally truncated enzyme form NS5B(DELTA21)
0.000133
CTP
-
pH 7.5, 23°C, reaction with heteropolymeric template T500, C-terminally truncated enzyme form NS5B(DELTA21)
0.000383
GTP
-
pH 7.5, 23°C, reaction with heteropolymeric template T500, C-terminally truncated enzyme form NS5B(DELTA21)
0.00108
GTP
-
pH 7.5, 23°C, deletion mutant DELTAC21, poly(C)-oligo(G)18 as template
0.000167
UTP
-
pH 7.5, 23°C, reaction with heteropolymeric template T500, C-terminally truncated enzyme form NS5B(DELTA21)
0.00583
UTP
-
pH 7.5, 23°C, deletion mutant DELTAC21, poly(A)-oligo(U)18 as template
0.0272
UTP
-
pH 7.5, 23°C, C-terminally truncated enzyme form NS5B(DELTA21), reaction with dT16/poly(rA)
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00129
remdesivir triphosphate
pH 7.0, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.1
rGTP
substrate inhibition, pH 7.5, 30°C, recombinant enzyme
additional information
additional information
-
kinetics of inhibition of VPg uridylylation, overview
-
0.000034
beta-D-2'-deoxy-2'-fluoro-2'-C-methylcytidine
clinical isolate GT-1a
0.00004
beta-D-2'-deoxy-2'-fluoro-2'-C-methylcytidine
clinical isolate GT-1b
0.000059
beta-D-2'-deoxy-2'-fluoro-2'-C-methylcytidine 5'-triphosphate
-
wild type enzyme, with 5 mM MgCl2, and 2 mM dithiothreitol in 50 mM HEPES buffer, pH 7.5
0.00031
beta-D-2'-deoxy-2'-fluoro-2'-C-methylcytidine 5'-triphosphate
-
mutant enzyme S282T, with 5 mM MgCl2, and 2 mM dithiothreitol in 50 mM HEPES buffer, pH 7.5
0.00022
beta-D-2'-deoxy-2'-fluoro-2'-C-methyluridine 5'-triphosphate
-
mutant enzyme S282T, with 5 mM MgCl2, and 2 mM dithiothreitol in 50 mM HEPES buffer, pH 7.5
0.00042
beta-D-2'-deoxy-2'-fluoro-2'-C-methyluridine 5'-triphosphate
-
wild type enzyme, with 5 mM MgCl2, and 2 mM dithiothreitol in 50 mM HEPES buffer, pH 7.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000055
(2E)-3-(4-[[(1-[[(1-cyclohexyl-2-furan-3-yl-1H-benzimidazol-5-yl)carbonyl]amino]cyclobutyl)carbonyl]amino]phenyl)prop-2-enoic acid
Hepacivirus C
-
-
0.0013
(2E)-3-(4-[[(2-cyclohexyl-3-phenylquinoxalin-6-yl)carbonyl]amino]phenyl)prop-2-enoic acid
Hepacivirus C
-
0.00069 - 0.0069
(2E)-3-[4-([[1-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
0.0012
(2E)-3-[4-([[1-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclopentyl]carbonyl]amino)phenyl]prop-2-enoic acid
Hepacivirus C
-
0.0051
(2E)-3-[4-([[1-([[2-cyclohexyl-3-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
Hepacivirus C
-
0.0013
(2E)-3-[4-([[1-([[3-cyclohexyl-2-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
Hepacivirus C
-
0.017
(2E)-3-[4-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)phenyl]prop-2-enoic acid
Hepacivirus C
-
0.0041
(2E)-3-[4-([[2-cyclohexyl-3-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)phenyl]prop-2-enoic acid
Hepacivirus C
-
0.0046
(2E)-3-[4-([[3-cyclohexyl-2-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)phenyl]prop-2-enoic acid
Hepacivirus C
-
0.003
(2S)-(((5Z)-5-[(5-ethyl-2-furyl)methylene]-4-oxo-4,5-dihydro-1,3-thiazol-2-yl)amino)(4-fluorophenyl)acetic acid
Hepacivirus C
-
-
0.0031
(2S)-1-[(2-amino-4-chloro-5-methylphenyl)sulfonyl]pyrrolidine-2-carboxylic acid
Hepacivirus C
-
-
0.00008
(2S)-1-[(3,4,5-trichloro-2-hydroxyphenyl)sulfonyl]pyrrolidine-2-carboxylic acid
Hepacivirus C
-
-
0.00077
(2S)-1-[(3,5-dichloro-2-hydroxyphenyl)sulfonyl]pyrrolidine-2-carboxylic acid
Hepacivirus C
-
-
0.0007
(2S)-2-[(2,4-dichlorobenzoyl)(3-nitrobenzyl)amino]-3-phenylpropanoic acid
Hepacivirus C
-
-
0.0038
(2S,4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)pyrrolidine-2,4-dicarboxylic acid
0.0011
(2S,4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-5-thiophen-2-ylpyrrolidine-2,4-dicarboxylic acid
Hepacivirus C
-
-
0.00019 - 0.02
(2S,4S,5R)-2-(2-methylpropyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]pyrrolidine-2,4-dicarboxylic acid
0.02
(2S,4S,5R)-2-isobutyl-5-(thiophen-2-yl)-1-(4-(trifluoromethyl)benzoyl)pyrrolidine-2,4-dicarboxylic acid
Hepacivirus C
-
full-length enzyme
0.0051
(2Z)-3-[4-([[1-([[2-cyclohexyl-3-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
Hepacivirus C
-
0.0013
(2Z)-3-[4-([[1-([[3-cyclohexyl-2-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
Hepacivirus C
-
0.0032
(4R,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(ethoxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
-
0.001
(4R,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(hydroxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
-
0.000014
(4S,5R)-1-[(3-bromo-4-tert-butylphenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
-
0.00002
(4S,5R)-1-[(4-tert-butyl-3-chlorophenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
-
0.00043
(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(ethoxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
-
0.00073
(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(hydroxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
-
0.00044
(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(methoxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
-
0.000005
(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
-
0.000019
(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-methoxy-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
-
0.0031
(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-4-(phenylcarbamoyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
full-length enzyme
0.00423
(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-4-[[(2-phenylethoxy)sulfinyl]carbamoyl]-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
full-length enzyme
0.022
(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-4-(methylcarbamoyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
full-length enzyme
0.00097 - 0.0044
(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
0.068
(4S,5R)-4-(benzylcarbamoyl)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
full-length enzyme
0.00315
(4S,5R)-4-[[(benzyloxy)sulfinyl]carbamoyl]-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
full-length enzyme
0.03
(5,7-difluoro-1-propyl-2,3,4,9-tetrahydro-1H-carbazol-1-yl)acetic acid
Hepacivirus C
-
-
0.0023
(5,8-dicyano-1-propyl-2,3,4,9-tetrahydro-1H-carbazol-1-yl)acetic acid
Hepacivirus C
-
-
0.000055
(5-cyano-6-fluoro-8-methyl-1-propyl-3,4-dihydro-1H-[1]benzothieno[2,3-c]pyran-1-yl)acetic acid
Hepacivirus C
-
-
0.0021
(5-cyano-8-fluoro-1-propyl-2,3,4,9-tetrahydro-1H-carbazol-1-yl)acetic acid
Hepacivirus C
-
-
0.00057
(5-cyano-8-methyl-1-propyl-1,3,4,9-tetrahydropyrano[3,4-b]indol-1-yl)acetic acid
Hepacivirus C
-
-
0.0021
(5-cyano-8-methyl-1-propyl-2,3,4,9-tetrahydro-1H-carbazol-1-yl)acetic acid
Hepacivirus C
-
-
0.0023
(5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(methoxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
-
0.0004
1,3-bis-(4-chloro-1H(3H)-triazolo[4,5-g]quinoline)propan-2-one
Bovine viral diarrhea virus 1
-
pH 7.0, 22°C
0.00001
1-(2-cyclopropylethyl)-3-(1,1-dioxido-4H-1,2,4-benzothiadiazin-3-yl)-6-fluoro-4-hydroxyquinolin-2(1H)-one
Hepacivirus C
-
-
0.00011 - 0.00028
1-(cyclobutylamino)-3-(1,1-dioxido-4H-1,2,4-benzothiadiazin-3-yl)-4-hydroxyquinolin-2(1H)-one
0.001
1-cyclohexyl-2-(2-fluoro-4-[[2-(3-oxomorpholin-4-yl)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.00015
1-cyclohexyl-2-(2-fluoro-4-[[2-(4-hydroxypiperidin-1-yl)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.00013
1-cyclohexyl-2-(2-fluoro-4-[[2-(4-methylpiperazin-1-yl)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.00041
1-cyclohexyl-2-(2-fluoro-4-[[2-methoxy-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.00009
1-cyclohexyl-2-(2-fluoro-4-[[2-morpholin-4-yl-5-(2-oxopiperidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.000066
1-cyclohexyl-2-(2-fluoro-4-[[2-morpholin-4-yl-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.00015
1-cyclohexyl-2-(2-fluoro-4-[[5-(2-oxopyrrolidin-1-yl)-2-piperidin-1-ylbenzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.00003
1-cyclohexyl-2-(4-[[2-morpholin-4-yl-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-indole-5-carboxylic acid
Hepacivirus C
-
-
0.00064
1-cyclohexyl-2-(4-[[4-(dimethylcarbamoyl)phenyl](phenyl)methoxy]-2-fluorophenyl)-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.000071
1-cyclohexyl-2-(4-[[5-(1,1-dioxidoisothiazolidin-2-yl)-2-morpholin-4-ylbenzyl]oxy]-2-fluorophenyl)-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.000068
1-cyclohexyl-2-(4-[[5-(dimethylcarbamoyl)-2-morpholin-4-ylbenzyl]oxy]-2-fluorophenyl)-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.0003
1-cyclohexyl-2-furan-3-yl-N-[(1S)-2-(5-hydroxy-1H-indol-3-yl)-1-(1,3-thiazol-4-yl)ethyl]-1H-benzimidazole-5-carboxamide
Hepacivirus C
-
-
0.000048
1-cyclohexyl-2-[2-fluoro-4-([5-[(1-methylethyl)carbamoyl]-2-morpholin-4-ylbenzyl]oxy)phenyl]-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.000099
1-cyclohexyl-2-[2-fluoro-4-([5-[(methoxyacetyl)(methyl)amino]-2-morpholin-4-ylbenzyl]oxy)phenyl]-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.00013
1-cyclohexyl-2-[2-fluoro-4-[(2-morpholin-4-ylbenzyl)oxy]phenyl]-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.00014
12-cyclohexylindolo[1,2-c][1,3]benzoxazine-9-carboxylic acid
Hepacivirus C
-
dihedral angle between the C2-aryl group and the indole ring is 24°
0.0000072
13-cyclohexyl-3-[[2-morpholin-4-yl-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]-6,7-dihydroindolo[1,2-d][1,4]benzoxazepine-10-carboxylic acid
Hepacivirus C
-
-
0.000009
13-cyclohexyl-5-(2-piperidin-1-ylethyl)-6,7-dihydro-5H-indolo[1,2-d][1,4]benzodiazepine-10-carboxylic acid
Hepacivirus C
-
-
0.000021
13-cyclohexyl-6,7-dihydro-5H-indolo[1,2-d][1,4]benzodiazepine-10-carboxylic acid
Hepacivirus C
-
dihedral angle between the C2-aryl group and the indole ring is 46°
0.000077
13-cyclohexyl-6,7-dihydro-5H-indolo[2,1-a][2]benzazepine-10-carboxylic acid
Hepacivirus C
-
dihedral angle between the C2-aryl group and the indole ring is 53°
0.000038
13-cyclohexyl-6,7-dihydroindolo[1,2-d][1,4]benzothiazepine-10-carboxylic acid
Hepacivirus C
-
dihedral angle between the C2-aryl group and the indole ring is 56°
0.000026
13-cyclohexyl-6,7-dihydroindolo[1,2-d][1,4]benzoxazepine-10-carboxylic acid
Hepacivirus C
-
dihedral angle between the C2-aryl group and the indole ring is 43°
0.000047
14-cyclohexyl-7,8-dihydro-6H-indolo[1,2-e][1,5]benzoxazocine-11-carboxylic acid
Hepacivirus C
-
dihedral angle between the C2-aryl group and the indole ring is 61°
0.0159
2'-C-ethynyl-2'-fluoro-uridine triphosphate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.00065
2'-C-ethynyl-4'-fluoro-uridine triphosphate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0016
2'-C-ethynyl-uridine triphosphate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0066
2'-C-methyl-4'-fluoro-uridine triphosphate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.005
2'-C-methyl-uridine triphosphate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0028
2'-C-propynyl-4'-fluoro-uridine triphosphate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.002
2'-C-propynyl-uridine triphosphate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0015
2-(3-[[(2-chlorobenzyl)carbamoyl]amino]thiophen-2-yl)-5,6-dihydroxypyrimidine-4-carboxylic acid
Hepacivirus C
-
-
0.00012
2-(4-benzylphenyl)-3-cyclohexyl-1-methyl-1H-indole-6-carboxylic acid
Hepacivirus C
-
-
0.000009
2-(4-chlorophenyl)-3-cyclohexyl-1-[2-[4-(diethylamino)piperidin-1-yl]-2-oxoethyl]-1H-indole-6-carboxylic acid
Hepacivirus C
-
-
0.00011
2-(4-[[2-(4-acetylpiperazin-1-yl)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]-2-fluorophenyl)-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.00018
2-(4-[[2-(4-carboxypiperidin-1-yl)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]-2-fluorophenyl)-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.00023
2-(4-[[2-(4-chlorophenoxy)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]-2-fluorophenyl)-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.000017
2-(4-[[4'-chloro-4-(2-oxopyrrolidin-1-yl)biphenyl-2-yl]methoxy]-2-fluorophenyl)-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.00007
2-(4-[[5-(acetylamino)-2-morpholin-4-ylbenzyl]oxy]-2-fluorophenyl)-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.000018
2-([3-[1-(2-cyclopropylethyl)-6-fluoro-4-hydroxy-2-oxo-1,2-dihydroquinolin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]oxy)acetamide
Hepacivirus C
-
-
0.000016 - 0.000046
2-([3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydro-1,8-naphthyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]oxy)acetamide
0.0001
2-amino-7-(2-C-methyl-beta-D-ribofuranosyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
Hepacivirus C
-
-
0.000036
2-[2-chloro-4-(2-[2-cyclopentyl-5-[(5,7-dimethyl[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)methyl]-4-hydroxy-6-oxo-3,6-dihydro-2H-pyran-2-yl]ethyl)phenyl]-2-methylpropanenitrile
Hepacivirus C
-
wild type enzyme
0.000004
2-[4-(2-[2-cyclopentyl-5-[(5,7-dimethyl[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)methyl]-4-hydroxy-6-oxo-3,6-dihydro-2H-pyran-2-yl]ethyl)-2-fluorophenyl]-2-methylpropanenitrile
Hepacivirus C
-
wild type enzyme
0.0032
2-[4-(benzyloxy)phenyl]-1-cyclopentyl-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.000006
2-[4-(benzyloxy)phenyl]-3-cyclohexyl-1-[2-(dimethylamino)-2-oxoethyl]-1H-indole-6-carboxylic acid
Hepacivirus C
-
-
0.000014
2-[4-([4'-chloro-4-[(4-hydroxypiperidin-1-yl)carbonyl]biphenyl-2-yl]methoxy)-2-fluorophenyl]-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.000042
2-[4-([5-[acetyl(1-methylethyl)amino]-2-morpholin-4-ylbenzyl]oxy)-2-fluorophenyl]-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.000051
2-[4-([5-[acetyl(methyl)amino]-2-morpholin-4-ylbenzyl]oxy)-2-fluorophenyl]-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.0001
2-[4-[(5-chloro-2-morpholin-4-ylbenzyl)oxy]-2-fluorophenyl]-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
Hepacivirus C
-
-
0.000032
3-(1,1-dioxido-4H-1,2,4-benzothiadiazin-3-yl)-4-hydroxy-1-(3-methylbutyl)quinolin-2(1H)-one
Hepacivirus C
-
-
0.000017
3-(benzyloxy)-13-cyclohexyl-6,7-dihydroindolo[1,2-d][1,4]benzoxazepine-10-carboxylic acid
Hepacivirus C
-
-
0.008
3-(isopropyl[(4-methylphenyl)sulfonyl]amino)-5-phenylthiophene-2-carboxylic acid
Hepacivirus C
-
-
0.0014
3-([(2,4-dimethylphenyl)sulfonyl]amino)-5-phenylthiophene-2-carboxylic acid
Hepacivirus C
-
-
0.012
3-([(4-chloro-2,5-dimethylphenyl)sulfonyl]amino)-5-phenylthiophene-2-carboxamide
Hepacivirus C
-
-
0.0012
3-allyl-5,8-dichloro-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
Hepacivirus C
-
-
0.0145
3-allyl-8-cyano-5-fluoro-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
Hepacivirus C
-
-
0.011
3-allyl-8-cyano-5-methyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
Hepacivirus C
-
-
0.0063
3-allyl-8-cyano-7-fluoro-5-methyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
Hepacivirus C
-
-
0.0012
3-benzyl-5-chloropyrido[3,2-g]quinoxalin-2(1H)-one
Bovine viral diarrhea virus 1
-
pH 7.0, 22°C
0.0019
3-butyl-5,8-dichloro-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
Hepacivirus C
-
-
0.0054
3-butyl-8-cyano-5-fluoro-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
Hepacivirus C
-
-
0.0046
3-butyl-8-cyano-5-methyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
Hepacivirus C
-
-
0.0015
3-butyl-8-cyano-7-fluoro-5-methyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
Hepacivirus C
-
-
0.00003
3-cyclohexyl-1-(2-oxo-2-piperidin-1-ylethyl)-2-phenyl-1H-indole-6-carboxylic acid
Hepacivirus C
-
-
0.000018
3-cyclohexyl-1-(2-[methyl[(1-methylpiperidin-3-yl)methyl]amino]-2-oxoethyl)-2-phenyl-1H-indole-6-carboxylic acid
Hepacivirus C
-
-
0.0000072
3-cyclohexyl-1-methyl-2-(4-[[2-morpholin-4-yl-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-indole-6-carboxylic acid
Hepacivirus C
-
-
0.000018
3-cyclohexyl-1-[2-(dimethylamino)-2-oxoethyl]-2-(4-methoxyphenyl)-1H-indole-6-carboxylic acid
Hepacivirus C
-
-
0.00006
3-cyclohexyl-1-[2-(dimethylamino)-2-oxoethyl]-2-phenyl-1H-indole-6-carboxylic acid
Hepacivirus C
-
-
0.00032
3-cyclohexyl-1-[2-(dimethylamino)-2-oxoethyl]-2-phenyl-1H-pyrrolo[2,3-b]pyridine-6-carboxylic acid
Hepacivirus C
-
-
0.000015
3-cyclohexyl-2-furan-3-yl-1-[2-oxo-2-(4-pyrrolidin-1-ylpiperidin-1-yl)ethyl]-1H-indole-6-carboxylic acid
Hepacivirus C
-
-
0.0001
3-cyclohexyl-2-furan-3-yl-N-[(1S)-2-(5-hydroxy-1H-indol-3-yl)-1-(1,3-thiazol-4-yl)ethyl]-1-methyl-1H-indole-6-carboxamide
Hepacivirus C
-
-
0.003
3-oxo-3-[(2Z)-2-(3,4,5-trihydroxybenzylidene)hydrazino]propanoic acid
Hepacivirus C
-
-
0.00093
3-[(4-amino-2-tert-butyl-5-methylphenyl)sulfanyl]-6-cyclopentyl-4-hydroxy-6-[2-(4-hydroxyphenyl)ethyl]-5,6-dihydro-2H-pyran-2-one
Hepacivirus C
-
-
0.0015
3-[[(trans-4-methylcyclohexyl)carbonyl](1-methylethyl)amino]-5-phenylthiophene-2-carboxylic acid
Hepacivirus C
-
-
0.000019
3-[[4'-chloro-4-(2-oxopyrrolidin-1-yl)biphenyl-2-yl]methoxy]-13-cyclohexyl-6,7-dihydroindolo[1,2-d][1,4]benzoxazepine-10-carboxylic acid
Hepacivirus C
-
-
0.0021
4-methyl-N-((5Z)-5-[(5-methyl-2-furyl)methylene]-4-oxo-4,5-dihydro-1,3-thiazol-2-yl)benzenesulfonamide
Hepacivirus C
-
-
0.00003
5,6-dihydroxy-2-[4-(([(1-naphthylsulfonyl)amino]carbonyl)amino)-3-thienyl]pyrimidine-4-carboxylic acid
Hepacivirus C
-
-
0.0032
5,8-dichloro-1-propyl-2,3,4,9-tetrahydro-1H-carbazole-1-carboxylic acid
Hepacivirus C
-
-
0.00055 - 0.0021
5,8-dichloro-3-propyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
0.0032
5-(2-amino-2-oxoethoxy)-N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
Hepacivirus C
-
0.00044
5-(4-bromophenylmethylene)-3-(benzenesulfonylamino)-4-oxo-2-thionothiazolidine
Hepacivirus C
-
37°C, pH 7.5
0.00054
5-(4-chlorophenylmethylene)-3-(benzenesulfonylamino)-4-oxo-2-thionothiazolidine
Hepacivirus C
-
37°C, pH 7.5
0.00027
5-(4-cyanophenyl)-3-([(2-methylphenyl)sulfonyl]amino)thiophene-2-carboxylic acid
Hepacivirus C
-
-
0.0018
5-(4-[[(2-cyclohexyl-3-phenylquinoxalin-6-yl)carbonyl]amino]phenyl)furan-2-carboxylic acid
Hepacivirus C
-
0.0016
5-(4-[[(3-cyclohexyl-2-phenylquinoxalin-6-yl)carbonyl]amino]phenyl)furan-2-carboxylic acid
Hepacivirus C
-
0.000027
5-(carboxymethoxy)-N-[(1-cyclohexyl-2-furan-3-yl-1H-benzimidazol-5-yl)carbonyl]-L-tryptophan
Hepacivirus C
-
-
0.0059
5-([3,5-bis(trifluoromethyl)phenyl]amino)-3-hydroxyisothiazole-4-carbonitrile
Hepacivirus C
-
-
0.0052
5-azidomethyl-3-hydroxy-4-hydroxymethyl-pyridine-2-carboxylic acid hydroxyamide
Zika virus
-
30°C, pH 6.8
0.001
5-chloro-3-phenylpyrido[3,2-g]quinoxalin-2(1H)-one
Bovine viral diarrhea virus 1
-
pH 7.0, 22°C
0.01
5-cyano-8-fluoro-1-propyl-2,3,4,9-tetrahydro-1H-carbazole-1-carboxylic acid
Hepacivirus C
-
-
0.015
5-cyano-8-methyl-1-propyl-2,3,4,9-tetrahydro-1H-carbazole-1-carboxylic acid
Hepacivirus C
-
-
0.015
5-hydroxy-N-[[3-(3-methoxyphenyl)-2-(4-methoxyphenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
Hepacivirus C
-
0.0032
6-(2-amino-2-oxoethoxy)-N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
Hepacivirus C
-
0.00001
6-cyclohexyl-4-methyl-5-(4-[[2-morpholin-4-yl-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-4H-thieno[3,2-b]pyrrole-2-carboxylic acid
Hepacivirus C
-
-
0.00006
6-cyclohexyl-4-[2-(dimethylamino)-2-oxoethyl]-5-phenyl-4H-thieno[3,2-b]pyrrole-2-carboxylic acid
Hepacivirus C
-
-
0.000038
6-[2-(3-chloro-4-methoxyphenyl)ethyl]-6-cyclopentyl-4-hydroxy-3-[(4-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]-5,6-dihydro-2H-pyran-2-one
Hepacivirus C
-
-
0.00002
6-[2-(5-chloro-2,4-dimethoxyphenyl)ethyl]-6-cyclopentyl-3-[(5,7-dimethyl[1,2,4]triazolo[1,5-a]pyrimidin-2-yl)sulfanyl]-4-hydroxy-5,6-dihydro-2H-pyran-2-one
Hepacivirus C
-
wild type enzyme
0.00012
7-(2-C-methyl-beta-D-ribofuranosyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine
Hepacivirus C
-
-
0.0002
8,8'-[carbonylbis(imino-3,1-phenylene carbonylimino)]bis(1,3,5-naphthalene-trisulfonic acid)
Murine norovirus 1
pH and temperature not specified in the publication
0.0000715 - 0.00028
8,8'-[carbonylbis(iminobenzene-3,1-diylcarbonylimino)]dinaphthalene-1,3,5-trisulfonic acid
0.0058
8-chloro-1-propyl-5-(trifluoromethyl)-2,3,4,9-tetrahydro-1H-carbazole-1-carboxylic acid
Hepacivirus C
-
-
0.0081
8-cyano-5-fluoro-3-propyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
Hepacivirus C
-
-
0.0047
8-cyano-5-methyl-3-propyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
Hepacivirus C
-
-
0.0018
8-cyano-7-fluoro-5-methyl-3-propyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
Hepacivirus C
-
-
0.037
ethyl (2E)-3-[4-([[1-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoate
Hepacivirus C
-
0.1
ethyl (2E)-3-[4-([[1-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclopentyl]carbonyl]amino)phenyl]prop-2-enoate
Hepacivirus C
IC50 above 0.1 mM
0.1
ethyl (2E)-3-[4-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)phenyl]prop-2-enoate
Hepacivirus C
IC50 above 0.1 mM
0.0086
methyl 5-(2-amino-2-oxoethoxy)-N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophanate
Hepacivirus C
-
0.0086
methyl 6-(2-amino-2-oxoethoxy)-N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophanate
Hepacivirus C
-
0.026
methyl N-[(2,3-difuran-2-ylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophanate
Hepacivirus C
-
0.072
methyl N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophanate
Hepacivirus C
-
0.072
methyl N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-6-hydroxy-L-tryptophanate
Hepacivirus C
-
0.1
methyl N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-L-tryptophanate
Hepacivirus C
IC50 above 0.1 mM
0.1
methyl N-[(2,3-dipyridin-2-ylquinoxalin-6-yl)carbonyl]-L-tryptophanate
Hepacivirus C
IC50 above 0.1 mM
0.026
methyl N-[(2,3-ditetrahydrofuran-2-ylquinoxalin-6-yl)carbonyl]-6-hydroxy-L-tryptophanate
Hepacivirus C
-
0.1
methyl N-[(2,3-ditetrahydrofuran-2-ylquinoxalin-6-yl)carbonyl]-L-tryptophanate
Hepacivirus C
IC50 above 0.1 mM
0.1
methyl N-[[2,3-bis(3-methoxyphenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophanate
Hepacivirus C
IC50 above 0.1 mM
0.1
methyl N-[[2,3-bis(3-methoxyphenyl)quinoxalin-6-yl]carbonyl]-L-tryptophanate
Hepacivirus C
IC50 above 0.1 mM
0.1
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-(2-methoxy-2-oxoethoxy)-L-tryptophanate
Hepacivirus C
-
0.0055
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophanate
Hepacivirus C
-
0.053
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-[[(2E)-4-methoxy-4-oxobut-2-en-1-yl]oxy]-L-tryptophanate
Hepacivirus C
-
0.1
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-(2-methoxy-2-oxoethoxy)-L-tryptophanate
Hepacivirus C
-
0.0055
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophanate
Hepacivirus C
-
0.053
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-[[(2E)-4-methoxy-4-oxobut-2-en-1-yl]oxy]-L-tryptophanate
Hepacivirus C
-
0.1
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophanate
Hepacivirus C
IC50 above 0.1 mM
0.049
methyl N-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophanate
Hepacivirus C
-
0.049
methyl N-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophanate
Hepacivirus C
-
0.1
methyl N-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-L-tryptophanate
Hepacivirus C
IC50 above 0.1 mM
0.0199
N-(3-cyano-5,6-dihydro-4H-cyclopenta[b]thiophen-2-yl)-4-methyl-2-phenyl-1,3-thiazole-5-carboxamide
Rabbit hemorrhagic disease virus
pH 7.5, 30°C, recombinant enzyme
0.000067
N-(3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-5-[(1E)-pent-1-en-1-yl]-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl)methanesulfonamide
Hepacivirus C
-
-
0.000006
N-(3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-5-[(1E)-prop-1-en-1-yl]-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl)methanesulfonamide
Hepacivirus C
-
-
0.00048
N-(3-[4-hydroxy-5-[(E)-2-(4-methoxyphenyl)ethenyl]-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl)methanesulfonamide
Hepacivirus C
-
-
0.000406
N-(3-[5-[(1E)-3,3-dimethylbut-1-en-1-yl]-4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl)methanesulfonamide
Hepacivirus C
-
-
0.000046
N-[(13-cyclohexyl-6,7-dihydroindolo[1,2-d][1,4]benzoxazepin-10-yl)carbonyl]-2-methylalanine
Hepacivirus C
-
-
0.016
N-[(2,3-difuran-2-ylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophan
Hepacivirus C
-
0.011
N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-6-hydroxy-L-tryptophan
Hepacivirus C
-
0.1
N-[(2,3-dipyridin-2-ylquinoxalin-6-yl)carbonyl]-L-tryptophan
Hepacivirus C
IC50 above 0.1 mM
0.016
N-[(2,3-ditetrahydrofuran-2-ylquinoxalin-6-yl)carbonyl]-6-hydroxy-L-tryptophan
Hepacivirus C
-
0.033
N-[(2,3-ditetrahydrofuran-2-ylquinoxalin-6-yl)carbonyl]-L-tryptophan
Hepacivirus C
-
0.0017
N-[(2,4-dichlorophenyl)carbonyl]-N-[3-(trifluoromethyl)benzyl]-L-phenylalanine
Hepacivirus C
-
-
0.005
N-[(2-cyclohexyl-3-phenylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophan
Hepacivirus C
-
0.0037
N-[(2-cyclohexyl-3-phenylquinoxalin-6-yl)carbonyl]-L-tryptophan
Hepacivirus C
-
0.0006
N-[(3-cyclohexyl-2-phenylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophan
Hepacivirus C
-
0.0018
N-[(3-cyclohexyl-2-phenylquinoxalin-6-yl)carbonyl]-L-tryptophan
Hepacivirus C
-
0.0002
N-[(5Z)-5-((5-[2-chloro-5-(trifluoromethyl)phenyl]-2-furyl)methylene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]benzenesulfonamide
Hepacivirus C
-
-
0.00028
N-[(5Z)-5-(3,4-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]benzenesulfonamide
Hepacivirus C
-
-
0.00044
N-[(5Z)-5-(4-bromobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]benzenesulfonamide
Hepacivirus C
-
-
0.0027
N-[(Z)-2-[4-(2-bromophenoxy)phenyl]-1-[(2-hydroxyethyl)carbamoyl]ethenyl]benzamide
Hepacivirus C
-
-
0.000025
N-[3-[(4aR,7aS)-1-(4-fluorobenzyl)-4-hydroxy-2-oxo-2,4a,5,6,7,7a-hexahydro-1H-cyclopenta[b]pyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
above
0.000037
N-[3-[(4R)-5-(4-fluorobenzyl)-8-hydroxy-4-methyl-6-oxo-5-azaspiro[2.5]oct-7-en-7-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.00011
N-[3-[(5R)-1-cyclobutyl-4-hydroxy-5-methyl-2-oxo-5-propyl-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000044
N-[3-[(5R)-1-cyclobutyl-4-hydroxy-5-methyl-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000025
N-[3-[(5R)-1-cyclobutyl-5-(2-cyclopropylethyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
above
0.00017
N-[3-[(5R)-1-cyclobutyl-5-(3,3-dimethylbutyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.00017
N-[3-[(5R)-1-cyclohexyl-4-hydroxy-5-methyl-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.00065
N-[3-[(5R)-1-cyclopentyl-4-hydroxy-5-(3-methylbut-2-en-1-yl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.00012
N-[3-[(5R)-1-cyclopentyl-4-hydroxy-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000061
N-[3-[(5R)-1-cyclopentyl-4-hydroxy-5-methyl-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000057
N-[3-[(5R)-1-cyclopentyl-5-(2-cyclopropylethyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000048
N-[3-[(5R)-1-cyclopentyl-5-ethyl-4-hydroxy-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000068
N-[3-[(5R)-1-cyclopropyl-4-hydroxy-5-methyl-5-(3-methylbutyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000075
N-[3-[(5R)-1-cyclopropyl-5-(3,3-dimethylbutyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000049
N-[3-[(5R)-5-butyl-1-cyclobutyl-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.00012
N-[3-[(5R)-6-(4-fluorobenzyl)-9-hydroxy-5-methyl-7-oxo-6-azaspiro[3.5]non-8-en-8-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.0014
N-[3-[(5S)-1-(4-fluorobenzyl)-4-hydroxy-5-(3-methylbut-2-en-1-yl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000045
N-[3-[(5S)-5-ethyl-1-(4-fluorobenzyl)-4-hydroxy-5-methyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.00017
N-[3-[(6R)-1-(4-fluorobenzyl)-4-hydroxy-2-oxo-6-phenyl-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000026
N-[3-[(6R)-1-(4-fluorobenzyl)-4-hydroxy-6-(1-methylethyl)-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000042
N-[3-[(6R)-6-ethyl-1-(4-fluorobenzyl)-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000042
N-[3-[(6R)-6-tert-butyl-1-(4-fluorobenzyl)-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.0001
N-[3-[(6S)-1-(4-fluorobenzyl)-6-(4-fluorophenyl)-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000061
N-[3-[(6S)-6-(1-ethylpropyl)-1-(4-fluorobenzyl)-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000025
N-[3-[(6S)-6-ethyl-1-(4-fluorobenzyl)-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
above
0.00018
N-[3-[1-(4-fluorobenzyl)-4-hydroxy-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000085
N-[3-[1-(4-fluorobenzyl)-4-hydroxy-5,5-dimethyl-2-oxo-1,2,5,6-tetrahydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.000004 - 0.000005
N-[3-[1-(cyclobutylamino)-4-hydroxy-2-oxo-1,2-dihydroquinolin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]sulfamide
0.000002 - 0.000006
N-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydro-1,8-naphthyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
0.000274
N-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
-
0.000425
N-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-5-phenyl-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
-
0.000011
N-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-5-thiophen-2-yl-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
-
0.00028
N-[3-[5-acetyl-4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
-
0.000055
N-[3-[5-bromo-4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
-
0.000024
N-[3-[5-ethenyl-4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
-
0.000008
N-[3-[5-furan-2-yl-4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydropyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
-
0.00015
N-[3-[6-(4-fluorobenzyl)-9-hydroxy-7-oxo-6-azaspiro[4.5]dec-8-en-8-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.00022
N-[3-[7-(4-fluorobenzyl)-10-hydroxy-8-oxo-7-azaspiro[4.5]dec-9-en-9-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
0.015
N-[[2,3-bis(3-methoxyphenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophan
Hepacivirus C
-
0.1
N-[[2,3-bis(3-methoxyphenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
Hepacivirus C
IC50 above 0.1 mM
0.0017
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-(carboxymethoxy)-L-tryptophan
Hepacivirus C
-
0.0013
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophan
Hepacivirus C
-
0.0022
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-[[(2E)-3-carboxyprop-2-en-1-yl]oxy]-L-tryptophan
Hepacivirus C
-
0.0017
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-(carboxymethoxy)-L-tryptophan
Hepacivirus C
-
0.0013
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophan
Hepacivirus C
-
0.0022
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-[[(2E)-3-carboxyprop-2-en-1-yl]oxy]-L-tryptophan
Hepacivirus C
-
0.0019
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
Hepacivirus C
-
0.0061
N-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophan
Hepacivirus C
-
0.0061
N-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophan
Hepacivirus C
-
0.0041
N-[[2-cyclohexyl-3-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophan
Hepacivirus C
-
0.0034
N-[[2-cyclohexyl-3-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
Hepacivirus C
-
0.0046
N-[[3-cyclohexyl-2-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophan
Hepacivirus C
-
0.0016
N-[[3-cyclohexyl-2-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
Hepacivirus C
-
0.000034 - 0.00047
N2-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydro-1,8-naphthyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]glycinamide
0.0019
propan-2-yl (2S)-2-([([(2R,3R,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxy-4-(prop-1-yn-1-yl)oxolan-2-yl]methoxy)(phenoxy)phosphoryl]amino)propanoate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.00019
propan-2-yl (2S)-2-([([(2R,3R,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-3,4-dihydroxy-4-methyloxolan-2-yl]methoxy)(phenoxy)phosphoryl]amino)propanoate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.00045
propan-2-yl (2S)-2-([([(2R,3R,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-4-ethynyl-3,4-dihydroxyoxolan-2-yl]methoxy)(phenoxy)phosphoryl]amino)propanoate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.009
propan-2-yl (2S)-2-([([(2S,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-fluoro-3,4-dihydroxy-4-(prop-1-yn-1-yl)oxolan-2-yl]methoxy)(phenoxy)phosphoryl]amino)propanoate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.0011
propan-2-yl (2S)-2-([([(2S,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-2-fluoro-3,4-dihydroxy-4-methyloxolan-2-yl]methoxy)(phenoxy)phosphoryl]amino)propanoate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.00057
propan-2-yl (2S)-2-([([(2S,3S,4R,5R)-5-(2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-4-ethynyl-2-fluoro-3,4-dihydroxyoxolan-2-yl]methoxy)(phenoxy)phosphoryl]amino)propanoate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.00033
[(1R)-5-cyano-8-methyl-1-propyl-1,3,4,9-tetrahydropyrano[3,4-b]indol-1-yl]acetic acid
Hepacivirus C
-
-
0.003
[(1R)-8-chloro-5-ethyl-1-propyl-1,3,4,9-tetrahydropyrano[3,4-b]indol-1-yl]acetic acid
Hepacivirus C
-
-
0.000002
[(1S)-5-cyano-8-methyl-1-(1-methylpropyl)-7-[2-(1H-pyrazol-1-yl)ethoxy]-1,3,4,9-tetrahydropyrano[3,4-b]indol-1-yl]acetic acid
Hepacivirus C
-
-
0.00069
(2E)-3-[4-([[1-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
Hepacivirus C
-
0.0069
(2E)-3-[4-([[1-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
Hepacivirus C
-
0.0038
(2S,4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)pyrrolidine-2,4-dicarboxylic acid
Hepacivirus C
-
-
0.0038
(2S,4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)pyrrolidine-2,4-dicarboxylic acid
Hepacivirus C
-
full-length enzyme
0.00019
(2S,4S,5R)-2-(2-methylpropyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]pyrrolidine-2,4-dicarboxylic acid
Hepacivirus C
-
-
0.02
(2S,4S,5R)-2-(2-methylpropyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]pyrrolidine-2,4-dicarboxylic acid
Hepacivirus C
-
-
0.00097
(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
-
0.0044
(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
Hepacivirus C
-
full-length enzyme
0.00011
1-(cyclobutylamino)-3-(1,1-dioxido-4H-1,2,4-benzothiadiazin-3-yl)-4-hydroxyquinolin-2(1H)-one
Hepacivirus C
-
polymerase from 1 b genotype
0.00028
1-(cyclobutylamino)-3-(1,1-dioxido-4H-1,2,4-benzothiadiazin-3-yl)-4-hydroxyquinolin-2(1H)-one
Hepacivirus C
-
polymerase from 1 a genotype
0.000016
2-([3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydro-1,8-naphthyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]oxy)acetamide
Hepacivirus C
-
polymerase from 1 b genotype
0.000046
2-([3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydro-1,8-naphthyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]oxy)acetamide
Hepacivirus C
-
polymerase from 1 a genotype
0.00067
3'-dUTP
Zika virus
pH 7.5, 35°C, measured in the presence of 0.001 mM competing UTP, RNA template
0.00006
4-chloro-2-(4-nitrophenyl)-3H-imidazo[4,5-g]quinoline
Bovine viral diarrhea virus 1
-
pH 7.0, 22°C
0.00055
5,8-dichloro-3-propyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
Hepacivirus C
-
-
0.0021
5,8-dichloro-3-propyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
Hepacivirus C
-
-
0.0000715
8,8'-[carbonylbis(iminobenzene-3,1-diylcarbonylimino)]dinaphthalene-1,3,5-trisulfonic acid
norovirus
-
wild-type, pH 7.5, 30°C
0.00028
8,8'-[carbonylbis(iminobenzene-3,1-diylcarbonylimino)]dinaphthalene-1,3,5-trisulfonic acid
norovirus
-
mutant Y41A, pH 7.5, 30°C
0.05513
beta-D-2'-alpha-deoxy-2'-beta-fluoro-2'-C-methyluridine-5'-triphosphate
Dengue virus
-
pH 7.5, 35°C
0.09076
beta-D-2'-alpha-deoxy-2'-beta-fluoro-2'-C-methyluridine-5'-triphosphate
Zika virus
pH 7.5, 35°C, measured in the presence of 0.001 mM competing UTP, RNA template
0.00046
beta-D-2'-beta-C-ethynyluridine-5'-triphosphate
Zika virus
pH 7.5, 35°C, measured in the presence of 0.001 mM competing UTP, RNA template
0.00578
beta-D-2'-beta-C-methyluridine-5'-triphosphate
Zika virus
pH 7.5, 35°C, measured in the presence of 0.001 mM competing UTP, RNA template
0.00011
beta-D-2'-deoxy-2'-fluoro-2'-C-methylcytidine
Hepacivirus C
clinical isolate GT-1b
0.00013
beta-D-2'-deoxy-2'-fluoro-2'-C-methylcytidine
Hepacivirus C
clinical isolate GT-1a
0.202
gliotoxin
Hepacivirus C
-
in presence of MnCl2 the IC50 value is 0.036 mM, in presence of Mn2+ the IC50 value is 0.202 mM
0.000004
N-[3-[1-(cyclobutylamino)-4-hydroxy-2-oxo-1,2-dihydroquinolin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]sulfamide
Hepacivirus C
-
polymerase from 1 b genotype
0.000005
N-[3-[1-(cyclobutylamino)-4-hydroxy-2-oxo-1,2-dihydroquinolin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]sulfamide
Hepacivirus C
-
polymerase from 1 a genotype
0.000002
N-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydro-1,8-naphthyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
-
0.000002
N-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydro-1,8-naphthyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
polymerase from 1 a genotype
0.000006
N-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydro-1,8-naphthyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]methanesulfonamide
Hepacivirus C
-
polymerase from 1 b genotype
0.000034
N2-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydro-1,8-naphthyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]glycinamide
Hepacivirus C
-
polymerase from 1 b genotype
0.00047
N2-[3-[4-hydroxy-1-(3-methylbutyl)-2-oxo-1,2-dihydro-1,8-naphthyridin-3-yl]-1,1-dioxido-4H-1,2,4-benzothiadiazin-7-yl]glycinamide
Hepacivirus C
-
polymerase from 1 a genotype
0.00026
remdesivir triphosphate
Yellow fever virus
-
pH and temperature not specified in the publication
0.00101
remdesivir triphosphate
Tick-borne encephalitis virus
pH and temperature not specified in the publication
0.00136
remdesivir triphosphate
Zika virus
pH and temperature not specified in the publication
0.0014
remdesivir triphosphate
Dengue virus type 3
-
pH and temperature not specified in the publication
0.00166
remdesivir triphosphate
West Nile virus
-
pH and temperature not specified in the publication
0.00214
remdesivir triphosphate
Japanese encephalitis virus
-
pH and temperature not specified in the publication
0.018
sofosbuvir triphosphate
Dengue virus type 2
-
pH and temperature not specified in the publication
0.00007
suramin
Murine norovirus 1
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
activities of wild-type and deletion and point mutation mutant enzymes on HP1 RNA substrate, overview
additional information
relative activity of mutant enzymes compared to the wild-type enzyme, overview
additional information
-
relative activity of mutant enzymes compared to the wild-type enzyme, overview
additional information
-
strains A/WSN/33, H1N1, and A/NT/60/68, H3N2, show standard RNA polymerase activity, while strains A/HongKong/156/97, H5N1, and A/Vietnam/1194/04, H5N1, show increased polymerase activity correlated with enhanced promoter binding. The N-terminal region of the PA subunit is the major determinant of this enhanced promoter activity
additional information
the in vitro polymerase activity of a non-pathogenic calicivirus RdRp is at least two times higher than that of the RdRp of the highly virulent RHDV
additional information
-
the in vitro polymerase activity of a non-pathogenic calicivirus RdRp is at least two times higher than that of the RdRp of the highly virulent RHDV
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.5 - 8
8.2
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
-
pH 6: about 10% of maximal activity, pH 9: about 20% of maximal activity
6.3 - 9.7
-
pH 6.3: about 45% of maximal activity, pH 9.7: about 35% of maximal activity
6.5 - 8
-
pH 6.5: about 50% of maximal activity, pH 9.0: about 55% of maximal activity, poly(A) as template and biotinylated oligo(dU)15 as the primer
7 - 9
-
pH 7.0: about 70% of maximal activity, pH 9.0: about 40% of maximal activity
7.2 - 8
-
pH 7.2: about 60% of maximal activity, pH 8.0: about 60% of maximal activity
7.3 - 9.1
-
pH 7.3: about 45% of maximal activity, pH 9.1: about 80% of maximal activity
7.6 - 8.4
-
pH 7.6: about 80% of maximal activity, pH 8.4: about 65% of maximal activity, in Tris hydrochloride buffer
7.6 - 9
-
pH 7.6: about 70% of maximal activity, pH 9.0: about 80% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
30 - 37
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
17 - 37
-
17°C: about 20% of maximal activity, dramatic drecrease in activity between 32°C and 37°C, 37°C: no activity, poly(A) as template and biotinylated oligo(dU)15 as the primer
18 - 37
-
18°C: about 50% of maximal activity, 37°C: about 50% of maximal activity
22 - 37
-
when the assay temperature is increased from 22°C to 37°C the turnover number is significantly increased
25 - 40
-
25°C: about 55% of maximal activity, 40°C: about 20% of maximal activity
4 - 42
-
28.7% at 4°C and 13.4% at 42°C of the activity at 25°C, no activity at 0°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. AaV-1, isolated from the mycelia of EGS 35-193 strain of Alternaria alternata
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i.e. BlVS, from Rubus canadensis berris, the virus might belong to the family Tymoviridae
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i.e. CsfrRNAV, from the cytosol of axenic clonal algal strain L-4 of the bloom-forming Chaetoceros socialis f. radians, isolated from surface water at the Itsukaichi fishing port in Hiroshima Bay, Japan
UniProt
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i.e. ORMV, a tobamovirus taxonomically distinct from the type member of the genus, cultivated on Nicotiana benthamiana and Nicotiana tabacum plants
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Cystovirus phi6
a picornavirus, harvested from MOI-infected RD cells
UniProt
brenda
Fusarium graminearum dsRNA mycovirus 4
i.e. FgV4, a dsRNA mycovirus from Fusarium graminearum strain DK4
UniProt
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i.e. FgV3, a dsRNA mycovirus from Fusarium graminearum strain DK3
UniProt
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i.e. GLRaV-Pr, an isolate from Greek grapevines, Vitis vinifera cv. Mantilaria, belongs to the Ampelovirus group
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subunit P2; Victoria/3/1975, H3N2
UniProt
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i.e. IYSV, belongs to the genus Tospovirus, family Bunyaviridae, transmitted by onion thrips, Thrips tabaci
UniProt
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Potato spindle tuber viroid (PSTVd) RNA genome in Solanum lycopersicum
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dsR1; i.e. PmV1, belongs to the genus Partitivirus, a plant-associated virus
UniProt
brenda
Rotavirus cell entry results in loss of an outer protein layer and delivery into the cytosol of an intact, inner capsid particle (the double-layer particle or DLP). The RNA-dependent RNA polymerase (RdRp, VP1) is active inside the DLP. Each VP1 achieves many rounds of mRNA transcription from its associated genome segment. One VP1 molecule lies close to each fivefold axis of the icosahedrally symmetric DLP, just beneath the inner surface of its protein shell, embedded in tightly packed RNA. Outer layer dissociation enables the DLP to synthesize RNA, in vitro as well as in vivo, but appears not to induce any detectable structural change in the RdRp. Addition of NTPs, Mg2+, and S-adenosyl methionine, which allows active transcription, results in conformational rearrangements, in both VP1 and the DLP capsid shell protein, that allow a transcript to exit the polymerase and the particle. The position of VP1 (among the five symmetrically related alternatives) at one vertex does not correlate with its position at other vertices. This stochastic distribution of site occupancies limits long-range order in the 11-segment, dsRNA genome
UniProt
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Rotavirus A RRV
Rotavirus cell entry results in loss of an outer protein layer and delivery into the cytosol of an intact, inner capsid particle (the double-layer particle or DLP). The RNA-dependent RNA polymerase (RdRp, VP1) is active inside the DLP. Each VP1 achieves many rounds of mRNA transcription from its associated genome segment. One VP1 molecule lies close to each fivefold axis of the icosahedrally symmetric DLP, just beneath the inner surface of its protein shell, embedded in tightly packed RNA. Outer layer dissociation enables the DLP to synthesize RNA, in vitro as well as in vivo, but appears not to induce any detectable structural change in the RdRp. Addition of NTPs, Mg2+, and S-adenosyl methionine, which allows active transcription, results in conformational rearrangements, in both VP1 and the DLP capsid shell protein, that allow a transcript to exit the polymerase and the particle. The position of VP1 (among the five symmetrically related alternatives) at one vertex does not correlate with its position at other vertices. This stochastic distribution of site occupancies limits long-range order in the 11-segment, dsRNA genome
UniProt
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cv. Pentland Dell, gene StRDR1 or PGSC0003DMG400023601
UniProt
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P2a-P2b fusion protein forming the viral RNA replicase; i.e. RuCMV, a sobemovirus, isolated from raspberry and bramble plants in north east Scotland
UniProt
brenda
i.e. TSV, isolated from tail muscle tissue of infected shrimp from shrimp farms in Texas in 2004, a member of the family Dicistroviridae
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i.e. TMV, is a type member of the tobamovirus family, clone TMV-KK1, cultivated on Nicotiana benthamiana and Nicotiana tabacum plants
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infected with Cowpea mosaic virus. The host-encoded enzyme is strongly stimulated upon CPMV infection of cowpea leaves
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expressed in Escherichia coli
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genotype 1b isolate J4 with 21 amino acid C-terminal truncation and genotype 1b isolate RB01
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genotype-1b. HC-J4 NS5BDELTA21, a C-terminally truncated polymerase based on the consensus sequence of pCV-J4L6S
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standard activity strains A/WSN/33, H1N1, and A/NT/60/68, H3N2, and increased activity strains A/HongKong/156/97, H5N1, and A/Vietnam/1194/04, H5N1
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infected with alfalfa mosaic virus. The synthesis of the viral RNA is mediated by a pre-existing host enzyme, possibly modified by virus-coded proteins
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tobacco contains an RNA replicating capability, the amount of which is increased by infection with an RNA virus without noticeable changes in its enzymatic properties
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containing only nsp5, nsp7, nsp8, and nsp12; 2019-nCoV, SARS-CoV-2
UniProt
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i.e. SARS-CoV-2
MN908947
GenBank
brenda
replicase polyprotein 1ab; SARS-CoV-2
758739, 759010, 759029, 759086, 759100, 759153, 759164, 759229, 759350, 759357, 759377, 759513, 759517, 759551, 759616, 759672, 759673, 759687, 759688, 759693, 759699, 759829, 759847, 759905, 759910, 760198, 760199
UniProt
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human, i.e. SARS-CoV
UniProt
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replicase polyprotein 1ab
UniProt
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inoculated with potato spindle tuber viroid. In viroid-infected tomato leaf the activity of the host-encoded RdRP is significantly increased. Viroids are not translated into proteins so that they cannot code for a viroid-specific RNA replicase
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i.e. SINV-3, Argentinean isolate from the Santa Fe region of Argentina
UniProt
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i.e. SINV-3, from a colony in the United States, DM isolate
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
expression is specifically localized in phloem cell layers in roots
brenda
additional information
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leaf inoculated with potato spindle tuber viroid. In viroid-infected tomato leaf the activity of the host-encoded RdRP is significantly increased. Viroids are not translated into proteins so that they cannot code for a viroid-specific RNA replicase
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additional information
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cells of Drosophila melanogaster infected with Black beetle virus
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additional information
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RdRp activity is associated with heavy cytoplasmic membrane fractions in the host cell, a large fraction of the polymerase is also found in the nucleus of DENV-infected cells
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additional information
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RdRp activity is associated with heavy cytoplasmic membrane fractions in the host cell, a large fraction of the polymerase is also found in the nucleus of DENV-infected cells
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brenda
additional information
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the viral replication complex assembles on the host mitochondrial outer membrane, the enzyme preferentially binds to specific anionic phospholipids, in particular the mitochondrion-specific phospholipid cardiolipin
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additional information
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in JEV-infected cells the viral RNA-dependent RNA polymerase NS5 colocalizes with the cellular metabolic protein glyceraldehyde-3-phosphate dehydrogenase, GAPDH, in the cytosol without direct protein-protein interaction
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additional information
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RdRp activity is associated with heavy cytoplasmic membrane fractions in the host cell
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additional information
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RdRp activity is associated with heavy cytoplasmic membrane fractions in the host cell
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additional information
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leaf of Zea mays infected with Maize dwarf mosaic virus
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additional information
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the MNV-1 replication complex is localized to virus-induced vesicle clusters formed in the cytoplasm of infected RAW264.7 cells, both dsRNA and MNV-1 NS7 localize to the limiting membrane of the individual clusters, immunohistochemnic analysis, overview
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additional information
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RdRp activity is associated with heavy cytoplasmic membrane fractions in the host cell
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additional information
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RdRp activity is associated with heavy cytoplasmic membrane fractions in the host cell
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additional information
RdRp activity is associated with heavy cytoplasmic membrane fractions in the host cell
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additional information
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RdRp activity is associated with heavy cytoplasmic membrane fractions in the host cell
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additional information
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RdRp activity is associated with heavy cytoplasmic membrane fractions in the host cell, a large fraction of the polymerase is also found in the nucleus of YFV-infected cells
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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3AB is a membrane-binding protein responsible for the localization of the polymerase to the membranous vesicles at which replication occurs
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additional information
enzyme 3Dpol and Prp8 are colocalized in the nucleus
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efficient polymerase assembly is a limiting factor in the viability of reassortant viruses, mechanism of nuclear import and assembly of the three polymerase subunits, PB1, PB2, and PA, overview. PB1 and PA form a dimer in the cytoplasm, which is imported into the nucleus, separately from PB2. The PB1/PA heterodimer is imported into the nucleus by RanBP5, a member of importin beta family. Once in the nucleus, the PB1/PA dimer associates with PB2 to form the trimeric polymerase
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to improve the solubility of NS5B, the hydrophobic C-terminus containing 21 amino acids is removed, yielding a truncated NS5B which is highly soluble and monodispersed in the absence of detergents
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the enzyme is associated with the cores of the virus
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additional information
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particulate material of cells of Drosophila melanogaster infected with Black beetle virus
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additional information
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cellular membrane of brome mosaic virus infected Hordeum vulgare
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additional information
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in soluble and particulate fractions of extract of Cucumis sativus infected with Cucumber mosaic virus
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additional information
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the enzyme is closely associated with the smooth membranes of infected BHK-21 cells
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additional information
Foxtail mosaic potexvirus
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membrane fraction of Chenopodium guinoa infected with foxtail mosaic potexvirus
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additional information
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the C-termimnal region of NS5B, which is dispensable for the RNA-dependent RNA polymerase activity, dramatically affects the subcellular localization of NS5B retaining it in perinuclear sites in transiently overexpressed mammalian cells. The C-terminal region of NS5B, especially the putative anchoring domain has a role in retaining the protein in the cytoplasm
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additional information
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the enzyme is associated with particulate fraction of Zea mays leaf infected with Maize dwarf mosaic virus
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additional information
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RNA-dependent RNA polymerase activity is mediated on membrane-bound replication complexes in the host cell cytoplasm, not an integral membrane protein but tightly associated with membranes
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additional information
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enzyme is localized in the soluble phase of infected Hela cells
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additional information
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analysis of cellular localization in transfected Spodoptera frugiperda Sf9 cells of the three recombinant RdRp fragments and their interactions with nucleocapsid protein, overview. All three RdRp fragments display punctuate staining patterns in the cytoplasm, and the C-terminal fragment colocalizes with the nucleocapsid protein in the perinuclear region, but only the C-terminal fragment can interact with the nucleocapsid protein
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug target
evolution
the enzyme belongs to the RDR gene family, phylogenetic analysis of RDR genes present in potato and in a range of other plant species, overview
malfunction
metabolism
physiological function
additional information
drug target
MN908947
important target for design of antiviral drugs against 2019-nCoV
drug target
the high sequence conservation between SARS-CoV RNA-dependent RNA polymerase (RdRp) and SARS-CoV-2 RNA polymerase makes it very likely that any potent agents developed for the SARS-CoV RdRp will exhibit equal potency and efficacy on the SARS-CoV-2 enzyme
drug target
MN908947
the high sequence conservation between SARS-CoV RNA-dependent RNA polymerase (RdRp) and SARS-CoV-2 RNA polymerase makes it very likely that any potent agents developed for the SARS-CoV RdRp will exhibit equal potency and efficacy on the SARS-CoV-2 enzyme
drug target
analysis of the enzyme as a potential therapeutic drug target using a computational approach. Targeting the RdRpactive sites, ASP760 and ASP761, by antiviral drugs could be a potential therapeutic option for inhibition of coronavirus RdRp, and thus viral replication. Target-based virtual screening and molecular docking results show that the antiviral Galidesivir and its structurally similar compounds show promise against SARS-CoV-2. CID123624208 and CID11687749 may be considered for in vitro and in vivo clinical trials
drug target
cryo-electron microscopy structure of the SARS-CoV-2 RNA-dependent RNA polymerase provides insights into the mechanism of viral RNA replication and a rational template for drug design to combat the viral infection
drug target
FDA approved library of drugs are docked against the active site of the enzyme (RdRp) using Schrodinger's computer-aided drug discovery tools for in silico drug-repurposing. In molecular dynamics simulations, pitavastatin, ridogrel and rosoxacin displayed superior binding with the active site through Arg555 and Mg2+
drug target
inhibition of the viral RNA-dependent RNA polymerase (RdRp) to resolve chronic infection is a useful therapeutic strategy against Hepatitis C virus
drug target
RNA-dependent RNA polymerase inhibitors are prospective therapeutics against SARS-CoV-2
drug target
SARS-CoV-2 polymerase is a key drug target for COVID-19
drug target
search for drugs that target RNA-dependent RNA polymerase (RdRp) by in silico screening of the U.S. Food and Drug Administration approved drug library. Well-tolerated and widely used drugs are selected for molecular dynamics simulations to evaluate drug-protein interactions and their persistence under physiological conditions. Eltrombopag, tipranavir, ergotamine, and conivaptan bind to the enzyme with high binding free energies
drug target
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since virally-encoded RNA-dependent RNA polymerases of RNA viruses synthesizes new genomes in the infected host they are prime targets for antiviral therapy
drug target
systemic discussion of the pharmacological therapeutics targeting RNA-dependent RNA polymerase (RdRp)
drug target
target for antiviral drugs
drug target
the enzyme (RdRp) of the SARS-CoV-2 RNA virus represents the most optimal target for an antiviral drug. Linear amino acid sequence as well as molecule structure show the highest homology to RdRps of other positive-sense RNA viruses. It is highly predictable that an antiviral developed for an RNA virus with a genome of the same polarity (i.e. Sofosbuvir for Hepatitis C virus) could have a higher inhibitory efficacy against the SARS-CoV-2, compared to antiviral developed for negative-sense RNA viruses
drug target
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the enzyme is a key target for the development of antiviral agents against Norwalk virus gastroenteritis
drug target
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the enzyme is considered as a promising target for specific antiviral therapeutics
drug target
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the enzyme is considered as a promising target for specific antiviral therapeutics
drug target
the enzyme plays a crucial role in SARS-CoV-2 replication, and thus could be a potential drug target. Comprehensive computational approaches including drug repurposing and molecular docking are employed to predict an effective drug candidate targeting RdRp of SARS-CoV-2. This study reveales that Rifabutin, Rifapentine, Fidaxomicin, 7-methyl-guanosine-5'-triphosphate-5'-guanosine and Ivermectin have a potential inhibitory interaction with RNA-dependent RNA polymerase (RdRp) of SARS-CoV-2 and could be effective drugs for COVID-19. Virtual screening of the compounds from ZINC database allow the prediction of two compounds (ZINC09128258 and ZINC09883305) with pharmacophore features that interact effectively with RdRp of SARSCoV-2, indicating their potentiality as effective inhibitors of the enzyme. Comparative structural analysis of protein-inhibitor complexes reveals that the amino acids Y32, K47, Y122, Y129, H133, N138, D140, T141, S709 and N781 are crucial for drug surface hotspot in the RdRp of SARS-CoV-2
drug target
the structural characteristics of the catalytic domain of the RNA-dependent RNA polymerase are explored using a computational pharmacology method. Ligand-binding characteristics of the binding site are determined using a receptor-ligand function-site interaction fingerprint strategy. Binding characteristics determined by this method help to rationalize RNA-dependent RNA polymerase-targeted drug discovery and provide insights into the specific binding mechanisms important for containing the SARS-CoV-2 virus
drug target
the viral RNA-dependent-RNA-polymerase (RdRp) is a target with polymerase inhibitors successfully used for the treatment of several viral diseases
malfunction
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D-elp1 depletion inhibits RNAi in S2 cells but does not affect micro RNA function. In D-elp1 null third instar larvae transposon RNA levels are also increased and the corresponding transposon antisense RNAs are reduced
malfunction
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impairing the nuclear import of PB2 by mutating its nuclear localization signal leads to abnormal formation of the trimeric polymerase in the cytoplasm
malfunction
mutations in the hepatitis C virus polymerase that increase RNA binding can confer resistance to cyclosporine A, an inhibitor that is used as therpeutic against HCV-induced acute and chronic liver disease
malfunction
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RRF-3 mutation is involved in compromised spermatogenesis, that accounts for reduced brood size and X-chromosome loss from rrf-3 mutant hermaphrodites
malfunction
in deletion strains of the RNA-dependent RNA polymerase RrpC, full-length and shorter retrotransposable element DIRS-1 (Dictyostelium intermediate repeat sequence 1) messenger RNAs are strongly enriched, shorter versions of long non-coding RNA in DIRS-1 antisense orientation are also enriched in rrpC- strains. DIRS-1 misregulation in the absence of RrpC leads to retrotransposon mobilization
malfunction
silencing SlRDR1 using virus-induced gene silencing system significantly reduces SlRDR1 expression and tomato defense against tobacco mosaic virus but has no evident effect on alternative oxidase SlAOX1a transcription
malfunction
StRDR1 transcript accumulation decreases in transgenic potato plants constitutively expressing a hairpin construct. These plants when challenged with three viruses, potato virus Y, potato virus X, and tobacco mosaic virus show no increase in the susceptibility of potato to these viruses. Suppression of StRDR1 gene expression does not increase in the susceptibility to the viruses
malfunction
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suppression of Nicotiana benthamiana canonical 9-zinc finger transcription factor TFIIIA-7ZF reduces PSTVd replication, and overexpression of TFIIIA-7ZF enhances PSTVd replication in planta
malfunction
inhibition of RDR1c1/c2 expression leads to increased virus accumulation
malfunction
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in deletion strains of the RNA-dependent RNA polymerase RrpC, full-length and shorter retrotransposable element DIRS-1 (Dictyostelium intermediate repeat sequence 1) messenger RNAs are strongly enriched, shorter versions of long non-coding RNA in DIRS-1 antisense orientation are also enriched in rrpC- strains. DIRS-1 misregulation in the absence of RrpC leads to retrotransposon mobilization
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malfunction
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RRF-3 mutation is involved in compromised spermatogenesis, that accounts for reduced brood size and X-chromosome loss from rrf-3 mutant hermaphrodites
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metabolism
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Pol IV functions independently of the small RNA accumulation facilitated by RMR1 and RDR2. RMR1, RNA-directed DNA methylation factor, acts upstream of the RNA-dependent RNA polymerase, RDR2. While transposon-like sequences may be a common target of the maize RdDM pathway, the RMR1 and RDR2 proteins act differently with respect to their roles in mediating the type of trans-regulation induced by inverted repeats
metabolism
the salicylic acid-induced viral defense in plants is distinct from the pathways mediating bacterial and fungal defense, which is pathogenesis-related protein-independent but involves an RNA-dependent RNA polymerase 1 (RDR1)-mediated RNA silencing mechanism and/or an alternative oxidase (AOX)-associated defense pathway. As the RDR1-mediated RNA silencing pathway and the AOX-regulated pathway are both involved in the salicylic acid-induced defense against viruses but are independent of pathogenesis-related protein genes, crosstalk between these two antiviral pathways may exist
physiological function
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D-elp1 is required for RNA interference, interacts with Dcr-2 protein, and has a role in transposon suppression, overview. It might be interacting with components of the RISC
physiological function
Q9LKP0
RDR6 functions in trans-acting short interfering RNA, ta-siRNA, production. Positive regulators or effectors of SI and pistil development are regulated by ta-siRNAs, regulation, overview
physiological function
Cystovirus phi6
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RdRps are unique in that they create dsRNA by initiating polymerization at the 3' end of the substrate
physiological function
RDRs play a key role in RNA silencing, heterochromatin formation and natural gene regulation. It may play an important role in response to biotic and abiotic stresses
physiological function
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RRF-3 is required for spermatocyte cell division, overview
physiological function
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small RNA deep sequencing reveals a functional role for RDR in promoting viral siRNA biogenesis through distinct mechanisms, overview. RDR1and RDR6 are also implicated in antiviral defense
physiological function
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the enzyme is required for replication of the genomes of positive-strand RNA viruses occuring in highly oligomeric complexes on the cytosolic surfaces of the intracellular membranes of infected host cells
physiological function
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the enzyme is required for the RNA-directed DNA methylation, dedicated to the methylation of target sequences, which include transposable elements, regulatory regions of several protein-coding genes, and 5S rRNA-encoding DNA arrays. Pol IV, RDR2, DRM2, and Pol V, actors of the RdDM, are required to maintain a transcriptional silencing of 5S RNA genes at chromosomes 4 and 5, regulation, overview
physiological function
the enzyme is responsible for replication and transcription of the eight separate segments of the viral RNA genome in the nuclei of infected cells
physiological function
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the FHV RNA-dependent RNA polymerase, protein A, is the only viral protein necessary for genome replication in the budding yeast Saccharomyces cerevisiae
physiological function
expression in Drosophila melanogaster enhances transitive dsRNA-dependent silencing
physiological function
expression in Drosophila melanogaster triggers transcriptional silencing of unpaired DNA during embryonic mitosis. Isoform ego-1 triggers dsRNA-independent silencing, specifically of transgenes. The strain w, da-Gal4, UAST-ego-1, constitutively expressing ego-1, is capable of silencing transgene including dsRNA hairpin upon a single cross
physiological function
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isoform RDR6 acts in the biogenesis of various types and sizes of small RNAs. An rdr6-1 mutant, which is temperature sensitive and shows spikelet defects, displays reduced accumulation of trans-acting siR-auxin response factors, the conserved trans-acting siRNAs derived from the TAS3 locus, and ectopic expression of trans-acting siR-auxin response factors target genes. 21-Nucleotide phased small RNAs are also largely dependent on isoform RDR6. Isoform RDR6 has a strong impact on the accumulation of 24-nt phased small RNAs, but not on unphased ones
physiological function
isoform RDR6 is required for efficient hpRNA-induced RNA silencing in plants. Generation of wild-type and rdr6-11 Arabidopsis thaliana lines expressing green fluorescent protein and transformation with a green fluorescent protein-RNA interference construct leads to almost complete silencing of green fluorescent protein expression in the T1 generation of most green fluorescent protein-RNAi-transformed wild-type lines, whereas various levels of green fluorescent protein expression remain among the green fluorescent protein-RNAi-transformed rdr6-11 lines. Homozygous expression of green fluorescent protein-RNAi in the T3 generation is not sufficient to induce complete green fluorescent protein silencing in several rdr6-11 lines
physiological function
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Nicotiana benthamiana transformed with isoform RDR1 from Nicotiana tabacum exhibits hypersusceptibility to plum pox potyvirus and other viruses, resembling RDR6-silenced Nicotiana benthamiana. Nicotiana tabacum-RDR1 possesses silencing suppression activity and does not interfere with isoform RDR6-dependent siRNA accumulation but turns out to suppress RDR6-dependent sense-transgenes Isoform RDR1 might have a dual role, contributing, on one hand, to salicylic acid-mediated antiviral defense, and suppressing, on the other hand, the RDR6-mediated antiviral RNA silencing
physiological function
systematic analysis of susceptibility and small RNA formation in Arabidopsis mutants lacking combinations of RNA-dependent RNA polymerase isoforms and dicer-like proteins. The vast majority of turnip mosaic virus-derived small interfering RNAs are dependent on dicer-like protein isoform DCL4 and RNA polymerase isoform RDR1, although full antiviral defense also requires isoforms DCL2 and RDR6. DCL4 is sufficient for antiviral silencing in inoculated leaves, but isoforms DCL2 and DCL4 are both involved in silencing in systemic tissues. Basal levels of antiviral RNA silencing and siRNA biogenesis are detected in mutants lacking isoforms RDR1, RDR2, and RDR6, indicating an alternate route to form double-stranded RNA that does not depend on the three previously characterized RNA-dependent RNA polymerase proteins
physiological function
cellular RNA-dependent RNA polymerases catalyze synthesis of double-stranded RNAs that can serve to initiate or amplify RNA silencing. Enzyme RDR1 contributes to basal virus resistance in several plants
physiological function
enzyme RDR1 is involved in the AOXmediated defense pathway against tobacco mosaic virus infection and plays a crucial role in enhancing RNA silencing to limit virus systemic spread
physiological function
mechanism of viruses attacking hosts whereby picornaviral 3D polymerase (3Dpol) enters the nucleus and targets the central pre-mRNA processing factor 8 (Prp8) to block premRNA splicing and mRNA synthesis. The 3Dpol inhibits the second catalytic step of the splicing process, resulting in the accumulation of the lariat-form and the reduction of the mRNA. 3Dpol inhibits intracellular pre-mRNA splicing by interacting with Prp8, modelling, overview
physiological function
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negative-sense RNA viruses, such as influenza, encode large, multidomain RNA-dependent RNA polymerases that can both transcribe and replicate the viral RNA genome. Replication occurs through de novo initiation and involves a complementary RNA intermediate
physiological function
P2, an RNA-directed polymerase (RdRp), is the critical component of a four-protein polymerase complex (PX) that includes in addition to P2, the major capsid protein, P1, a packaging NTPase, P4, and an accessory protein, P71. P2 performs the dual tasks of transcription and replication de novo without the use of a primer (i. e. P2 is a self-priming RdRp), and plays a critical role in the cystoviral life cycle
physiological function
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probing of the entire Dengue genome for interactions via Y3H with viral RNA-dependent RNA polymerase reveals a dominant interaction as a loop-forming ACAG motif in the 3' positive-stranded terminus, RdRp recognizes the top loop of 3'-SL in both genomic forms, interactions sites coincides with known flaviviral recombination sites inside the viral protein-coding region. Specific recognition of the RNA element occurs via an arginine patch in the C-terminal thumb domain of enzyme RdRp. Disruption of the interaction results in loss of viral replication ability in cells. This unique RdRp-RNA interface is found throughout flaviviruses
physiological function
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RNA polymerase II acts as an RNA-dependent RNA polymerase to extend and destabilize a non-coding RNA. Mammalian Pol II acts as an RdRP to control the stability of a cellular RNA by extending its 3'-end. Extended B2 RNA can repress transcription, but with decreased potency
physiological function
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role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
physiological function
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role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
physiological function
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role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
physiological function
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role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
physiological function
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role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
physiological function
role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
physiological function
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segment 2 (S2)-encoded RNA-dependent RNA polymerase (RdRp) helps the virus to propagate its genome in the host cell of the silkworm, Antheraea mylitta
physiological function
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the DNA-dependent RNA polymerase (DdRP) from Potato spindle tuber viroid (PSTVd) RNA genome in Solanum lycopersicum possesses RNA-dependent RNA polymerase activity. A land plant-specific transcription factor directly enhances transcription of a pathogenic noncoding RNA template by DNA-dependent RNA polymerase II
physiological function
the RNA-dependent RNA polymerase activity resides in the C-terminal two-thirds of non-structural protein (NS) 5 responsible for the de novo synthesis of the viral RNA genome. RdRp specifically binds to the viral UTR
physiological function
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the RNA-dependent RNA polymerase of rice stripe virus is critical for both the transcription and replication of the viral genome
physiological function
the RNA-dependent RNA polymerase RrpC silences the centromeric retrotransposon DIRS-1 post-transcriptionally and is required for the spreading of RNA silencing signals. RrpC is a key player in the silencing of centromeric retrotransposon DIRS-1. RrpC acts at the post-transcriptional level and is involved in spreading of RNA silencing signals, both in the 5' and 3' directions
physiological function
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viral RNA-dependent RNA polymerases (RdRPs) play essential roles in viral genome replication and transcription
physiological function
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viral RNA-dependent RNA polymerases (RdRPs) play essential roles in viral genome replication and transcription
physiological function
essential enzyme for viral RNA replication
physiological function
essential enzyme of the coronaviral replication/transcription machinery. It catalyzes the synthesis of coronavirus RNA
physiological function
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expression of rabbit calicivirus RNA-dependent RNA polymerase induces a redistribution of both cis/medial and medial/trans Golgi membrane markers, but not that of an endoplasmic reticulum membrane marker
physiological function
-
Flavivirus replication occurs on the ER and is regulated by many mechanisms and factors. NS5, which consists of a C-terminal RNA-dependent RNA polymerase (RdRp) domain and an N-terminal methyltransferase domain, plays a pivotal role in genome replication and capping. The C-terminal RdRp domain acts as the polymerase for RNA synthesis and cooperates with diverse viral proteins to facilitate productive RNA proliferation within the replication complex. RdRp recognizes the initiation site of the genome via an RdRp-UTR interaction, the interaction between RdRp and NS3 promotes NTPase and helicase activity, and the interaction between the RdRp and the MTase is involved in new RNA synthesis. The RdRp is indispensable for flavivirus replication because of not only its own polymerase activity, but also its interactions with other viral proteins and RNAs, which leads to efficient genomic RNA replication
physiological function
-
Flavivirus replication occurs on the ER and is regulated by many mechanisms and factors. NS5, which consists of a C-terminal RNA-dependent RNA polymerase (RdRp) domain and an N-terminal methyltransferase domain, plays a pivotal role in genome replication and capping. The C-terminal RdRp domain acts as the polymerase for RNA synthesis and cooperates with diverse viral proteins to facilitate productive RNA proliferation within the replication complex. RdRp recognizes the initiation site of the genome via an RdRp-UTR interaction, the interaction between RdRp and NS3 promotes NTPase and helicase activity, and the interaction between the RdRp and the MTase is involved in new RNA synthesis. The RdRp is indispensable for flavivirus replication because of not only its own polymerase activity, but also its interactions with other viral proteins and RNAs, which leads to efficient genomic RNA replication
physiological function
-
Flavivirus replication occurs on the ER and is regulated by many mechanisms and factors. NS5, which consists of a C-terminal RNA-dependent RNA polymerase (RdRp) domain and an N-terminal methyltransferase domain, plays a pivotal role in genome replication and capping. The C-terminal RdRp domain acts as the polymerase for RNA synthesis and cooperates with diverse viral proteins to facilitate productive RNA proliferation within the replication complex. RdRp recognizes the initiation site of the genome via an RdRp-UTR interaction, the interaction between RdRp and NS3 promotes NTPase and helicase activity, and the interaction between the RdRp and the MTase is involved in new RNA synthesis. The RdRp is indispensable for flavivirus replication because of not only its own polymerase activity, but also its interactions with other viral proteins and RNAs, which leads to efficient genomic RNA replication
physiological function
-
Flavivirus replication occurs on the ER and is regulated by many mechanisms and factors. NS5, which consists of a C-terminal RNA-dependent RNA polymerase (RdRp) domain and an N-terminal methyltransferase domain, plays a pivotal role in genome replication and capping. The C-terminal RdRp domain acts as the polymerase for RNA synthesis and cooperates with diverse viral proteins to facilitate productive RNA proliferation within the replication complex. RdRp recognizes the initiation site of the genome via an RdRp-UTR interaction, the interaction between RdRp and NS3 promotes NTPase and helicase activity, and the interaction between the RdRp and the MTase is involved in new RNA synthesis. The RdRp is indispensable for flavivirus replication because of not only its own polymerase activity, but also its interactions with other viral proteins and RNAs, which leads to efficient genomic RNA replication
physiological function
-
Flavivirus replication occurs on the ER and is regulated by many mechanisms and factors. NS5, which consists of a C-terminal RNA-dependent RNA polymerase (RdRp) domain and an N-terminal methyltransferase domain, plays a pivotal role in genome replication and capping. The C-terminal RdRp domain acts as the polymerase for RNA synthesis and cooperates with diverse viral proteins to facilitate productive RNA proliferation within the replication complex. RdRp recognizes the initiation site of the genome via an RdRp-UTR interaction, the interaction between RdRp and NS3 promotes NTPase and helicase activity, and the interaction between the RdRp and the MTase is involved in new RNA synthesis. The RdRp is indispensable for flavivirus replication because of not only its own polymerase activity, but also its interactions with other viral proteins and RNAs, which leads to efficient genomic RNA replication
physiological function
-
Flavivirus replication occurs on the ER and is regulated by many mechanisms and factors. NS5, which consists of a C-terminal RNA-dependent RNA polymerase (RdRp) domain and an N-terminal methyltransferase domain, plays a pivotal role in genome replication and capping. The C-terminal RdRp domain acts as the polymerase for RNA synthesis and cooperates with diverse viral proteins to facilitate productive RNA proliferation within the replication complex. RdRp recognizes the initiation site of the genome via an RdRp-UTR interaction, the interaction between RdRp and NS3 promotes NTPase and helicase activity, and the interaction between the RdRp and the MTase is involved in new RNA synthesis. The RdRp is indispensable for flavivirus replication because of not only its own polymerase activity, but also its interactions with other viral proteins and RNAs, which leads to efficient genomic RNA replication
physiological function
-
Flavivirus replication occurs on the ER and is regulated by many mechanisms and factors. NS5, which consists of a C-terminal RNA-dependent RNA polymerase (RdRp) domain and an N-terminal methyltransferase domain, plays a pivotal role in genome replication and capping. The C-terminal RdRp domain acts as the polymerase for RNA synthesis and cooperates with diverse viral proteins to facilitate productive RNA proliferation within the replication complex. RdRp recognizes the initiation site of the genome via an RdRp-UTR interaction, the interaction between RdRp and NS3 promotes NTPase and helicase activity, and the interaction between the RdRp and the MTase is involved in new RNA synthesis. The RdRp is indispensable for flavivirus replication because of not only its own polymerase activity, but also its interactions with other viral proteins and RNAs, which leads to efficient genomic RNA replication
physiological function
-
Flavivirus replication occurs on the ER and is regulated by many mechanisms and factors. NS5, which consists of a C-terminal RNA-dependent RNA polymerase (RdRp) domain and an N-terminal methyltransferase domain, plays a pivotal role in genome replication and capping. The C-terminal RdRp domain acts as the polymerase for RNA synthesis and cooperates with diverse viral proteins to facilitate productive RNA proliferation within the replication complex. RdRp recognizes the initiation site of the genome via an RdRp-UTR interaction, the interaction between RdRp and NS3 promotes NTPase and helicase activity, and the interaction between the RdRp and the MTase is involved in new RNA synthesis. The RdRp is indispensable for flavivirus replication because of not only its own polymerase activity, but also its interactions with other viral proteins and RNAs, which leads to ex0ecient genomic RNA replication
physiological function
key enzyme responsible for the SARS-CoV-2 replication process, catalyzes the synthesis of complementary minus strand RNA and genomic plus strand RNA
physiological function
-
potyviral RNA-dependent RNA polymerase NIb plays key roles in diverse virus-host interactions. It recruits several host proteins into the viral replication complexes (VRCs), which are essential for the formation of functional VRCs for virus multiplication, and interacts with the sumoylation pathway proteins to suppress NPR1-mediated immunity response. NIb serves as a target of selective autophagy as well as an elicitor of effector-triggered immunity, resulting in attenuated virus infection
physiological function
-
potyviral RNA-dependent RNA polymerase NIb plays key roles in diverse virus-host interactions. It recruits several host proteins into the viral replication complexes (VRCs), which are essential for the formation of functional VRCs for virus multiplication, and interacts with the sumoylation pathway proteins to suppress NPR1-mediated immunity response. NIb serves as a target of selective autophagy as well as an elicitor of effector-triggered immunity, resulting in attenuated virus infection
physiological function
-
potyviral RNA-dependent RNA polymerase NIb plays key roles in diverse virus-host interactions. It recruits several host proteins into the viral replication complexes (VRCs), which are essential for the formation of functional VRCs for virus multiplication, and interacts with the sumoylation pathway proteins to suppress NPR1-mediated immunity response. NIb serves as a target of selective autophagy as well as an elicitor of effector-triggered immunity, resulting in attenuated virus infection
physiological function
-
potyviral RNA-dependent RNA polymerase NIb plays key roles in diverse virus-host interactions. It recruits several host proteins into the viral replication complexes (VRCs), which are essential for the formation of functional VRCs for virus multiplication, and interacts with the sumoylation pathway proteins to suppress NPR1-mediated immunity response. NIb serves as a target of selective autophagy as well as an elicitor of effector-triggered immunity, resulting in attenuated virus infection
physiological function
-
RNA-dependent RNA polymerase 6 is a core component of the small RNA biogenesis pathway. Based on its core role in small RNA processing, it plays an important role in plant development and immunity. The enzyme plays an important role in DNA methylation. It contributes to double-strand break formation in meiosis
physiological function
RNA-dependent RNA polymerase is a critical enzyme for coronavirus replication
physiological function
RNA-dependent RNA polymerase is a key enzyme which regulates the viral replication of SARS-CoV-2
physiological function
the enzyme (RdRP) is essential for both transcription and replication of the viral RNA genome
physiological function
-
the enzyme catalyzes the replication of the hepatitis C virus genome
physiological function
-
the enzyme induces a rearrangement of the Golgi network. Inactivating mutations in the conserved GDD motif do not abolish the ability of Rabbit haemorrhagic disease virus RNA-dependent RNA polymerase to rearrange the Golgi network, suggesting that polymerase activity and metal co-factors are not required for this function
physiological function
-
the enzyme is essential for replicating the genome of the virus
physiological function
the enzyme plays a crucial role in plant defence against viruses
physiological function
the enzyme plays a crucial role in plant defence against viruses. A constitutive high level of RDR1b gene expression independent of salicylic acid is associated with broad virus resistance
physiological function
the enzyme plays a crucial role in SARS-CoV-2 replication
physiological function
the enzyme plays a key role in the replication of SARS-CoV-2
physiological function
the nsp12 (RdRp) is a central component of SARS-CoV-2 replication/transcription machinery. It catalyzes the synthesis of a complementary RNA strand using the virus RNA template with the assistance of nsp7 and nsp8 as cofactors
physiological function
-
virally-encoded RNA-dependent RNA polymerases of RNA viruses synthesizes new genomes in the infected host
physiological function
-
role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
-
physiological function
-
the RNA-dependent RNA polymerase RrpC silences the centromeric retrotransposon DIRS-1 post-transcriptionally and is required for the spreading of RNA silencing signals. RrpC is a key player in the silencing of centromeric retrotransposon DIRS-1. RrpC acts at the post-transcriptional level and is involved in spreading of RNA silencing signals, both in the 5' and 3' directions
-
physiological function
-
role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
-
physiological function
-
the enzyme is responsible for replication and transcription of the eight separate segments of the viral RNA genome in the nuclei of infected cells
-
physiological function
-
role of motif B loop in allosteric regulation of RNA-dependent RNA polymerization activity, allosteric factors regulating B-loop dynamics
-
physiological function
-
RRF-3 is required for spermatocyte cell division, overview
-
physiological function
-
mechanism of viruses attacking hosts whereby picornaviral 3D polymerase (3Dpol) enters the nucleus and targets the central pre-mRNA processing factor 8 (Prp8) to block premRNA splicing and mRNA synthesis. The 3Dpol inhibits the second catalytic step of the splicing process, resulting in the accumulation of the lariat-form and the reduction of the mRNA. 3Dpol inhibits intracellular pre-mRNA splicing by interacting with Prp8, modelling, overview
-
additional information
-
efficient polymerase assembly is a limiting factor in the viability of reassortant viruses, mechanism of nuclear import and assembly of the three polymerase subunits, PB1, PB2, and PA, overview
additional information
-
the RNA polymerase of influenza virus is a heterotrimeric complex of PB1, PB2 and PA subunits, which cooperate in the transcription and replication of the viral genome
additional information
-
overall enzyme structure analysis from crystal structure, PDB ID 1WNE. Structure solution of RdRP-RNA-rNTP complexes, overview
additional information
overall enzyme structure analysis from crystal structure, PDB ID 3ZED. Structure solution of RdRP-RNA-rNTP complexes, open and closed conformations of the B-loop in IBDV VP, overview
additional information
-
overall enzyme structure analysis from crystal structure, PDB IDs 2PUS and 2R70. Structure solution of RdRP-RNA-rNTP complexes, conformational changes in the B-loop of RdRP, overview
additional information
-
overall enzyme structure analysis from crystal structure, PDB IDs 2XXD and 4E76. Structure solution of RdRP-RNA-rNTP complexes, overview
additional information
-
overall enzyme structure analysis from crystal structure, PDB IDs 3N6L, 3N6N, and 3N6M, conformational changes in the B-loop of RdRP. Structure solution of RdRP-RNA-rNTP complexes, overview
additional information
-
overall enzyme structure analysis from crystal structures, PDB IDs 1SH0, 3BSO, and 1SH3. Structure solution of RdRP-RNA-rNTP complexes, conformational changes in the B-loop of RdRP, overview
additional information
-
phase-distributed sRNAs are identified within the dsRNA-seq read-covered regions. sRNA sequences from Col-0 (GSM121455, GSM154336, and GSM154375) are mapped onto the sequence regions with two or more phase-distributed, RDRdependent sRNA loci
additional information
-
polymerase FluPol is composed of three polypeptides: PB1, PB2 and PA/P3. PB1 houses the polymerase active site, whereas PB2 and PA/P3 contain, respectively, cap-binding and endonuclease domains required for transcription initiation by cap-snatching. Comparison of apo-FluPolC with promoter-bound FluPolA, overview
additional information
-
seven RdRP elongation complex structures derived from a crystal lattice that allows three RdRP nucleotide addition cycle (NAC) events. NTP recognition and translocation mechanisms in viral RdRPs and uniqueness of the viral RdRPs compared with other processive polymerases, modelling, overview. Determination of initial NTP binding, active site closure, and, in particular the RNA motion during translocation that shows an asymmetric movement of the two strands in the template-product duplex
additional information
-
several structural states of the poliovirus RdRP nucleotide addition cycle (NAC) reveal a unique palm domain-based active site closure mechanism and propose a six-state NAC model including a hypothetical state representing translocation intermediates. NTP recognition and translocation mechanisms in viral RdRPs and uniqueness of the viral RdRPs compared with other processive polymerases, modelling, overview
additional information
structure of P2, the self-priming RdRp from cystovirus phi12, crystal structure analysis, overview. The tunnel through which template ssRNA accesses the active site is partially occluded by a flexible loop; this feature, along with sub-optimal positioning of other structural elements that prevent the formation of a stable initiation complex, indicate an inactive conformation in crystallo
additional information
the in vitro polymerase activity of a non-pathogenic calicivirus RdRp is at least two times higher than that of the RdRp of the highly virulent RHDV
additional information
-
the in vitro polymerase activity of a non-pathogenic calicivirus RdRp is at least two times higher than that of the RdRp of the highly virulent RHDV
additional information
-
the RNA-dependent RNA polymerase (RdRp) in equine arteritis virus is expressed as the C-terminal domain of nonstructural protein 9 (nsp9)
additional information
-
treatment of cells with a-amanitin or actinomycin D revealed that extension of B2 RNA by Pol II destabilizes the RNA
additional information
-
viral enzymes contain unique structure elements on the N-terminus of the molecule that are not common for polymerases of other types. The element that is adjacent to the N-terminus of the subdomain fingers, and is therefore sometimes called the fingertips, interacts with the C-terminal subdomain (thumb), resulting in transformation of the catalytic cavity into the passthrough tunnel. Therefore, this structure is called a closed hand, in contrast to such structures as prokaryotic DNA polymerases or reverse transcriptase in which the catalytic cavity has the shape of an open trough, i.e. the fingers and thumb subdomains are distanced (the structure of an open hand), structural elements of viral rNA polymerases, overview. Formation of the active site by palm conservative elements
additional information
-
viral enzymes contain unique structure elements on the N-terminus of the molecule that are not common for polymerases of other types. The element that is adjacent to the N-terminus of the subdomain fingers, and is therefore sometimes called the fingertips, interacts with the C-terminal subdomain (thumb), resulting in transformation of the catalytic cavity into the passthrough tunnel. Therefore, this structure is called a closed hand, in contrast to such structures as prokaryotic DNA polymerases or reverse transcriptase in which the catalytic cavity has the shape of an open trough, i.e. the fingers and thumb subdomains are distanced (the structure of an open hand), structural elements of viral rNA polymerases, overview. Formation of the active site by palm conservative elements, birnaviral RdRP contains a K+-binding site within its palm subdomain. In most known polymerases, the conservative elements are arranged in alphabetical order, but variants with non-canonical sequence in the primarystructure also exist. In this way the polymerases of birnaviruses and some insect viruses possess elements of the active site in the order: C-A-B-D-E-F. Motif F carries conservative basic lysine and arginine residues that may be involved in the binding of RNA polymerase of birnaviruses. In birnavirus polymerases a serine residue located in the fingers subdomain can be subjected to guanidylation that birnavirus RdRP requires for self-priming. The thumb subdomain of birnaviral RdRP is close in size to the latter and also consists of four alpha-helices and small beta-sheet, which interacts with two beta-strands of the palm subdomain. The C-terminal subdomains of birnaviral polymerase represents an extra, expanded region with several alpha-helices not assembled into compact structure, and interact with the thumb subdomain and fingertips
additional information
-
viral enzymes contain unique structure elements on the N-terminus of the molecule that are not common for polymerases of other types. The element that is adjacent to the N-terminus of the subdomain fingers, and is therefore sometimes called the fingertips, interacts with the C-terminal subdomain (thumb), resulting in transformation of the catalytic cavity into the passthrough tunnel. Therefore, this structure is called a closed hand, in contrast to such structures as prokaryotic DNA polymerases or reverse transcriptase in which the catalytic cavity has the shape of an open trough, i.e. the fingers and thumb subdomains are distanced (the structure of an open hand), structural elements of viral rNA polymerases, overview. Formation of the active site by palm conservative elements. Molecular dynamics of hepatitis C virus RdRP, when interacting with the molecule of a specific inhibitor that binds to the thumb subdomain, show that the ligand binding significantly reduces the ability of the polymerase to change its conformation
additional information
-
viral enzymes contain unique structure elements on the N-terminus of the molecule that are not common for polymerases of other types. The element that is adjacent to the N-terminus of the subdomain fingers, and is therefore sometimes called the fingertips, interacts with the C-terminal subdomain (thumb), resulting in transformation of the catalytic cavity into the passthrough tunnel. Therefore, this structure is called a closed hand, in contrast to such structures as prokaryotic DNA polymerases or reverse transcriptase in which the catalytic cavity has the shape of an open trough, i.e. the fingers and thumb subdomains are distanced (the structure of an open hand), structural elements of viral rNA polymerases, overview. The Gly64 in the polymerase molecule binds through hydrogen with N-terminal Gly1, which, in turn, interacts with the amino acid residues from the fingers subdomain (Ala239 and Leu241). Formation of the active site by palm conservative elements
additional information
-
overall enzyme structure analysis from crystal structure, PDB ID 1WNE. Structure solution of RdRP-RNA-rNTP complexes, overview
-
additional information
-
overall enzyme structure analysis from crystal structure, PDB IDs 2PUS and 2R70. Structure solution of RdRP-RNA-rNTP complexes, conformational changes in the B-loop of RdRP, overview
-
additional information
-
phase-distributed sRNAs are identified within the dsRNA-seq read-covered regions. sRNA sequences from Col-0 (GSM121455, GSM154336, and GSM154375) are mapped onto the sequence regions with two or more phase-distributed, RDRdependent sRNA loci
-
additional information
-
overall enzyme structure analysis from crystal structure, PDB IDs 2XXD and 4E76. Structure solution of RdRP-RNA-rNTP complexes, overview
-
additional information
-
the in vitro polymerase activity of a non-pathogenic calicivirus RdRp is at least two times higher than that of the RdRp of the highly virulent RHDV
-
Show AA Sequence and Transmembrane Helices (155666 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
A0A7L9RWV7
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
130000
-
the low value compared to the sum of molecular weights of the four subunits is probably a result of an oblate shape conferred by ribosomal protein S1, glycerol gradient sedimentation
250000
Influenza virus A/PR8
-
3 * 250000, the enzyme is a heterocomplex composed of one each of the three P-proteins: PB1, PB2 and PA. Each of them shows a MW of 250000 Da in glycerol gradient centrifugation
35000
-
x * 35000 + x * 450000 + x * 650000 + x * 700000, the enzyme is composed of 4 nonidentical subunits, only the 65000 Da subunit is phage-coded. The 70000 Da protein is 30S ribosomal protein S1 and the other two are the protein synthesis elongation factors Tu and Ts
42000
x * 42000, recombinant His6-tagged NS5B, SDS-PAGE, x * 68000, recombinant RDRP, SDS-PAGE
450000
-
x * 35000 + x * 450000 + x * 650000 + x * 700000, the enzyme is composed of 4 nonidentical subunits, only the 65000 Da subunit is phage-coded. The 70000 Da protein is 30S ribosomal protein S1 and the other two are the protein synthesis elongation factors Tu and Ts
650000
-
x * 35000 + x * 450000 + x * 650000 + x * 700000, the enzyme is composed of 4 nonidentical subunits, only the 65000 Da subunit is phage-coded. The 70000 Da protein is 30S ribosomal protein S1 and the other two are the protein synthesis elongation factors Tu and Ts
68000
700000
-
x * 35000 + x * 450000 + x * 650000 + x * 700000, the enzyme is composed of 4 nonidentical subunits, only the 65000 Da subunit is phage-coded. The 70000 Da protein is 30S ribosomal protein S1 and the other two are the protein synthesis elongation factors Tu and Ts
82000
-
x * 82000, SDS-PAGE, fusion protein using the N-terminal domain of Escherichia coli lysyl-tRNA synthetase
additional information
68000
x * 42000, recombinant His6-tagged NS5B, SDS-PAGE, x * 68000, recombinant RDRP, SDS-PAGE
additional information
-
a major polypeptide of 100000 Da is specific for the RNA replicase, determined by SDS-PAGE
additional information
-
presence of two protein bands of MW 110000 Da and 100000 Da which are present in fractions from CMV-infected plants but not from healthy plants
additional information
Influenza virus A/PR8
-
the three P proteins, PB1, PB2, and PA sediment altogether with 250000 Da in glycerol gradient centrifugation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotrimer
monomer
tetramer
trimer
additional information
?
x * 42000, recombinant His6-tagged NS5B, SDS-PAGE, x * 68000, recombinant RDRP, SDS-PAGE
?
-
x * 82000, SDS-PAGE, fusion protein using the N-terminal domain of Escherichia coli lysyl-tRNA synthetase
heterotrimer
-
the RNA polymerase complex consists of three subunits, PB1, PB2, and PA. These polymerase subunits and nucleoprotein, together with the viral RNA, form the viral ribonucleoprotein complex, which is the minimum component for viral RNA replication and transcription
heterotrimer
-
the RNA polymerase of influenza virus is a heterotrimeric complex of PB1, PB2 and PA subunits, which cooperate in the transcription and replication of the viral genome. The N-terminal region of the PA subunit of two recent H5N1 strains can influence promoter binding
heterotrimer
the three subunits, PB1, PB2 and PA, are all required for both transcription and replication, PB1 carries the polymerase active site, PB2 includes the capped-RNA recognition domain, and PA, whose C-terminal domain consists of 13 alpha-helices and 9 beta-strands, is involved in assembly of the functional complex. The subunit interface is important for viral replication, overview
monomer
-
monomers are observed at NaCl concentrations above 300 mM. Binding of short RNA substrates leads to a further increase in oligomerization, whereas GTP does not show any effect on protein/protein interactions. Nucleotide incorporation studies indicate the oligomerization state does not correlate with enzymatic activities
tetramer
-
the enzyme contains four nonidentical polypeptide chains, only one of which is a product of the phage genome. The other three subunits, present in uninfected cells are ribosomal protein S1 and protein synthesis elongation factors EF-Tu and EF-TS
tetramer
-
x * 35000 + x * 450000 + x * 650000 + x * 700000, the enzyme is composed of 4 nonidentical subunits, only the 65000 Da subunit is phage-coded. The 70000 Da protein is 30S ribosomal protein S1 and the other two are the protein synthesis elongation factors Tu and Ts
tetramer
-
composed of one phage-coded polypeptide and three host-supplied polypeptides
tetramer
Qubevirus durum Qbetaam12
-
x * 35000 + x * 450000 + x * 650000 + x * 700000, the enzyme is composed of 4 nonidentical subunits, only the 65000 Da subunit is phage-coded. The 70000 Da protein is 30S ribosomal protein S1 and the other two are the protein synthesis elongation factors Tu and Ts
-
tetramer
Qubevirus durum QbetaamB86
-
the enzyme contains four nonidentical polypeptide chains, only one of which is a product of the phage genome. The other three subunits, present in uninfected cells are ribosomal protein S1 and protein synthesis elongation factors EF-Tu and EF-TS
-
tetramer
Qubevirus durum QbetaamB86
-
x * 35000 + x * 450000 + x * 650000 + x * 700000, the enzyme is composed of 4 nonidentical subunits, only the 65000 Da subunit is phage-coded. The 70000 Da protein is 30S ribosomal protein S1 and the other two are the protein synthesis elongation factors Tu and Ts
-
trimer
-
mechanism of nuclear import and assembly of the three polymerase subunits, PB1, PB2, and PA, overview. PB1 and PA form a dimer in the cytoplasm, which is imported into the nucleus separately from PB2. Once in the nucleus, the PB1/PA dimer associates with PB2 to form the trimeric polymerase. The strong interface that can be formed between the N-terminal extremity of PB2 and the C-terminal extremity of PB1 is present only in the fully assembled trimeric polymerase
trimer
Influenza virus A/PR8
-
3 * 250000, the enzyme is a heterocomplex composed of one each of the three P-proteins: PB1, PB2 and PA. Each of them shows a MW of 250000 Da in glycerol gradient centrifugation
additional information
-
the enzyme has a basic right-handed structure having a palm (residues 520-563, 641-735), thumb (residues 736-879) and fingers (residues 350-519, 564-640) subdomains. The central polymerase domain (PD) shows nucleotide binding properties, but neither the N-terminal domain (NTD) nor the C-terminal domain (CTD). Isolated PD does not exhibit RdRp activity but this activity can be reconstituted when all three domains are included in the reaction mixture. Molecular dynamics simulation suggests that the isolated PD has increased internal motions in comparison to when it is associated with the NTD and CTD. The motions of the separated PD may lead to the formation of a less accessible RNA template-binding channel and, thus, impair RdRp activity
additional information
-
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
Q8H1K9
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
Q9LKP0
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
-
the nonstructural viral protein P1 is a component of the RdRp complex. The P1 protein is associated with at least six proteins in the infected cell
additional information
-
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
Cystovirus phi6
-
structure-function analysis, molecular mapping, overview
additional information
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
-
the enzyme contains four different subunits: I, II, II and IV. The molecular weights of which are 74000 Da, 60000 Da, 47000 Da and 36000 Da, respectively. Three of them, I, III and IV are host-coded proteins, ribosomal protein S1 and elongation factor Tu(III) and Ts(IV)
additional information
-
open and closed enzyme conformation, and enzyme domain structure, structure-function relationship, overview
additional information
-
structure of the RNA polymerase of poliovirus (1RA6) with subdomains fingers, palm, and thumb. Molecular dynamics simulations
additional information
-
Qbeta replicase is composed of the bacteriophage Qbeta catalytic beta-subunit as well as the Escherichia coli host translation elongation factors EF-Tu and EF-Ts
additional information
-
enzyme domain structure, structure-function relationship, overview
additional information
-
enzyme domain structure, structure-function relationship, overview
-
additional information
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
-
the enzyme is part, as RdRp_2 domain, of a 253-kDa polyprotein that also contains a papain-like protease, a methyltransferase, AlkB and helicase domains, a 5.2-kDa hydrophobic protein, a 58.5-kDa heat shock 70 protein homologue, a 60-kDa protein, a 30-kDa coat protein, and a 23-kDa protein
additional information
-
the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
additional information
-
open and closed enzyme conformation, and enzyme domain structure, structure-function relationship, overview
additional information
-
open and closed enzyme conformation, and enzyme domain structure, structure-function relationship, overview
-
additional information
-
the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
additional information
-
open and closed enzyme conformation, and enzyme domain structure, structure-function relationship, overview
additional information
-
open and closed enzyme conformation, and enzyme domain structure, structure-function relationship, overview
-
additional information
open and closed enzyme conformation, and enzyme domain structure, structure-function relationship, overview
additional information
-
polymerase FluPol is composed of three polypeptides: PB1, PB2 and PA/P3. PB1 houses the polymerase active site, whereas PB2 and PA/P3 contain, respectively, cap-binding and endonuclease domains required for transcription initiation by cap-snatching. The apo-enzyme in closed conformation forms a compact particle with PB1 at its centre, capped on one face by PB2 and clamped between the two globular domains of P3. The endonuclease domain of P3 and the domains within the carboxy-terminal two-thirds of PB2 are completely rearranged. The cap-binding site is occluded by PB2, resulting in a conformation that is incompatible with transcription initiation. Tremendous flexibility of the protein complex. Comparison of apo-FluPolC with promoter-bound FluPolA
additional information
-
the RNA-dependent RNA polymerase of arenaviruses is an integral part of the L protein, a 200-kDa multifunctional and multidomain protein, structure and function of the Lassa virus RdRp domain, folding model of the domain, overview
additional information
-
the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
additional information
-
the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
additional information
-
RNA-dependent RNA polymerase complex, which consists of L protein (250000 Da) and P proteins (80000 Da)
additional information
-
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
-
the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
additional information
-
enzyme domain structure, structure-function relationship, overview
additional information
-
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
Q8LTE0
Qbeta replicase is composed of the bacteriophage Qbeta catalytic beta-subunit as well as the Escherichia coli host translation elongation factors EF-Tu and EF-Ts
additional information
crystal structure of RHDV RdRp reveals that the enzyme adopts a shape that resembles a right hand, with domains corresponding to the fingers, palm and thumb
additional information
-
crystal structure of RHDV RdRp reveals that the enzyme adopts a shape that resembles a right hand, with domains corresponding to the fingers, palm and thumb
additional information
-
crystal structure of RHDV RdRp reveals that the enzyme adopts a shape that resembles a right hand, with domains corresponding to the fingers, palm and thumb
-
additional information
-
the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
additional information
the core polymerase in respiratory syncytial virus (RSV) is composed of two proteins, a 250 kDa polymerase subunit (L), which contains the RNA-dependent RNA polymerase, the polyribonucleotidyl transferase (PRNTase, capping), and the methyltransferase enzymatic domains essential for viral transcription and replication, and the 27 kDa phosphoprotein (P) accessory protein
additional information
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
additional information
a transition model from the nsp7-nsp8 hexadecameric primase complex to the nsp12-nsp7-nsp8 polymerase complex is proposed to provide clues for the understanding of the coronavirus transcription and replication machinery
additional information
-
a transition model from the nsp7-nsp8 hexadecameric primase complex to the nsp12-nsp7-nsp8 polymerase complex is proposed to provide clues for the understanding of the coronavirus transcription and replication machinery
additional information
cryo-electron microscopy structure of COVID-19 virus full-length nsp12 in complex with cofactors nsp7 and nsp8 at 2.9 A resolution
additional information
-
cryo-electron microscopy structure of COVID-19 virus full-length nsp12 in complex with cofactors nsp7 and nsp8 at 2.9 A resolution
additional information
cryo-electron microscopy structure of the SARS-CoV-2 RdRp in an active form that mimics the replicating enzyme. The structure comprises the viral proteins non-structural protein 12 (nsp12), nsp8 and nsp7, and more than two turns of RNA template-product duplex. The active-site cleft of nsp12 binds to the first turn of RNA and mediates RdRp activity with conserved residues. Two copies of nsp8 bind to opposite sides of the cleft and position the second turn of RNA. Long helical extensions in nsp8 protrude along exiting RNA, forming positively charged sliding poles
additional information
-
cryo-electron microscopy structure of the SARS-CoV-2 RdRp in an active form that mimics the replicating enzyme. The structure comprises the viral proteins non-structural protein 12 (nsp12), nsp8 and nsp7, and more than two turns of RNA template-product duplex. The active-site cleft of nsp12 binds to the first turn of RNA and mediates RdRp activity with conserved residues. Two copies of nsp8 bind to opposite sides of the cleft and position the second turn of RNA. Long helical extensions in nsp8 protrude along exiting RNA, forming positively charged sliding poles
additional information
cryo-EM structure of SARS-CoV-2 nsp12-nsp7-nsp8 core polymerase complex. The structure of the SARS-CoV-2 nsp12-nsp7-nsp8 complex is determined at 3.7-A resolution. The SARSCoV-2 polymerase complex consists of the nsp12 catalytic subunit and nsp7-nsp8 cofactors
additional information
-
cryo-EM structure of SARS-CoV-2 nsp12-nsp7-nsp8 core polymerase complex. The structure of the SARS-CoV-2 nsp12-nsp7-nsp8 complex is determined at 3.7-A resolution. The SARSCoV-2 polymerase complex consists of the nsp12 catalytic subunit and nsp7-nsp8 cofactors
additional information
evolutionary connection between the catalytic subunits of DNA-dependent RNA polymerases and eukaryotic RNA-dependent RNA polymerases. Eukaryotic RNA-dependent RNA polymerases share the catalytic double psi barel domain, containing a signature metal-coordination motif, with the universally conserved beta-subunit of DNA-dependent RNA polymerase
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
phosphoprotein
-
the enzyme consists of the phosphoprotein and the large protein, phosphorylation of the phosphoprotein at the CKII sites is not required, while phosphorylation by host kinases AKT1 and PLK1 are critical for paramyxovirus RNA synthesis with a regulatory role
phosphoprotein
-
RdRp phosphorylation by PRK2 is required for activation and RNA replication
phosphoprotein
-
the enzyme consists of the phosphoprotein and the large protein, phosphorylation of the phosphoprotein at the CKII sites is not required, while phosphorylation by host kinases AKT1 and PLK1 are critical for paramyxovirus RNA synthesis with a regulatory role
phosphoprotein
-
the enzyme consists of the phosphoprotein and the large protein, phosphorylation of the phosphoprotein at the CKII sites is not required, while phosphorylation by host kinases AKT1 and PLK1 are critical for paramyxovirus RNA synthesis with a regulatory role
phosphoprotein
-
the enzyme consists of the phosphoprotein and the large protein, phosphorylation of the phosphoprotein at the CKII sites is not required, while phosphorylation by host kinases AKT1 and PLK1 are critical for paramyxovirus RNA synthesis with a regulatory role
phosphoprotein
-
the enzyme consists of the phosphoprotein and the large protein, phosphorylation of the phosphoprotein at the CKII sites is not required, while phosphorylation by host kinases AKT1 and PLK1 are critical for paramyxovirus RNA synthesis with a regulatory role
phosphoprotein
-
the enzyme consists of the phosphoprotein and the large protein, phosphorylation of the phosphoprotein at the CKII sites is not required, while phosphorylation by host kinases AKT1 and PLK1 are critical for paramyxovirus RNA synthesis with a regulatory role
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapour-diffusion with sitting drops, structure of a truncated enzyme form (residues 71-679 with a C-terminal His tag), structure of a truncated enzyme form (residues 71-679 with a C-terminal His tag) complexed with GTP, determined at 2.9 A resolution
crystallization using a nanolitre-drop crystallization robot, 2.1 A resolution
-
in complex with its protein primer VPg and diphosphate, hanging drop vapour diffusion method, in 20 mM Tris (pH 9.0), 300 mM NaCl, 15% glycerol, 0.5 mM Tris(2-carboxyethyl)phosphine
-
nanolitre-drop crystallization, with 2.0 M (NH4)2SO4, 100 mM CAPS pH 10.5, 200 mM Li2SO4
-
hanging drop vapour diffusion method, using 0.1 M Tris-HCl at pH 8.5, 0.8 M potassium-sodium tartrate, 0.5% (w/v) PEG monomethyl ether 5000
Q6DLV0
hanging drop vapour diffusion method, with 0.1 M Tris-HCl pH 8.5, 0.8 M potassium/sodium tartrate, and 0.5% (w/v) PEG monomethyl ether 5000
-
hanging-drop vapor diffusion method at 4°C, three-dimensional structure of a catalytically active DENV RdRp domain determined to 1.85 A resolution by X-ray crystallography
Q6DLV0
native and in complex with inhibitor 5-[[(4-chlorophenyl)sulfonyl]amino]-2-methyl-1-benzofuran-3-carboxylic acid, to 1.79 and 2.1 A resolution, respectively. The inhibitor binds to the protein as a dimer and causes conformational changes in the protein
Q6DLV0
purified enzyme in complex with NTP substrate, X-ray diffraction structure determination and analysis at 2.45-2.78 A resolution, analysis of multiple nucleotide-incorporation events and different NAC states
-
crystal structure of poliovirus 3CD protein, a virally encoded protease and precursor to the RNA-dependent RNA polymerase
-
hanging drop vapor diffusion at 16°C using 12 mg/ml protein. Full-length enzyme at 2.0 A resolution, enzyme in complex with GTP at 2.35 A resolution, mutant enzyme G1A and and DELTA68
-
hanging drop vapour diffusion method, with 2 M ammonium sulfate, 0.1 M HEPES (pH 7.0), and 0.3% Jeffamine M600 (pH 7.0)
-
sitting drop vapor diffusion method at 14°C, crystal structure of the enzyme (RdRp) in the apo state and in complex with the inhibitor NADPH
-
structure of Qbeta replicase complex, to 2.5 A resolution. Qbeta replicase is composed of the bacteriophage Qbeta catalytic beta-subunit as well as the Escherichia coli host translation elongation factors EF-Tu and EF-Ts. The basic catalytic machinery in the viral subunit appears similar to other RNA-dependent RNA polymerases, while a C-terminal region of the beta-subunit engages in extensive interactions with EF-Tu and may contribute to the separation of the transient duplex formed between the template and the nascent product to allow exponential amplification of the phage genome
-
hanging-drop vapour-diffusion method, structure of the enzyme in a free form at 1.9 A resolution and in complex with a template-primer RNA decanucleotide at 3.0 A resolution
-
HCV NS5B polymerase by hanging drop method at room temperature using a well buffer of 20% PEG 4000, 50 mM ammonium sulfate, 100 mM sodium acetate, pH 4.7, with 5 mM DTT, complexes are prepared by soaking the crystals for 3-24 h in solutions containing 15-20% DMSO, 20% glycerol, 20% PEG 4000, 0.1 M Hepes and 10 mM MgCl2 at pH 7.6 and an inhibitor concentration of 2-10 mM, X-ray diffraction structure determination and analysis at 2.6 A resolution for compound 29 and 2.15 A for compound 49
a large fragment of subunit PA bound to a fragment of subunit PB1, hanging dropn vapour diffusion method, 20°C, mixing of 0.001 ml of protein solution, containing 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, and 100 mM sodium chloride, and 0.001 ml of reservoir solution consisting of 100 mM Tris-HCl, pH 7.5, and 2.4 M sodium formate, X-ray diffraction structure determination and analysis at 2.3 A resolution
purified recombinant enzyme, at 20°C by the hanging drop method using a protein solution of 5-10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 100 mM NaCl and 2.5 mM MnCl2 and a reservoir composition of 1.2 M Li2SO4, 100 mM MES, pH 6.0, 10 mM Mg acetate and 3% ethylene glycol
purified apo-FluPol in closed conformation, sitting-drop vapour-diffusion, protein:precipitant ratio of 2:1, mixing of 5 mg/ml protein with either 70% v/v Morpheus G2, supplemented with 0%-1% 1 M NaOH, to generate P43212 crystals, or with crystal-seeds and 0.2 M NaCl, 0.1 M Na-HEPES, pH 7.5, and 25% w/v PEG 4000 for P212121 crystals, 20°C, heavy atom derivatization by P43212 crystals soaking in a solution of gold(I) potassium cyanide dissolved in mother liquor, for 2-3 h at 20°C, X-ray diffraction structure determination and analysis at 3.9 A resolution
-
purified recombinant enzyme in apo-form or in complex with ATP or GTP, jRdRp (0.08 mM) is incubated with GTP/ATP (5 mM) for 30 min before setting crystallization trials, screening and method optimization, hanging drop vapour diffusion method, mixing of protein-ATP/GTP with 10-18% w/v PEG 4000, 100 mM Tris-Cl buffer, pH 8.0, and 7% v/v 1-propanol, 25°C, for the apo-enzyme mixing of 0.096 mM protein with 10-15% PEG 5000 mono methyl ether, 100 mM Tris-Cl, pH 8.0, and 200mM NaSCN, 25°C, X-ray diffraction structure determination and analysis at 2.28-3.65 A resolution, molecular replacement using the apo-enzyme structures of WNV and DENV, PDB IDs 2HFZ and 2J7W, as search models
in-silico docking search of inhibitors. The location of inhibitors 8,8'-[carbonylbis(iminobenzene-3,1-diylcarbonylimino)]dinaphthalene-1,3,5-trisulfonic acid and Suramin inner head is stabilized by offset-tilted aromatic/aromatic interaction with residue Trp42
-
in-silico docking search of inhibitors. The location of inhibitors 8,8'-[carbonylbis(iminobenzene-3,1-diylcarbonylimino)]dinaphthalene-1,3,5-trisulfonic acid and Suramin inner head is stabilized by offset-tilted aromatic/aromatic interaction with residue Trp41
-
a complex of Norovirus RNA-dependent RNA polymerase bound to Mn2+ and an RNA primer-template duplex is investigated using X-ray crystallography and hybrid quantum chemical/molecular mechanical simulations. The complex crystallizes in a tetragonal crystal form. The nature of the primer/template duplex binding in the resulting structure indicates that the complex is a closed back-tracked state of the enzyme, in which the 3'-end of the primer occupies the position expected for the postincorporated nucleotide before translocation. Computationally, it is found that the complex can accept a range of divalent metal cations without marked distortions in the active site structure. The highest binding energy is for copper, followed closely by manganese and iron, and then by zinc, nickel, and cobalt
-
enzyme in two crystal forms A and B, method screening, 300 nl of 6-20 mg/ml protein in 50 mM Tris, 100 mM NaCl, and 2 mM DTT, pH 8.0, are mixed with reservoir solution containing 4.0 M sodium formate, 0.2 M magnesium formate, and 20% w/v PEG 3350, in hanging drops at 20°C, or with 4.3 M NaCl, 0.1 M HEPES, and 30 mM tri-glycine in sitting drops at room temperature, X-ray diffraction structure determination and analysis at resolutions of 1.7 A and 2.1 A, respectively. Form A contains Mg2+ bound at a site that deviates from the canonical non-catalytic position seen in form B
structure of Qbeta replicase complex, to 2.5 A resolution. Qbeta replicase is composed of the bacteriophage Qbeta catalytic beta-subunit as well as the Escherichia coli host translation elongation factors EF-Tu and EF-Ts. The basic catalytic machinery in the viral subunit appears similar to other RNA-dependent RNA polymerases, while a C-terminal region of the beta-subunit engages in extensive interactions with EF-Tu and may contribute to the separation of the transient duplex formed between the template and the nascent product to allow exponential amplification of the phage genome
Q8LTE0
overall structure of the sapovirus 3Dpol is determined by X-ray crystallography to 2.32 A resolution
-
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D682A
-
site-directed mutagenesis of the central polymerase domain 1 active site residue
D683A
-
site-directed mutagenesis of the central polymerase domain 1 active site residue
C768Y
Q9LKP0
a C-to-T missense mutation in the first exon, the naturally occuring mutant rdr6-11 of RDR6 shows simultaneously enhanced SI and stigma exsertion, without associated increases in SRK transcript levels, phenotype, overview. The mutant exhibits stochastic stigma exsertion, and the S-locus receptor kinase, SRK, gene further enhances pistil elongation and stigma exsertion in this mutant background, a process that requires SRK catalytic activity and correlates with SRK transcript levels. rdr6-11 mutant plants are fertile and produce full siliques. By contrast, self-pollination of rdr6-11::Sb stigmas results in very low numbers of seeds per silique, indicating that mutant stigmas maintain SI into late stages of flower development even upon prolonged pollen-stigma contact
E291G
mutant is insensitive against inhibitor ethyl 2-methylimidazo[1,2-a]pyrrolo[2,3-c]pyridin-8-carboxylate
F224P
-
2-phenyl-N-(1-phenyl-1H-pyrazol-3-yl)-4-quinolinecarboxamide (CSFCII) resistant bovine viral diarrhea virus variants carry the F224P mutation in the viral RNA-dependent RNA polymerase (RdRp)
F224S
mutant is insensitive against inhibitors ethyl 2-methylimidazo[1,2-a]pyrrolo[2,3-c]pyridin-8-carboxylate, 5-[(4-bromophenyl)methyl]-2-phenyl-5H-imidazo[4,5-c]pyridine, and VP32947
F224Y/N264D
-
2-(2-furanyl)-N-(6-methyl-2-benzothiazolyl)-4-quinolinecarboxamide (CSFCI) resistant bovine viral diarrhea virus variants carry two mutations in the viral RNA-dependent RNA polymerase (RdRp), N264D and F224Y
F364A
-
the hydrophobic mutation leads to conformations with closed active site
F364W
-
the mutant enzym has no preference between the open and closed active sites, similar to wild-type enzyme
E1069A
-
the mutation in RNA-dependent RNA polymerase can prevent the superinfection of the virus, with protection efficiency of 100%
E634Q
Cystovirus phi6
-
site-directed mutagenesis in the specificity pocket, the mutation to glutamine E634 eliminates this salt bridge without major disruption of the internal packaging within the polymerase
K541A
Cystovirus phi6
-
site-directed mutagenesis in the rim of the template tunnel, the mutation reduces both the positive charge as well as the size and shape of the template tunnel rim
K541L
Cystovirus phi6
-
site-directed mutagenesis in the rim of the template tunnel, the mutation reduces both the positive charge as well as the size and shape of the template tunnel rim
R30A
Cystovirus phi6
-
site-directed mutagenesis in the rim of the template tunnel, the mutation reduces both the positive charge as well as the size and shape of the template tunnel rim
D238A
D238E
-
poly(rU) polymerase activity determined by using dT15/rA30 in presence of Mn2+ is 45% of the activity of the wild-type enzyme. AMP incorporation in presence of Mg2+, at 0.1 mM ATP, is 0.04% of the activity of the wild-type enzyme. AMP incorporation in presence of Mn2+, at 0.1 mM ATP, is 0.74% of the activity of the wild-type enzyme
D238F
-
poly(rU) polymerase activity determined by using dT15/rA30 in presence of Mn2+ is 4.4% of the activity of the wild-type enzyme. No AMP incorporation activity in presence of Mn2+ or Mg2+
D238N
-
poly(rU) polymerase activity determined by using dT15/rA30 in presence of Mn2+ is 45% of the activity of the wild-type enzyme. AMP incorporation in presence of Mg2+, at 0.1 mM ATP, is 0.05% of the activity of the wild-type enzyme. AMP incorporation in presence of Mn2+, at 0.1 mM ATP, is 0.797% of the activity of the wild-type enzyme
D238V
-
poly(rU) polymerase activity determined by using dT15/rA30 in presence of Mn2+ is 11% of the activity of the wild-type enzyme. No AMP incorporation activity in presence of Mn2+ or Mg2+
D339A/S341A/D349A
-
site-directed mutagenesis, the mutant shows a partial loss of oligomerization with the less severe viral phenotype
G1A
-
mutant is only partially active and the N-terminal hydrogen-bonding network is partly disrupted
G64S
IF-PS-KH I331F/P356S/K359H
-
the triple mutant replicates even faster but still exhibits a significant reduction in the rate of replication relative to wild-type enzyme. The virus is impaired substantially for recombination in cells
K359H
-
the mutant enzyme catalyzes nucleotidyl transfer at a rate 10fold lower than wild-type. K359H poliovirus is genetically unstable and acquires mutations encoding two second-site amino acid substitutions after a few passages in cell cultures
K359R
-
the mutant enzyme catalyzes nucleotidyl transfer at a rate 10fold lower than wild-type
L446N/R455A/R456A
-
site-directed mutagenesis, catalytically complete inactive mutant
L446N/R455A/R456A/D328A/D329A
-
site-directed mutagenesis, catalytically complete inactive mutant
N297A
N297D
-
poly(rU) polymerase activity determined by using dT15/rA30 in presence of Mn2+ is 89% of the activity of the wild-type enzyme. AMP incorporation in presence of Mg2+, at 0.1 mM ATP, is 38.2% of the activity of the wild-type enzyme. AMP incorporation in presence of Mn2+, at 0.1 mM ATP, is 21.2% of the activity of the wild-type enzyme
N297Q
-
poly(rU) polymerase activity determined by using dT15/rA30 in presence of Mn2+ is about 35% of the activity of the wild-type enzyme. AMP incorporation in presence of Mg2+, at 0.1 mM ATP, is 1.4% of the activity of the wild-type enzyme. AMP incorporation in presence of Mn2+, at 0.1 mM ATP, is 0.72% of the activity of the wild-type enzyme
N297V
-
poly(rU) polymerase activity determined by using dT15/rA30 in presence of Mn2+ is about 55% of the activity of the wild-type enzyme. AMP incorporation in presence of Mg2+, at 0.1 mM ATP, is 15.3% of the activity of the wild-type enzyme. AMP incorporation in presence of Mn2+, at 0.1 mM ATP, is 4.9% of the activity of the wild-type enzyme
PS-KH P356S/K359H
-
the mutant is competent for forced-copy-choice recombination
R455A/R456A
-
site-directed mutagenesis, catalytically complete inactive mutant
V391L
-
naturally occuring mutant, temperature-sensitive mutant. Some function of V391L polymerase other than its catalytic activity can be supplemented at the nonpermissive temperature, most likely via the formation of oligomeric structures on the surface of membranous vesicles that facilitate the tethering of the active enzyme
K802A
-
grapevine fanleaf virus produces characteristic symptoms of vein clearing in apical leaves in its systemic host Nicotiana benthamiana. The mutation abolishes symptom expression
K802G
-
grapevine fanleaf virus produces characteristic symptoms of vein clearing in apical leaves in its systemic host Nicotiana benthamiana. The mutation abolishes symptom expression
K802N
-
grapevine fanleaf virus produces characteristic symptoms of vein clearing in apical leaves in its systemic host Nicotiana benthamiana. The mutation attenuates symptom expression
K802P
-
grapevine fanleaf virus produces characteristic symptoms of vein clearing in apical leaves in its systemic host Nicotiana benthamiana. The mutation attenuates symptom expression
K802Q
-
grapevine fanleaf virus produces characteristic symptoms of vein clearing in apical leaves in its systemic host Nicotiana benthamiana. The mutation abolishes symptom expression
A396G
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
A421V
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
C575S
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
D225A
-
mutant enzyme is capable of robust de novo initiation in the presence of Mn2+, produces reduced amounts of product of 38 nt and longer that arose from template switch
E440G
naturally occuring mutation, location in the protein and role in RNA binding, overview
I11V
naturally occuring mutation, location in the protein and role in RNA binding, overview
I11V/I454V
naturally occuring mutation, location in the protein and role in RNA binding, overview
I239L
the mutation occurs under PSI-6130 selection in cell culture, it increases the enzyme activity compared to the wild-type enzyme
I239V
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
I432V
naturally occuring mutation, location in the protein and role in RNA binding, overview
I454V
naturally occuring mutation, location in the protein and role in RNA binding, overview
I482S
-
mutant confers resistance to AG-021541 and structurally related compounds but remains sensitive to interferon and HCV polymerase inhibitors known to interact with the active site or other allosteric sites of the protein
I482T
-
mutant confers resistance to AG-021541 and structurally related compounds but remains sensitive to interferon and HCV polymerase inhibitors known to interact with the active site or other allosteric sites of the protein
K72M
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
K72M/S282T
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
K72M/S282T/L564M
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
K81R
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
K81R/S282T
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
K81S/S282T
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
L320F
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
M423I
-
mutant confers resistance to AG-021541 and structurally related compounds but remains sensitive to interferon and HCV polymerase inhibitors known to interact with the active site or other allosteric sites of the protein
M423T
-
mutant confers resistance to AG-021541 and structurally related compounds but remains sensitive to interferon and HCV polymerase inhibitors known to interact with the active site or other allosteric sites of the protein
M423V
-
mutant confers resistance to AG-021541 and structurally related compounds but remains sensitive to interferon and HCV polymerase inhibitors known to interact with the active site or other allosteric sites of the protein
M426T
-
mutant confers resistance to AG-021541 and structurally related compounds but remains sensitive to interferon and HCV polymerase inhibitors known to interact with the active site or other allosteric sites of the protein
P495A
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation decreases RNA replication in the cell
P496A
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation decreases RNA replication in the cell
P538T
naturally occuring mutation, location in the protein and role in RNA binding, overview
Q438R
naturally occuring mutation, location in the protein and role in RNA binding, overview
Q438R/E440G
naturally occuring mutation, location in the protein and role in RNA binding, overview
R158A/R367A/R386A
-
mutation eliminates de novo initiation product even in presence of Mn2+, but enzyme is capable of primer extension
R158A/R386A
-
mutation eliminates de novo initiation product even in presence of Mn2+, but enzyme is capable of primer extension
R158A/R394A
-
mutation eliminates de novo initiation product even in presence of Mn2+, but enzyme is capable of primer extension
R32A
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation decreases RNA replication in the cell
R32K
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation decreases RNA replication in the cell
R32S
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation decreases RNA replication in the cell
R503A
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation completely ablates RNA replication in the cell
R556V
naturally occuring mutation, location in the protein and role in RNA binding, overview
S282S/T/C575S/Y586C
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T
S282T/A396G
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/A421V
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/C575S
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/I239L
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/I239L/A396G
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/I239L/A396G/V485L
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/I239S
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/I239V
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/I239V/A396G
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/K81R/S84S/P I239L/A300T/L320F/L/C, A421V, Y586C
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/L320F
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/L320S
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S282T/Y586C
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
S29A
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation decreases RNA replication in the cell
S556G
naturally occuring mutation, location in the protein and role in RNA binding, overview
S96T/N142T
the mutation of the NS5B polymerase mediates resistance to R7128. Long-term culture selection with PSI-6130 in replicon cells harboring preexisting mutation S96T/N142T results in the emergence of the S282T substitution and the reversion of S96T to wild-type serine
V405L
naturally occuring mutation, location in the protein and role in RNA binding, overview
V494A
-
mutant confers resistance to AG-021541 and structurally related compounds but remains sensitive to interferon and HCV polymerase inhibitors known to interact with the active site or other allosteric sites of the protein
V499A
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation increases RNA replication in cells
V499G
-
mutation in the rGTP-specific binding site does not cause a decrease in RNA-dependent RNA polymerase in vitro. Mutation completely ablates RNA replication in the cell
W550R
naturally occuring mutation, location in the protein and role in RNA binding, overview
Y586C
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme
L640D
the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme
L666D
the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme
V636S
the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme
W706A
the mutant of the PA subunit shows reduced transcriptional activity compared to the wild-type enzyme
D536A
D541A
site-directed mutagenesis, the mutant's elongation activity is marginally reduced compared to the wild-type enzyme
D668A
D669A
D669N
G605A
K691A
R734A
site-directed mutagenesis, the mutant catalyzes elongation almost identically to the wild-type enzyme
R742A
site-directed mutagenesis, the mutant catalyzes elongation almost identically to the wild-type enzyme
S604A
site-directed mutagenesis, the mutant's elongation activity is marginally reduced compared to the wild-type enzyme
S604A-D541A
site-directed mutagenesis, the mutant shows no detectable primer extension activity
S799A
site-directed mutagenesis, the mutant catalyzes elongation almost identically to the wild-type enzyme
S799Y
site-directed mutagenesis, the mutant catalyzes elongation almost identically to the wild-type enzyme
D536A
K691A
D541A
-
site-directed mutagenesis, the mutant's elongation activity is marginally reduced compared to the wild-type enzyme
-
R734A
-
site-directed mutagenesis, the mutant catalyzes elongation almost identically to the wild-type enzyme
-
R742A
-
site-directed mutagenesis, the mutant catalyzes elongation almost identically to the wild-type enzyme
-
S799A
-
site-directed mutagenesis, the mutant catalyzes elongation almost identically to the wild-type enzyme
-
S799Y
-
site-directed mutagenesis, the mutant catalyzes elongation almost identically to the wild-type enzyme
-
Y41A
-
mutation in inhibitor-binding site, about 5fold increase in IC50 values for inhibitors suramin and 8,8'-[carbonylbis(iminobenzene-3,1-diylcarbonylimino)]dinaphthalene-1,3,5-trisulfonic acid
N812A
active site variant of RSV L-protein in the RSV L/P complex. The RSV L(N812A)/P complex does not produce RNA products with TrC sequence RNA as template
A185V
mutation causes change in secondary structure
A466V
mutation has no effect on secondary structure
A97V
mutation causes change in secondary structure
I201L
mutation has no effect on secondary structure
L329I
mutation has no effect on secondary structure
P323L
mutation causes change in secondary structure
V880I
mutation has no effect on secondary structure
A365N
mutation selected to stabilize the secondary structural elements near the rNTP binding pocket of the enzyme. Mutant viruses were tested in vitro on Vero, C6/36, Culex tarsalis and DF-1 cell types and in vivo in one day old chickens and Culex pipiens mosquitoes. Mutation affects plaque morphology and particularly alters growth and RNA replication kinetics
T363N
mutation selected to stabilize the secondary structural elements near the rNTP binding pocket of the enzyme. Mutant viruses were tested in vitro on Vero, C6/36, Culex tarsalis and DF-1 cell types and in vivo in one day old chickens and Culex pipiens mosquitoes. Mutation affects plaque morphology and alters growth and RNA replication kinetics
T537I
mutation selected to stabilize the secondary structural elements near the rNTP binding pocket of the enzyme. Mutant viruses were tested in vitro on Vero, C6/36, Culex tarsalis and DF-1 cell types and in vivo in one day old chickens and Culex pipiens mosquitoes. Mutation affects plaque morphology and alters growth and RNA replication kinetics
A365N
-
mutation selected to stabilize the secondary structural elements near the rNTP binding pocket of the enzyme. Mutant viruses were tested in vitro on Vero, C6/36, Culex tarsalis and DF-1 cell types and in vivo in one day old chickens and Culex pipiens mosquitoes. Mutation affects plaque morphology and particularly alters growth and RNA replication kinetics
-
T363N
-
mutation selected to stabilize the secondary structural elements near the rNTP binding pocket of the enzyme. Mutant viruses were tested in vitro on Vero, C6/36, Culex tarsalis and DF-1 cell types and in vivo in one day old chickens and Culex pipiens mosquitoes. Mutation affects plaque morphology and alters growth and RNA replication kinetics
-
T537I
-
mutation selected to stabilize the secondary structural elements near the rNTP binding pocket of the enzyme. Mutant viruses were tested in vitro on Vero, C6/36, Culex tarsalis and DF-1 cell types and in vivo in one day old chickens and Culex pipiens mosquitoes. Mutation affects plaque morphology and alters growth and RNA replication kinetics
-
S604T
-
the mutation confers resistance to nucleotide inhibitors, also conferred resistance to sofosbuvir triphosphate but not to 5-azidomethyl-3-hydroxy-4-hydroxymethyl-pyridine-2-carboxylic acid hydroxyamide
additional information
D238A
-
poly(rU) polymerase activity determined by using dT15/rA30 in presence of Mn2+ is 45% of the activity of the wild-type enzyme. AMP incorporation in presence of Mg2+, at 0.1 mM ATP, is 0.24% of the activity of the wild-type enzyme. AMP incorporation in presence of Mn2+, at 0.1 mM ATP, is 1.9% of the activity of the wild-type enzyme
D238A
-
mutation destabilizes the catalytically competent enzyme-primer/template-NTP complex and reduces the efficiency of phosphoryl transfer
G64S
-
mutation of the key structural element of the alpha-helix in poliovirus RdRP, leads to the appearance of virus that reproduced better than the wild-type, the mutation stabilizes the interaction f Gly64 with residues Ala239 and Leu241 of the fingers subdomain
N297A
-
poly(rU) polymerase activity determined by using dT15/rA30 in presence of Mn2+ is 89% of the activity of the wild-type enzyme. AMP incorporation in presence of Mg2+, at 0.1 mM ATP, is 11.2% of the activity of the wild-type enzyme. AMP incorporation in presence of Mn2+, at 0.1 mM ATP, is 4.5% of the activity of the wild-type enzyme
N297A
-
mutation destabilizes the catalytically competent enzyme-primer/template-NTP complex and reduces the efficiency of phosphoryl transfer
S282T
-
the mutation shows reduced sensitivity to 2'-hydroxy-2'-C-methyl nucleosides
S282T
the mutation occurs under PSI-6130 selection in cell culture, it reduces the enzyme activity compared to the wild-type enzyme. The mutation of the NS5B polymerase mediates a three to sixfold loss of sensitivity to PSI-6130 compared to the wild-type enzyme, lack of cross-resistance between PSI-6130 and R1479, overview
D669N
-
reduction in activity to about 5% relative to the parental NS5
D669N
-
mutant shows a reduction in activity to about 5% relative to the wild type enzyme
additional information
-
construction of dr2 knockout mutant plants, rdr2-1, showing reduced asymmetric 5S rDNA methylation at chromosomes 4 and 5 compared to the wild-type enzyme
additional information
-
construction of rdr1 and rdr6 mutants, that exhibit globally reduced levels of viral small RNA production as well as reduced strand bias in viral small RNA population, revealing an important role for these host RDRs in viral siRNA biogenesis, analysis of Tobacco Mosaic Virus small RNA profile in Arabidopsis thaliana wild-type plants as well as rdr mutants rdr1-1 and rdr6-15 by applying small RNA deep sequencing technology, overview
additional information
-
RNA-dependent RNA polymerase activity remains in truncated proteins coding for the amino acids from position 514 or 893 to the C terminus
additional information
-
identification of RRF-3 siRNAs, overview. RRF-3 suppression by siRNA results in pleiotropic effects in sperm development, the sperm defects lead to embryonic lethality, nuclei of the mutant sperms are surrounded by ectopic microtubule structures with spindle abnormalities, phenotype, overview
additional information
-
identification of RRF-3 siRNAs, overview. RRF-3 suppression by siRNA results in pleiotropic effects in sperm development, the sperm defects lead to embryonic lethality, nuclei of the mutant sperms are surrounded by ectopic microtubule structures with spindle abnormalities, phenotype, overview
-
additional information
-
construction of several chimeras of a tobacco mosaic virus/oilseed rape mosaic virus RdRp chimeric mutant, the R-54k chimera consiting of a hybrid TMV-ORMV RdRp gene, and MP and CP genes of TMV, with an ORMV polymerase domain. Arabidopsis thaliana plants, RLD and Can-0 ecotypes, give nonuniform responses when inoculated with the chimeras
additional information
-
truncated enzyme forms resulting from deletions of 24, 36, or amino acid residues at the C terminal have RNA-dependent RNA polymerase activity. Truncated enzyme with a deletion of 82 amino acid residues at the C terminal shows no RNA-dependent RNA polymerase activity. Template specificity of the enzyme is not strict wirth NS5B proteins truncated, suggesting that the C terminal of CSFV NS5B protein is involved in the template specificity of the enzyme
additional information
Cystovirus phi6
-
structure-based mutagenesis of the enzyme, the elongation rates are not compromised by the mutations, while the transcription rates vary, phenotypes, overview
additional information
-
construction of D-elp1 protein mutants through (1-1252 aa) and the DELTAC (1-843aa) and DELTAN (844-1252 aa) deletions. D-elp1 depletion inhibits RNAi in S2 cells but does not affect micro RNA function. D-elp1 depletion results in increased steady state levels of representative transposon RNAs and a decrease in the corresponding transposon antisense transcripts and endo siRNAs. In D-elp1 null third instar larvae transposon RNA levels are also increased and the corresponding transposon antisense RNAs are reduced
additional information
-
a mutant is generated as a result of the deletion of a trinucleotide in the N-terminal portion of the coding region, pT7-POL(TRP-). The protein expressed from this mutant lacks a tryptophan residue normally present at the fifth amino acid from the N-terminal glycine. This protein has no detectable enzymatic activity. Mutant pT7-POL(AvII), which lacks the C-terminal 53 amino acids of the normal protein is also inactive
additional information
-
generation of mutant 3D polymerase plasmids through splicing by overlapping extension PCR. Mutation of the active site of 3D polymerase does not impede its ability to oligomerize or to participate in functional complexes, the catalytically inactive polymerases participate productively in functional oligomer formation and catalysis. But polymerases containing mutations in the amino terminus, which lead to altered contacts in the folded polymerase and mutations in a known polymerase-polymerase interaction in the two-dimensional protein lattice, cannot participate in functional RNA replication complexes
additional information
-
a hexahistidine affinity-tagged NS5B fusion protein is expressed with recombinant baculoviruses in insect cells
additional information
-
mutant cm20t in which 7 amino acids in a row are changed to AAASAAA from aa17-23, is totally defective in RNA-dependent RNA polymerase activity
additional information
-
mutant cm1940t in which 7 amino acids in a row are changed to AAASAAA from aa191-197, is totally defective in RNA-dependent RNA polymerase activity
additional information
-
mutant enzymes cm2t and cm3t are totally defective in RNA-dependent RNA polymerase activity
additional information
-
soluble Hepatitis C virus NS5B in the glutathione S-transferase-fused form NS5Bt which lacks the C-terminal 21 amino acid residues, expressed in Escherichia coli. The recombinant soluble enzyme exhibits RNA-dependent RNA polymerase activity in vitro which is dependent on template and primer, but it does not exhibit the terminal transferase activity
additional information
-
mutant enzyme cm223t in which 7 amino acids in a row are changed to AAASAAA from aa220-226, shows 50% of the activity of the wild-type enzyme
additional information
-
C-terminal hydrophobic domain deletion mutant, NS5B DELTAC21, shows increased solubility, the deletion also positively affects the polymerase activity
additional information
-
deletion of only 19 amino acids from the amino terminus severely reduces the polymerase activity, which is completely abolished when 40 amino acids are removed. Truncations from the carboxy terminus are less deleterious
additional information
-
removal of the C21 domain enhances the enzyme stability. Whereas RNA synthesis by the full-length enzyme remains relatively constant at 12-100 mM KCl, synthesis by DELTA21 truncation mutatnt rapidly decreases at KCl concentrations greater than 12 mM. Binding by DELTA21 mutant but not full-length enzyme decreases proportionally as the KCl concentration increases from 25 to 200 mM. The truncation mutant becomes severely inhibited at elevated NTP concentrations, which most likely is due to competitive binding of the noncomplementary nucleotide to the polymerase catalytic center
additional information
mutant activity analysis by transient replicon assay, overview
additional information
-
mutant activity analysis by transient replicon assay, overview
additional information
mutant NS5B DELTA21, produced by cells expressing the HCV replicon, shows increased ability to bind to RNA, with 8fold higher affinity compared to the wild-type, in the presence of cyclosporine A, overview. CsA-resistance mutations locate to two functionally related regions in NS5B structure. Purified recombinant NS5B mutants show higher de novo initiated RNA synthesis than the wild-type control
additional information
-
mutant NS5B DELTA21, produced by cells expressing the HCV replicon, shows increased ability to bind to RNA, with 8fold higher affinity compared to the wild-type, in the presence of cyclosporine A, overview. CsA-resistance mutations locate to two functionally related regions in NS5B structure. Purified recombinant NS5B mutants show higher de novo initiated RNA synthesis than the wild-type control
additional information
-
impairing the nuclear import of PB2 by mutating its nuclear localization signal leads to abnormal formation of the trimeric polymerase in the cytoplasm
additional information
-
the activity of the 6His-tagged enzyme HRV-16 3D polymerase is identical to HRV-16 3D polymerase without the 6His-tag
additional information
transfection of a mutant icDNA expressing an RdRp lacking the C-terminal disordered domain leads to a drastic reduction in the copy numbers of both forms of viral RNA. This could be due to the loss of interaction between the disordered domain of RdRp and P10 and possibly other viral/host proteins that might be required for the assembly of viral replicase
additional information
-
transfection of a mutant icDNA expressing an RdRp lacking the C-terminal disordered domain leads to a drastic reduction in the copy numbers of both forms of viral RNA. This could be due to the loss of interaction between the disordered domain of RdRp and P10 and possibly other viral/host proteins that might be required for the assembly of viral replicase
additional information
TMV-induced SlRDR1 expression is blocked by SlAOX1a silencing and enhanced by AOX activator, but SlRDR1 silencing does not influence TMV-induced SlAOX1a activation
additional information
silencing of the transcripts of StRDR1a and StRDR1b by dsRNA hairpin transcripts, expression of silencing constructs for StRDR1 does not affect the expression of the StRDR2 or the StRDR6 genes. Gene silencing does not affect the plant susceptibility to plant viruses, potato virus Y, potato virus X, and tobacco mosaic virus
additional information
-
silencing of the transcripts of StRDR1a and StRDR1b by dsRNA hairpin transcripts, expression of silencing constructs for StRDR1 does not affect the expression of the StRDR2 or the StRDR6 genes. Gene silencing does not affect the plant susceptibility to plant viruses, potato virus Y, potato virus X, and tobacco mosaic virus
additional information
-
construction of several chimeras of a tobacco mosaic virus/oilseed rape mosaic virus RdRp chimeric mutant, the R-54k chimera consisting of a hybrid TMV-ORMV RdRp gene, and MP and CP genes of TMV, with an ORMV polymerase domain. Arabidopsis thaliana plants, RLD and Can-0 ecotypes, give nonuniform responses when inoculated with the chimeras
additional information
-
construction of an RdRp-defective gRNA mutant
additional information
-
non-polyadenylated transcripts from a sampling of long-terminal repeat, LTR, retrotransposons are lost in rdr2 mutants
additional information
active-site mutation, GDD -> GAA, in amino acid positions 663 to 665 of NS5 causes the complete loss of NS5 polymerase activity
additional information
-
active-site mutation, GDD -> GAA, in amino acid positions 663 to 665 of NS5 causes the complete loss of NS5 polymerase activity
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
60 min, 40-60% loss of poly(G) polymerase activity, in presence of 2 mM guanine nucleotides loss of activity is up to 91% of the original specific activity
additional information
additional information
lower thermostability of individual nsp7-8-12 subunits of SARS-CoV-2 core polymerase complex compared with SARS-CoV core polymerase complex
additional information
-
lower thermostability of individual nsp7-8-12 subunits of SARS-CoV-2 core polymerase complex compared with SARS-CoV core polymerase complex
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
after one cycle of freezing at -70°C and thawing, the activity is about 90% of the unfrozen control, but is reduced to 40-50% after two cycles
-
the EF-Tu*Ts complex rather than the individual polypeptides functions in the renaturation of Qbeta replicase, treatment of pure EF-Tu with kiromycin prevents it from functioning in the renaturation of Qbeta replicase
-
the purified enzyme loses most of its activity within 45 min when dialyzed against 10 mM Tris-HCl, pH 8.1, 0.025 M NH4Cl, 0.01 M Kcl, containing only 5% glycerol and no mercaptoethanol, but little activity is lost under these conditions if the glycerol concentration is raised to 30%
-
very dilute polymerase preparations lose significant amounts of activity upon freezing and thawing. Stability is obtained by adding bovine serum albumin, 0.1 mg/ml in 25% or 50% glycerol buffers at -20°C or -80°C
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
urea
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15°C, buffer containing 30% glycerol, complete loss of activity after 2-3 days
-
-20°C, 50% glycerol-containing buffer, activity decreases by about 15% per month
-
-20°C, enzyme concentration greater than 1 mg/ml, stable for more than 1 year
-
-70°C, stored for several months without any detectable loss of activity
Foxtail mosaic potexvirus
-
-80°C, stable for at least 3 months
0°C, buffer containing 30% glycerol, complete loss of activity after 1-2 days
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a hexahistidine affinity-tagged NS5B fusion protein expressed with recombinant baculoviruses in insect cells
-
ammonium sulfate precipitation, Q-Sepharose column chromatography, and Superdex 200 gel filtration
-
C-terminally truncated enzyme form NS5B(DELTA21) expressed in Escherichia coli
-
chelating Sepharose flast flow resin chromatography and Superdex 200 gel filtration
-
enzymatically active full-length recombinant JEV NS5 protein with a hexahistidine tag at the N-terminus
-
full-length enzyme and C-terminal hydrophobic domain deletion mutant expressed in Escherichia coli or in Sf9 cells
-
full-length enzyme and truncated enzyme forms resulting from deletions of 24, 36, 65 or 82 amino acid residues at the C terminal, with C-terminal hexahistidine tag
-
HisTrap HP column chromatography, 15S column chromatography, ultrafiltration, and Superdex 200 gel filtration
Q6DLV0
HisTrap HP column chromatography, Source 15S column chromatography, and gel filtration
-
NS5B-hexahistidine fusion protein expressed with recombinant baculoviruses in insect Sf9 cells
-
partial
purified from Escherichia coli to near homogeneity. When the 21 amino acids from the C-terminus of the protein are deleted, an inclusion body is not formed and a better purification yield is achieved
-
putative RNA-dependent RNA polymerase (RdRp) domain cloned and expressed in Escherichia coli
-
recombinant C-terminally His-tagged RdRp as the C-terminal domain of nonstructural protein 9 from Escherichia coli strain BL21 (DE3) by cobalt affinity chromatography and gel filtration
-
recombinant C-terminally HIs6-tagged enzyme from Escherichia coli by nickel affinity chromatography
recombinant enzyme from Escherichia coli by affinity chromatography and gel filtration
recombinant enzyme P2 from Escherichia coli strain BL21 (DE3) by anion exchange chromatography, gel filtration, dialysis, and ultrafiltration
recombinant enzyme, wild-type and mutant enzymes, expressed in Escherichia coli
-
recombinant FLAG-tagged D-elp1 from Spodoptera frugiperda Sf9 cells by affinity chromatography. His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography
-
recombinant His-tagged enzyme variants from Escherichia coli by nickel affinity chromatography
recombinant His-tagged RdRp_2 from Escherichia coli strain M15 by nickel affiniity chromatography
-
recombinant His-tagged subunits PA and PB1 from Escherichia coli by nickel affinity chromatography
recombinant His6-tagged NS5B from Hep-G2 cells by nickel affinity chromatography
recombinant N-terminally GST-tagged enzyme from Escherichia coli strain C41(DE3) by glutathione affinity chromatography and gel filtration
recombinant viral His18-tagged enzyme components from Sf21AE and TN5 insect cells
-
recombinant wild-type and mutant His-tagged enzymes from Escherichia coli strain BL21(DE3) or recombinant soluble His6-tagged wild-type enzyme from High Five insect cells by nickel affinity chromatgraphy to homogeneity
-
Sepharose SPHP XK16/20 column chromatography, Q20 column chromatography, Q5 column chromatography, and UNO column chromatography
-
soluble Hepatitis C virus NS5B in the glutathione S-transferase-fused form NS5Bt, expressed in Escherichia coli
-
three different recombinant forms of DENV-2 RdRp as either N- or C-terminally His-tagged fusions, or without tag from Escherichia coli strain s Rosetta (DE3) and BL21 (DE3) to homogeneity by nickel affinity and anion exchange chromatography, followed by gel filtration and ultracentrifugation
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
a codon-optimized cDNA sequence of ZIKV NS5 (amino acids 2522 to 3423; strain H/PF/2013) is synthesized de novo. The ZIKV NS5 polymerase portion is PCR amplified and cloned into a pMal-c5X vector under tac promoter control. Expression in Escherichia coli
a hexahistidine affinity-tagged NS5B fusion protein is expressed with recombinant baculoviruses in insect cells
-
bacterial production of the recombinant DENV-2 RdRp was difficult due to its low expression and solubility levels, recombinant expression of three different forms of DENV-2 RdRp as either N- or C-terminally His-tagged fusions, or without tag in Escherichia coli strains Rosetta (DE3) and BL21 (DE3). The presence of both the N- and C-terminal His-tag has a deleterious effect on polymerase activity, overview
co-expression of SARS-CoV-2 RNA-dependent RNA polymerase subunits with chaperones gives soluble expression in Escherichia coli
DNA and amino acid sequence determination and analysis, phylogenetic analysis based on the sequence of the RdRp whole domains, overview
DNA and amino acid sequence determination and analysis, sequence comparisons, NS5B genotyping, enzyme activities, and activity with ribavirin, overview. Expression of His-tagged enzyme variants in Escherichia coli
DNA sequence determination and analysis of hundreds of intronic regions encoding three or more RNA-dependent RNA polymerase-dependent sRNAs that are covered by dsRNA-seq (double-stranded RNA sequencing) reads, indicating that the intron-derived sRNAs are indeed generate from long double-stranded RNA precursors
-
enzymatically active full-length recombinant JEV NS5 protein with a hexahistidine tag at the N-terminus is expressed in Escherichia coli
-
enzyme RNA and amino acid sequence deermination and analysis, recombinant expression of wild-type and mutant His-tagged enzymes in Escherichia coli strain BL21(DE3), recombinant expression of soluble His6-tagged wild-type in High Five cells via the baculovirus expression system
-
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
expression in Escherichia coli using the N-terminal domain of Escherichia coli lysyl-tRNA synthetase as a solubility enhancer
-
expression in Escherichia coli, a mutant is generated as a result of the deletion of a trinucleotide in the N-terminal portion of the coding region, pT7-POL(TRP-). The protein expressed from this mutant lacks a tryptophan residue normally present at the fifth amino acid from the N-terminal glycine. This protein has no detectable enzymatic activity. Mutant pT7-POL(AvII), which lacks the C-terminal 53 amino acids of the normal protein is also inactive
-
expression of ego-1 in the P19 EC cell line derived of murine embryonal carcinoma stem cells, co-expression with si RNA leads to gene silencing that is enhanced by ego-1, overview
-
expression of FLAG-tagged D-elp1 in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system, and of His-tagged wild-type and mutant enzymes in Escherichia coli. Quantitative RT-PCR analysis for the expression levels of Dcr-2 and D-elp1 RNAs in S2 cells after depletion
-
expression of recombinant enzyme chimeras by in vitro transcription
expression of SARS-CoV-2 nsp12 in Sf9 cells. Expression of SARS-CoV-2 nsp7 and nsp8 in Escherichia coli
expression of wild-type and muztant enzymes in Escherichia coli strain BL21(DE3)
Cystovirus phi6
-
for recombinant expression in Spodoptera frugiperda Sf9 cells via baculovius transfection method, RSV RdRp is split into three pieces, since expression of the full protein cannot be achieved, expression as N-terminally His-tagged proteins or as GFP-fusion proteins
-
full-length enzyme and truncated enzyme forms resulting from deletions of 24, 36, 65 or 82 amino acid residues at the C terminal, with C-terminal hexahistidine tag, expression in Escherichia coli
-
fusion protein bearing a His6 tag at its C-terminus or at its N terminus is overexpressed in Escherichia coli
-
gene RdRP, phylogenetic analysis, quantitative real-time PCR enzyme expression analysis, Agrobacterium-mediated virus infection of Solanum lycopersicum plants into cotyledons
gene rrpC, DNA and amino acid sequence determination and analysis, quantitative real-time PCR expression analysis
gene StRDR1, phylogenetic analysis, enzyme expression analysis by quantitative reverse transcriptase PCR
identification and genomic analysis of 11956 non-transposon-related rice pseudogenes, most of which are from gene duplications, 145 of these pseudogenes potentially give rise to antisense small RNAs. 50% of these antisense RNAs are 24-nucleotides long, a feature often seen in plant repeat-associated small interfering RNAs produced by RNA-dependent RNA polymerase and Dicer-like protein 3
-
in vitro transcription of NS5B using SP6 RNA polymerase, and recombinant expression of His6-tagged NS5B and of untagged RDRP in Hep-G2 cells. In vitro cleavage of HCV core and NS5B mRNAs by DNAzyme in Hep-G2 cells is assessed by RT-PCR using RNA from cells co-transfected with cloned core or NS5B gene and its respective DNAzyme leading to reduction of NS5B protein activity in NDNAzyme co-transfected cells
N-terminal hexa-His-NS5BD21 (Con1 strain, GT1b with the C-terminal 21-amino acid membrane anchor domain deleted), expression in Escherichia coli
-
NgRDR1, DNA and amino acid sequence determination and analysis, semi-quantitative RT-PCR analysis, genetic structure, sequence comparisons, and phylogenetic tree
NS5B-hexahistidine fusion protein expressed with recombinant baculoviruses in insect Sf9 cells
-
p92, in vitro translation using an extract of Nicotiana tabacum BY-2 cells, together with in vitro translated p33 formng th viral RNA replicase, overview
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PmV1 genome organization analysis, nucleotide and amino acid sequence determination and analysis of sequence dsR2, phylogenetic analysis, recombinant expression in Escherichia coli strain TG1
putative RNA-dependent RNA polymerase (RdRp) domain cloned and expressed in Escherichia coli
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RdRp gene encoded in the large RNA segment that contains a single ORF, nucleotide and amino acid sequence determination, phylogenetic analysis
RdRp gene, nucleotide and amino acid sequence determination and analysis, genome organization, detailed phylogenetic analysis and reclassification of SARS-CoVs, overview
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RdRp gene, nucleotide and amino acid sequence determination and analysis, TSV genome organization, the Texas isolate has significant structural differences from the Hawaii isolate due to point mutation(s) in the RdRp gene in residues L1622, N1673, K1769, S1994, overview
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RdRp, dsRNA 1 sequence determination and analysis via syntesis of the correspondant DNA sequences, phylogenetic analysis. Little single-stranded form of dsRNA 1 exists in the host Alternaria alternata, and most of the dsRNA 1 is present as genomic RNA rather than the replicative form of the ssRNA genome
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RdRp, dsRNA sequence determination and analysis, genome structure and phylogenetic analysis, sequence comparisons
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RdRp_2, genome organization analysis, and nucleotide and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression of the His-tagged protein in Escherichia coli strain M15
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recombinant enzyme P2 expression in Escherichia coli strain BL21 (DE3)
recombinant expression of C-terminally His-tagged RNA-dependent RNA polymerase (RdRp) as the C-terminal domain of nonstructural protein 9 (nsp9) in Escherichia coli strain BL21 (DE3)
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recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli
recombinant expression of FLAG-tagged full-length enzyme in HEK-293 cells
recombinant expression of the viral His18-tagged enzyme components in Sf21AE and TN5 insect cells, establishing a single-round transcription system
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recombinant NV 3Dpol, as well as a 3Dpol active-site mutant are expressed in Escherichia coli
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RNA genome organization, DNA and amino acid sequence determination, phylogenetic analysis
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RNA genome organization, nucleotide and amino acid sequence determination, FgV3 is encoded in one of two geneome segments, phylogenetic analysis indicates that FgV3that FgV3 is closely related to members of the families Totiviriridae and Chrysoviridae, but is placed outside of their main clusters
RNA genome organization, nucleotide and amino acid sequence determination, segment FgV4 dsRNA-1 contains a single ORF, which has a conserved RdRp motif, phylogenetic analysis indicates that FgV4 forms a distinct clade with the family Partitiviridae
Fusarium graminearum dsRNA mycovirus 4
SARS-CoV-2 nsp12 polymerase and nsp7-nsp8 cofactors are expressed using the baculovirus and Escherichia coli expression systems, respectively. The three protein subunits were mixed in vitro to constitute the core polymerase complex
sequencing of the single positive-strand RNA, monopartite, bicistronic genome of SINV-3 ORF 1 encoding the RNA-dependent RNA polymerase, and a helicase and protease, phylogenetic analysis
single positive-strand RNA sequence determination and analysis, sequence comparisons
single, positive-strand RNA sequence determination and analysis, ORF2b encodes the RNA dependent RNA polymerase, phylogenetic analysis
soluble Hepatitis C virus NS5B in the glutathione S-transferase-fused form NS5Bt which lacks the C-terminal 21 amino acid residues, expressed in Escherichia coli
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the gene segment corresponding to the RdRp module corresponds to amino acid 272905 of the NS5 protein, recombinant expression of the enzyme as N-terminally GST-tagged protein in Escherichia coli strain C41(DE3)
the pol domain of gene 1 is cloned and expressed in cells as a fusion with green fluorescent protein, termed Gpol
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the SARS-CoV-2 nsp12 gene is codon-optimized for expression in insect cells. The SARS-CoV-2 nsp8 and nsp7 genes are codon-optimized for expression in Escherichia coli
wild-type and mutant enzymes, DNA and amino acid sequence determination and analysis
expression of recombinant enzyme chimeras by in vitro transcription
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ectopic application of salicylic acid induces the expression of cucumber RDR1b gene
ectopic application of salicylic acid induces the expression of cucumber RDRc1/c2 genes
ectopic application of salicylic acid induces the expression of RDR1a
large-scale mutagenesis of the RdRp domain of Lassa virus L protein, overview. Mutation of two adjacent residues in the putative palm-thumb subdomain junction, G1394 and D1395, by PCR-based mutagenesis in strain AV, lead to a defect in mRNA synthesis but do not affect antigenomic RNA synthesis. Clear dominant-negative effects are only seen with mutants affecting residues in motifs pre-A with K1127, R1134, E1135, L1136, D1140, and K1144, A with D1193, B with G1298, C with S1333, D1334, and D1335, and D with K1376, overview
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RDR1 expression is elevated following plant treatment with defensive phytohormones, StRDR1 is salicylic acid-responsive
the expression of all CsRDR1 genes is induced by virus infection
the expression of all CsRDR1 genes is induced by virus infection, after which the expression level of CsRDR1b increases 10-20fold in several virus-resistant cucumber cultivars
the expression of all CsRDR1 genes is induced by virus infection. CsRDR1c1/c2 genes are highly induced (25-1300fold) in susceptible cucumber cultivars infected with RNA or DNA viruses
the isoform RDR1 promoter has a broad-spectrum response to various stresses and is sensitive to 1-naphthaleneacetic acid, abscisic acid, and salicylic acid
tobacco mosaic virus inoculation onto Solanum lycopersicum leaves induces an increase in SlRDR1 gene expression in the upper uninoculated leaves. Expression of alternative oxidase SlAOX1a is more rapidly induced. Application of an exogenous AOX activator on empty vector-silenced control plants greatly induces the accumulation of SlRDR1 and SlAOX1a transcript and reduces tobacco mosaic virus viral RNA accumulation, but failed to have such effects on SlRDR1-silenced plants
transcripts of NgRDR1 can be induced by biotic stresses, such as exogenous signaling molecules including salicylic acid and analogues, hydrogen peroxide, and methyl jasmonate. NgRDR1 expression can be up-regulated by potato virus Y, tobacco mosaic virus, and cucumber mosaic virus, but not by potato virus X. Besides, different kinds of fungi can also induce NgRDR1 expression, expression profiles of NgRDR1 under abiotic stresses, overview
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
when the enzyme is denatured in 8 M urea, a maximum of about 40% of the poly(G) polymerase activity can be regained
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when the enzyme is denatured with 8 M urea, the rate of its renaturation following dilution in a high-salt buffer is inhibited by relatively low concentrations of GDP, ppGpp and GTP
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
AJ242654
assembly of a productive isoform NS5B primer-template elongation complex stalled after formation of a 9-nucleotide primer. Under optimized conditions up to 65% of NS5B can be converted into active elongation complexes. The elongation complex is extremely stable, allowing purification away from excess nucleotide and abortive initiation products
drug development
medicine
molecular biology
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the enzyme, that is absent in mammalian cells, enhances the effect of siRNA expression on target gene expression in mammalian cells, when coexpressed, for amplifying the use of hairpin siRNA expression vectors for gene silencing, method development, overview
pharmacology
synthesis
drug development
the enzyme is a target for drugs in therapy of HCV infection
drug development
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the functional nature of multimeric arrays of RNA-dependent RNA polymerase supplies a target for antiviral compounds
drug development
the virus causes significant economic losses in rabbit farming and reduces wild rabbit populations, and its RNA-dependent RNA polymerase (RdRp) is a primary target for the development of antiviral drugs
drug development
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the virus causes significant economic losses in rabbit farming and reduces wild rabbit populations, and its RNA-dependent RNA polymerase (RdRp) is a primary target for the development of antiviral drugs
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medicine
the enzyme is a key target for developing specific antiviral therapy
medicine
-
NS5B RdRp is a prime target for therapeutic intervention of hepatitis C virus infection
medicine
-
NS5B is strictly required for viral replication and thus represents an attractive therapeutic target
medicine
-
NS5B RNA-dependent RNA polymerase is essential for replication of hepatitis C virus and is a prime target for therapeutic intervention
pharmacology
-
targeting the active sites of polymerase molecules is not likely to be the best antiviral strategy, as inactivated polymerases do not inhibit replication of other viruses in the same cell and can, in fact, be useful in RNA replication complexes, because catalytically inactive polymerases participate productively in functional oligomer formation and catalysis
pharmacology
the viral RNA polymerase is an attractive target for inhibition in the treatment of viral infections
synthesis
Cystovirus phi6
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RdRp from the bacteriophage phi6 can be used to generate dsRNA for RNA interference, RNAi, applications, resulting in in vivo gene silencing. RNA molecules that are radioactively or fluorescently labeled using poly(A) polymerase can be used as probes in a wide variety of applications
synthesis
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the functional nature of multimeric arrays of RNA-dependent RNA polymerase provides an appreciation for enzymatic catalysis on membranous surfaces within cells
synthesis
Cystovirus phi6
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the RNA-dependent RNA polymerase of the bacteriophage phi6 is used for synthesis of long double-stranded RNA from a cloned region of the genome of Coxsackie virus B3, i.e. CBV3, a member of the human enterovirus B species, for usage in RNA interference in antiviral experimental therapies and gene function studies, overview. Synthesis of GFP CBV3 siRNA
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EXTERNAL LINKS (specific for EC-Number 2.7.7.48)
Transporter Classification Database (TCDB): 1.G.3.1.7, 1.A.53.1.5, 1.A.85.1.6, 1.A.122.1.2, 1.A.53.1.7, 1.A.85.1.7, 1.G.3.1.2, 1.G.3.1.1, 1.A.85.1.4, 1.A.85.1.8, 1.A.53.1.11, 1.A.53.1.6, 1.A.85.1.1
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Release 2023.1 (January 2023)
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