Information on EC 2.7.7.48 - RNA-directed RNA polymerase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
2.7.7.48
-
RECOMMENDED NAME
GeneOntology No.
RNA-directed RNA polymerase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
nucleoside triphosphate + RNAn = diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Metabolic pathways
-
Purine metabolism
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
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
-
-
-
-
3D polymerase
-
-
3Dpol
Human coxsackievirus B3 Nancy
-
-
-
3Dpol-like protein
-
the RNA-dependent RNA polymerase is associated with the 3Dpol-like protein
69.6 kDa protein
-
-
-
-
core protein
-
-
-
-
core protein VP1
-
-
-
-
DENV 3 polymerase
-
-
DENV 3 RdRp
Q6DLV0
-
DENV RdRp
-
-
ego-11
G5EBQ3
gene name
HC-J4 NS5BDELTA21
-
a C-terminally truncated polymerase based on the consensus sequence of pCV-J4L6S
HCN NS5B protein
-
-
HCV NS5B
-
-
HCV RdRp
-
-
hepatitis C virus polymerase
-
-
HRV16 3Dpol
Human rhinovirus 16
-
-
influenza polymerase PA
P31343
-
influenza polymerase PA
influenza A virus Victoria/3/1975 H3N2
P31343
-
-
inner layer protein VP1
-
-
-
-
JEV NS5
-
nonstructural protein that carries both methyltransferase and RNA-dependent RNA polymerase (RdRp) domains
JEV NS5 protein
-
-
JEV NS5 protein
Japanese encephalitis virus JaOH0566
-
-
-
L protein
-
-
-
-
large structural protein
-
-
-
-
M1 phosphoprotein
-
-
-
-
NgRDR1
C1I213
-
NIB
-
-
-
-
nonstructural phosphoprotein
-
-
-
-
nonstructural protein
-
-
-
-
nonstructural protein 12
P0C6X7
-
nonstructural protein 5B
-
-
-
-
nonstructural protein 5B
-
-
NS5
Japanese encephalitis virus JEV
-
-
-
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 protein
Q6DLV0
-
NS5 protein
Japanese encephalitis virus JaOH0566
-
-
-
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
NS5 RdRp
Q8JU43
-
NS5 RdRp
West Nile virus 3356
Q8JU43
-
-
NS5B
-
-
-
-
NS5B
AJ242654
-
NS5B
Q0G9P7
-
NS5B enzyme
-
-
NS5B polymerase
-
-
NS5B polymerase
B6EAV7
-
NS5B protein
-
-
-
-
NS5B RdRp
Hepatitis C virus NS5B
-
-
-
NS5B RNA-dependent RNA polymerase
-
-
NS5b-directed RNA polymerase
-
-
nsp12
P0C6X7
-
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
-
-
-
-
phi6 polymerase
-
-
Pol
-
-
-
-
Pol IV
-
-
polymerase 3Dpol
-
-
polymerase acidic protein
-
-
-
-
polymerase basic 1 protein
-
-
-
-
polymerase L
-
-
-
-
protein 3Dpol
-
-
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
-
-
Qbeta-replicase
-
-
-
-
RDR2
-
-
RDR2
-
-
RDR6
Q9SG02
gene name
RDRP
-
-
-
-
RDRP
Alternaria alternata dsRNA mycovirus
-
-
RDRP
-
-
RDRP
Caenorhabditis elegans Bristol N2
-
-
-
RDRP
Chaetoceros socialis f. radians RNA virus
B9A8E0
-
RDRP
-
-
RDRP
Dengue virus DENV
-
-
-
RDRP
B3SND7
-
RDRP
Q0G9P7
-
RDRP
Hepatitis C virus NS5B
-
-
-
RDRP
Human coxsackievirus B3 Nancy
-
-
-
RDRP
Japanese encephalitis virus JaOH0566, Japanese encephalitis virus JEV
-
-
-
RDRP
-
-
RDRP
Measles virus Alaska
-
;
-
RDRP
P0C6X7
-
RDRP
St. Louis encephalitis virus SLEV
-
-
-
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 dependent RNA polymerase
Q0G9P7
-
RNA dependent RNA polymerase
Hepatitis C virus NS5B
-
-
-
RNA dependent RNA polymerase
B5DC58
-
RNA nucleotidyltransferase (RNA-directed)
-
-
-
-
RNA polymerase
-
-
RNA polymerase
-
-
RNA polymerase
-
-
RNA polymerase
P03433
-
RNA polymerase
-
-
RNA polymerase IV
-
-
RNA replicase
-
-
-
-
RNA synthetase
-
-
-
-
RNA transcriptase
-
-
-
-
RNA-binding protein
-
-
-
-
RNA-dependent ribonucleate nucleotidyltransferase
-
-
-
-
RNA-dependent RNA polymerase
-
-
-
-
RNA-dependent RNA polymerase
Alternaria alternata dsRNA mycovirus
-
-
RNA-dependent RNA polymerase
-
-
RNA-dependent RNA polymerase
-
-
RNA-dependent RNA polymerase
-
-
RNA-dependent RNA polymerase
-
-
RNA-dependent RNA polymerase
Chaetoceros socialis f. radians RNA virus
B9A8E0
-
RNA-dependent RNA polymerase
-
-
RNA-dependent RNA polymerase
Q6DLV0
-
RNA-dependent RNA polymerase
-
-
RNA-dependent RNA polymerase
-
-
RNA-dependent RNA polymerase
-
-
RNA-dependent RNA polymerase
D0TZ30
-
RNA-dependent RNA polymerase
D0TZ31
-
RNA-dependent RNA polymerase
B3SND7
-
RNA-dependent RNA polymerase
-
-
RNA-dependent RNA polymerase
-
-
RNA-dependent RNA polymerase
-
-
RNA-dependent RNA polymerase
Human coxsackievirus B3 Nancy
-
-
-
RNA-dependent RNA polymerase
human parainfluenza virus
-
-
RNA-dependent RNA polymerase
Human rhinovirus 16
-
-
RNA-dependent RNA polymerase
-
-
RNA-dependent RNA polymerase
C0KQW8
-
RNA-dependent RNA polymerase
-
-
RNA-dependent RNA polymerase
Japanese encephalitis virus JaOH0566
-
-
-
RNA-dependent RNA polymerase
-
-
RNA-dependent RNA polymerase
-
-
RNA-dependent RNA polymerase
Measles virus Alaska
-
;
-
RNA-dependent RNA polymerase
-
-
RNA-dependent RNA polymerase
-
-
RNA-dependent RNA polymerase
C1I213
-
RNA-dependent RNA polymerase
-
-
RNA-dependent RNA polymerase
-
-
RNA-dependent RNA polymerase
-
-
RNA-dependent RNA polymerase
A8W7G1
-
RNA-dependent RNA polymerase
-
-
RNA-dependent RNA polymerase
-
-
RNA-dependent RNA polymerase
-
-
RNA-dependent RNA polymerase
-
-
RNA-dependent RNA polymerase
C1JCT1
-
RNA-dependent RNA polymerase
D2JRZ3
-
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
-
-
RNA-dependent RNA polymerase
-
-
RNA-Dependent RNA Polymerase 2
-
-
RNA-dependent RNA polymerase NS5B
-
-
RNA-dependent RNA polymerases
-
-
RNA-dependent RNA replicase
-
-
-
-
RNA-dependent RNA-polymerase
-
-
RNA-dependent RNA-polymerase
-
-
RNA-dependent RNA-polymerase
-
-
RNA-dependent RNA-polymerase
-
-
RNA-directed RNA polymerase
-
-
-
-
RNAdependent RNA polymerase
Q9LKP0
-
rrf-1
G5ECM1
gene name
RRF-3
Caenorhabditis elegans Bristol N2
-
-
-
sigma NS protein
-
-
-
-
transcriptase
-
-
-
-
VP1
-
-
-
-
VP1 protein
-
-
-
-
WNV NS5
-
-
MOP1
-
-
additional information
-
the RDR enzymes belong to the RDR family
additional information
-
the enzyme belongs to the supergroup I of RNA-dependent RNA polymerases
CAS REGISTRY NUMBER
COMMENTARY
9026-28-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Alternaria alternata dsRNA mycovirus
i.e. AaV-1, isolated from the mycelia of EGS 35-193 strain of Alternaria alternata
-
-
Manually annotated by BRENDA team
-
Q8H1K9, Q9LKP0
GenBank
Manually annotated by BRENDA team
ecotype Col-0, gene dr2
-
-
Manually annotated by BRENDA team
gene rdr6
Q9LKP0
GenBank
Manually annotated by BRENDA team
isoform RDR1
UniProt
Manually annotated by BRENDA team
isoform RDR6
UniProt
Manually annotated by BRENDA team
Drosophila melanogaster infected with
-
-
Manually annotated by BRENDA team
i.e. BlVS, from Rubus canadensis berris, the virus might belong to the family Tymoviridae
-
-
Manually annotated by BRENDA team
i.e. BVDV, from infected MDBK cells
P19711
Uniprot
Manually annotated by BRENDA team
strains Marloie, NADL, and 3435
P19711
Uniprot
Manually annotated by BRENDA team
Hordeum vulgare leaf infected with
-
-
Manually annotated by BRENDA team
isoform ego-1
UniProt
Manually annotated by BRENDA team
isoform rrf-1
UniProt
Manually annotated by BRENDA team
strain Bristol N2, gene rrf-3
-
-
Manually annotated by BRENDA team
Caenorhabditis elegans Bristol N2
strain Bristol N2, gene rrf-3
-
-
Manually annotated by BRENDA team
Chaetoceros socialis f. radians RNA virus
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
Manually annotated by BRENDA team
i.e. ORMV, a tobamovirus taxonomically distinct from the type member of the genus, cultivated on Nicotiana benthamiana and Nicotiana tabacum plants
-
-
Manually annotated by BRENDA team
expression in Escherichia coli
-
-
Manually annotated by BRENDA team
cowpea leaf infected with
-
-
Manually annotated by BRENDA team
cucumber cotyledons infected with
-
-
Manually annotated by BRENDA team
Cucumis sativus seedlings infected with
-
-
Manually annotated by BRENDA team
Nicotiana tabacum infected with
-
-
Manually annotated by BRENDA team
DENV
-
-
Manually annotated by BRENDA team
viral polyprotein
UniProt
Manually annotated by BRENDA team
Dengue virus DENV
DENV
-
-
Manually annotated by BRENDA team
BHK-21 cells infected with
-
-
Manually annotated by BRENDA team
Escherichia coli infected with
-
-
Manually annotated by BRENDA team
Escherichia coli infected with
-
-
Manually annotated by BRENDA team
Escherichia coli infected with; Qbetaam12; QbetaamB86
-
-
Manually annotated by BRENDA team
Escherichia coli infected with; QbetaamB86
-
-
Manually annotated by BRENDA team
Enterobacteria phage Qbeta Qbetaam12
Qbetaam12
-
-
Manually annotated by BRENDA team
Enterobacteria phage Qbeta QbetaamB86
QbetaamB86
-
-
Manually annotated by BRENDA team
i.e. FHV
-
-
Manually annotated by BRENDA team
BHK cells infected with
-
-
Manually annotated by BRENDA team
Foxtail mosaic potexvirus
Chenopodium guinoa infected with
-
-
Manually annotated by BRENDA team
i.e. FgV3, a dsRNA mycovirus from Fusarium graminearum strain DK3
UniProt
Manually annotated by BRENDA team
i.e. FgV4, a dsRNA mycovirus from Fusarium graminearum strain DK4
UniProt
Manually annotated by BRENDA team
cultivar lumian 22
UniProt
Manually annotated by BRENDA team
i.e. GLRaV-Pr, an isolate from Greek grapevines, Vitis vinifera cv. Mantilaria, belongs to the Ampelovirus group
-
-
Manually annotated by BRENDA team
-
AJ242654
GenBank
Manually annotated by BRENDA team
expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
expression in Escherichia coli
-
-
Manually annotated by BRENDA team
genotype 1b
-
-
Manually annotated by BRENDA team
genotype 1b isolate J4 with 21 amino acid C-terminal truncation and genotype 1b isolate RB01
-
-
Manually annotated by BRENDA team
genotype-1b. HC-J4 NS5BDELTA21, a C-terminally truncated polymerase based on the consensus sequence of pCV-J4L6S
-
-
Manually annotated by BRENDA team
genotypes 1a and 1b
-
-
Manually annotated by BRENDA team
GT-1a and GT-1b clinical isolates
UniProt
Manually annotated by BRENDA team
HepG2, Hep3B, and Bel-7402 cells transfected with
-
-
Manually annotated by BRENDA team
i.e. HCV
Q0G9P7
UniProt
Manually annotated by BRENDA team
i.e. HCV
Uniprot
Manually annotated by BRENDA team
i.e. HCV
-
-
Manually annotated by BRENDA team
i.e. HCV, genotype 1b, strain BKDELTA21
Uniprot
Manually annotated by BRENDA team
Hepatitis C virus NS5B
NS5B
-
-
Manually annotated by BRENDA team
strain Nancy
-
-
Manually annotated by BRENDA team
Human coxsackievirus B3 Nancy
strain Nancy
-
-
Manually annotated by BRENDA team
expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
expressed in Escherichia coli BL-21
-
-
Manually annotated by BRENDA team
HeLa cells infected with
-
-
Manually annotated by BRENDA team
strains 3D and 3AB
-
-
Manually annotated by BRENDA team
i.e. HSV-1
-
-
Manually annotated by BRENDA team
human parainfluenza virus
-
-
-
Manually annotated by BRENDA team
Human rhinovirus 16
-
-
-
Manually annotated by BRENDA team
Human rhinovirus 16
-
Uniprot
Manually annotated by BRENDA team
Human rhinovirus 2
-
-
-
Manually annotated by BRENDA team
belongs to the Orthomyxoviridae family
-
-
Manually annotated by BRENDA team
from insect cells
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
subunit P2; Victoria/3/1975, H3N2
UniProt
Manually annotated by BRENDA team
influenza A virus Victoria/3/1975 H3N2
subunit P2; Victoria/3/1975, H3N2
UniProt
Manually annotated by BRENDA team
Influenza virus A/PR8
-
-
-
Manually annotated by BRENDA team
i.e. IYSV, belongs to the genus Tospovirus, family Bunyaviridae, transmitted by onion thrips, Thrips tabaci
UniProt
Manually annotated by BRENDA team
; strain JaOH0566
-
-
Manually annotated by BRENDA team
Japanese encephalitis virus JaOH0566
strain JaOH0566
-
-
Manually annotated by BRENDA team
Japanese encephalitis virus JEV
JEV
-
-
Manually annotated by BRENDA team
strain MRM61C, Vero cells infected with
-
-
Manually annotated by BRENDA team
Kunjin virus MRM61C
strain MRM61C, Vero cells infected with
-
-
Manually annotated by BRENDA team
La France isometric virus
Agaricus bisporus infected with
-
-
Manually annotated by BRENDA team
Zea mays infected with
-
-
Manually annotated by BRENDA team
strain Alaska
-
-
Manually annotated by BRENDA team
Vero cells infected with
-
-
Manually annotated by BRENDA team
Measles virus Alaska
strain Alaska
-
-
Manually annotated by BRENDA team
delayed brain tumor cell monolayers infected with MHV A59
-
-
Manually annotated by BRENDA team
mouse cells infected with
-
-
Manually annotated by BRENDA team
i.e. MNV-1
-
-
Manually annotated by BRENDA team
group I RDR
UniProt
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
149 pseudogenes
-
-
Manually annotated by BRENDA team
isoform RDR 6
-
-
Manually annotated by BRENDA team
Phomopsis sp.
-
GenBank
Manually annotated by BRENDA team
i.e. PiRV-1, isolates MX980400 and MX980317
-
-
Manually annotated by BRENDA team
dsR1; i.e. PmV1, belongs to the genus Partitivirus, a plant-associated virus
UniProt
Manually annotated by BRENDA team
a complex double-stranded RNA virus of the family Cystoviridae
-
-
Manually annotated by BRENDA team
a dsRNA bacteriophage of the family Cystoviridae
-
-
Manually annotated by BRENDA team
expression in Escherichia coli
-
-
Manually annotated by BRENDA team
Respiratory Enteric Orphan Virus type-1, Reo-1
-
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
i.e. SARS-CoV
-
-
Manually annotated by BRENDA team
replicase polyprotein 1ab
UniProt
Manually annotated by BRENDA team
SA11 Rotavirus
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
i.e. SINV-3, Argentinean isolate from the Santa Fe region of Argentina
UniProt
Manually annotated by BRENDA team
i.e. SINV-3, from a colony in the United States, DM isolate
UniProt
Manually annotated by BRENDA team
St. Louis encephalitis virus SLEV
SLEV
-
-
Manually annotated by BRENDA team
i.e. TSV, isolated from tail muscle tissue of infected shrimp from shrimp farms in Texas in 2004, a member of the family Dicistroviridae
-
-
Manually annotated by BRENDA team
i.e. TMV, is a type member of the tobamovirus family, clone TMV-KK1, cultivated on Nicotiana benthamiana and Nicotiana tabacum plants
-
-
Manually annotated by BRENDA team
i.e. TBSV, a tombusvirus
-
-
Manually annotated by BRENDA team
Nicotiana tabacum plant infected with
-
-
Manually annotated by BRENDA team
infected with Cowpea mosaic virus. The host-encoded enzyme is strongly stimulated upon CPMV infection of cowpea leaves
-
-
Manually annotated by BRENDA team
BHK cells infected with
-
-
Manually annotated by BRENDA team
expressed in Escherichia coli
-
-
Manually annotated by BRENDA team
viral polyprotein
UniProt
Manually annotated by BRENDA team
West Nile virus 3356
viral polyprotein
UniProt
Manually annotated by BRENDA team
West Nile virus WNV
WNV
Uniprot
Manually annotated by BRENDA team
i.e. YFV
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
RRF-3 mutation is involved in compromised spermatogenesis, that accounts for reduced brood size and X-chromosome loss from rrf-3 mutant hermaphrodites
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
-
impairing the nuclear import of PB2 by mutating its nuclear localization signal leads to abnormal formation of the trimeric polymerase in the cytoplasm
malfunction
-
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
Caenorhabditis elegans Bristol N2
-
RRF-3 mutation is involved in compromised spermatogenesis, that accounts for reduced brood size and X-chromosome loss from rrf-3 mutant hermaphrodites
-
metabolism
-
key enzyme involved in vrial replication
metabolism
-
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
physiological function
-
RdRps are unique in that they create dsRNA by initiating polymerization at the 3' end of the substrate
physiological function
-
RRF-3 is required for spermatocyte cell division, overview
physiological function
-
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
P31343
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
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
C1I213, -
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
-
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
-
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
-
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
-
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
G5EBQ3, G5ECM1
expression in Drosophila melanogaster enhances transitive dsRNA-dependent silencing; 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
-
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
-
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; 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
-
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
Caenorhabditis elegans Bristol N2
-
RRF-3 is required for spermatocyte cell division, overview
-
physiological function
influenza A virus Victoria/3/1975 H3N2
-
the enzyme is responsible for replication and transcription of the eight separate segments of the viral RNA genome in the nuclei of infected cells
-
metabolism
Hepatitis C virus NS5B
-
key enzyme involved in vrial replication
-
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(dT)12 + UTP
diphosphate + ?
show the reaction diagram
-
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
-
-
?
5-fluorouridine triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
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
-
?
CTP + RNA9
diphosphate + RNA10
show the reaction diagram
AJ242654
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-, Q9Y7G6
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-, O82504, Q8H1K9, Q9LKP0
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-, Q8LHH9
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-, Q6DLV0
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
P26663
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
P26663
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Influenza virus A/PR8
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Foxtail mosaic potexvirus
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Human rhinovirus 2
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
P19711
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
La France isometric virus
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Q95ZG6, Q95ZG7
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Q95WU3
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Q8TGV4
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Q9Q9R1
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Phomopsis sp.
Q8X1C2
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
O14227
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Q9ZRY7
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Q9ZR58
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
B3SND7, -
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Q0G9P7
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
P31343
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
incorporation is more dependent on exogenopus UTP and GTP than ATP or CTP
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Human rhinovirus 16
-
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
show the reaction diagram
-
full-length negative strand BBV RNAs are synthesized
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
the polymerase product anneals only to measles RNA and not to Vero cell RNA
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
dependent on and specific for BMV RNA
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
in addition to RNA-dependent RNA polymerase activity the enzyme also possesses cap-snatching capacity
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
GTP + CMV RNA, yeast RNA or poly(C)
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Human rhinovirus 16
-
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
show the reaction diagram
-
GTP and polyC
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
GTP and polyC
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
inducible enzyme
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme should be involved in the replication of BaMV
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
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
show the reaction diagram
Human rhinovirus 16
-
required for replication of the HRV RNA genome
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme catalyzes cap methylation of virus-specific mRNA as well as RNA synthesis
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
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
show the reaction diagram
-
kinetic mechanism for single nucleotide incorporation catalyzed by poliovirus polymerase in presence of Mg2+
-
-
r
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
P11124
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
key enzyme of replication
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
NS5B RdRp is essential for viral replication
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-, Q6DLV0
homopolymer C as the template and biotinoligo(G)20 as the primer
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
kinetic model for the RNA replication reaction
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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, poly(A) RNA template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
O92972
poly(C) RNA template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
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
show the reaction diagram
-, Q6DLV0
using homopolymer C as the template
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
using poly(rA)/(dT)15 as a template-primer system
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
in vitro transcription using the model RNA template, v84
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Q0G9P7
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
substrate is HP1 RNA
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
P31343
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
show the reaction diagram
-
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
show the reaction diagram
Japanese encephalitis virus JaOH0566
-
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, 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, 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
show the reaction diagram
Human coxsackievirus B3 Nancy
-
using poly(rA)/(dT)15 as a template-primer system
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
influenza A virus Victoria/3/1975 H3N2
P31343
-, 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
show the reaction diagram
Measles virus Alaska
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Enterobacteria phage Qbeta QbetaamB86
-
GTP and polyC
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Enterobacteria phage Qbeta 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, GTP and polyC
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Enterobacteria phage Qbeta 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, GTP and polyC
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Kunjin virus MRM61C
-
incorporation is more dependent on exogenopus UTP and GTP than ATP or CTP
-
?
ribavirin triphosphate + RNAn
?
show the reaction diagram
P26663
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
-
-
?
GTP + poly(C)
diphosphate + ?
show the reaction diagram
-
use of poly(C) as template annealed with oligoG12 as primer
-
-
?
additional information
?
-
-
comparison of necrotic lesions of wild-type and chimeric mutant virusses
-
-
-
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
?
-
-
enzyme-host membrane interactions are an initial step of FHV RNA replication complex assembly, 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
?
-
P06935
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
?
-
-
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
?
-
-
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
?
-
-
the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
-
-
-
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 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 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 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
?
-
-
construction of a Coxsackie virus B3-specific GFP siRNA pool
-
-
-
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
?
-
P06935
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
?
-
-
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
?
-
-
In silico template RNA modelling, 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 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 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
?
-
P31343
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 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
?
-
P0C6X7
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
?
-
Hepatitis C virus NS5B
-
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
?
-
Japanese encephalitis virus JEV
-
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, 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
?
-
St. Louis encephalitis virus SLEV
-
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, 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
?
-
influenza A virus Victoria/3/1975 H3N2
P31343
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
?
-
Dengue virus DENV
-
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, 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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-, Q6DLV0
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
Q0G9P7
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
P31343
-
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
inducible enzyme
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme should be involved in the replication of BaMV
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
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
show the reaction diagram
Human rhinovirus 16
-
required for replication of the HRV RNA genome
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
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
show the reaction diagram
-
the enzyme catalyzes cap methylation of virus-specific mRNA as well as RNA synthesis
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
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
show the reaction diagram
-
key enzyme of replication
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
NS5B RdRp is essential for viral replication
-
-
?
nucleoside triphosphate + RNAn
diphosphate + RNAn+1
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Japanese encephalitis virus JaOH0566
-
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
show the reaction diagram
influenza A virus Victoria/3/1975 H3N2
P31343
-
-
-
?
additional information
?
-
-
comparison of necrotic lesions of wild-type and chimeric mutant virusses
-
-
-
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
?
-
-
enzyme-host membrane interactions are an initial step of FHV RNA replication complex assembly, 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
?
-
P06935
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
?
-
-
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
?
-
-
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
?
-
-
the enzyme consists of the phosphoprotein and the large protein, that are both essential for viral synthesis
-
-
-
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 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 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 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
?
-
Japanese encephalitis virus JEV, St. Louis encephalitis virus SLEV, Dengue virus DENV
-
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
divalent cation required, Ca2+ shows about 20% of the activity with Mg2+ at about 1 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
K+
-
optimal activity at 10 mM
K+
-
slight stimulation by potassium acetate, optimal activity at 60 mM
K+
Human rhinovirus 16
-
modest stimulation below 10 mM
K+
-
K+ exhibits a stimulatory effect at 25 mM, while the stimulatory effect decreases when the concentration of K+ is higher than 25 mM
Mg2+
-
optimal activity at 32 mM Mg2+
Mg2+
-
optimal concentration is 13 mM
Mg2+
-
strict dependence on Mg2+
Mg2+
-
optimal concentration is 8-20 mM; required
Mg2+
-
optimal activity at 10-12 mM
Mg2+
Foxtail mosaic potexvirus
-
the enzyme is strictly dependent on presence of Mg2+, optimal activity in presence of 5 mM MgCl2
Mg2+
-
maximal activity at 10 mM magnesium acetate
Mg2+
-
Mg2+ is the preferred divalent cation, optimal activity at 3-30 mM
Mg2+
-
maximal activity at 2.8 mM
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
Mg2+
-
maximal activity at 5 mM MgCl2
Mg2+
-
absolutely dependent on, optimal activity at 12.5 mM MgCl2
Mg2+
-
required, optimal activity with 10-20 mM magnesium acetate
Mg2+
La France isometric virus
-
maximal activity in presence of
Mg2+
Human rhinovirus 16
-
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+
-
absolute requirement for divalent cation, effective concentration range is 5-10 mM
Mg2+
-
optimal polymerase activity at 10 mM MgCl2
Mg2+
-
stimulates
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+
-
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+
-
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+
-
dependent on divalent cations, Mn2+ is 20times more effective than Mg2+ at optimal concentration (3 mM); Mg2+ is 20 times less effective than Mn2+ in coordinating the catalytic reaction of RdRp
Mg2+
-
over a concentration range from 0.5 to 5 mM, sapovirus 3Dpol displays a clear preference for Mn2+ over Mg2+
Mg2+
-
optimum concentration at 0.8 mM
Mg2+
-
activates optimally at 8 mM, recombinant viral enzyme purified from insect cells
Mg2+
-
and Mn2+, both required. Maximum activity in presence of 5.0 mM Mg2+ and 1.0-2.0 mM Mn2+
Mg2+
-
or Mn2+, required. Assay in presence of 5 mM
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+
-
can not efficiently replace Mg2+
Mn2+
-
poor substitute for Mg2+
Mn2+
-
optimal activity at 1 mM, 20% of the activity obtained with 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
Mn2+
-
1 mM MnCl2, 65% of the activity with MgCl2
Mn2+
-
can replace for Mg2+, optimal concentration is 7-9 mM MnCl2
Mn2+
-
Mg2+ requirement can be partially replaced by Mn2+
Mn2+
-
for optimal activity Mn2+ is the preferred divalent cation
Mn2+
Human rhinovirus 16
-
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+
-
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+
-
stimulates to a higher extent than Mg2+, poly(rU) polymerase activity using dT15/rA30
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+
-
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+
-
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+ is 20 times more effective than Mg2+ in coordinating the catalytic reaction of RdRp
Mn2+
-
dependent on Mn2+, optimal concentration at 2.5 mM
Mn2+
-
over a concentration range from 0.5 to 5 mM, sapovirus 3Dpol displays a clear preference for Mn2+ over Mg2+
Mn2+
-
optimum concentration at 0.1 mM, RdRp is twice as active at the Mn2+ concentration optimum compared to that of Mg2+
Mn2+
P0C6X7
strictly dependent on Mn2+
Mn2+
-
and Mg2+, both required. Maximum activity in presence of 5.0 mM Mg2+ and 1.0-2.0 mM Mn2+
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
NaCl
-
optimal activity at 80-100 mM
NaCl
-
15-40 mM, 2 to 4fold stimulation
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
Zn
Q6DLV0
structure reveals the presence of two zinc ion binding motifs
Zn2+
Human rhinovirus 2
-
0.05 mM, maximal stimulation of fourfold compared with the control
Zn2+
Q6DLV0
contains zinc, Zn2+ likely contributes to the structural stability of the region near motif E of the DENV 3 polymerase
Mn2+
-
or Mg2+, required. Assay in presence of 10 mM
additional information
-
no detectable level of RdRp activity is observed in the presence of 0.5 to 10 mM Mg2+
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(1R)-6-bromo-N-[(1S)-1-phenylethyl]-2,3,4,9-tetrahydro-1H-carbazol-1-amine
-
-
(1S)-1-(4-aminofuro[3,2-d]pyrimidin-7-yl)-1,4-anhydro-2-C-methyl-D-ribitol
-
-
(1S)-1-(4-aminothieno[3,2-d]pyrimidin-7-yl)-1,4-anhydro-2-C-methyl-D-ribitol
-
-
(2E)-3-(4-[[(1-[[(1-cyclohexyl-2-furan-3-yl-1H-benzimidazol-5-yl)carbonyl]amino]cyclobutyl)carbonyl]amino]phenyl)prop-2-enoic acid
-
-
(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)
-
-
(2R,3S,5S)-5-(methoxycarbonyl)-5-(2-methylpropyl)-2-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]pyrrolidine-3-carboxylic acid
-
-
(2R,3S,5S)-5-[(aminooxy)carbonyl]-5-(2-methylpropyl)-2-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]pyrrolidine-3-carboxylic acid
-
-
(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)-2-[(2,4-dichlorobenzoyl)(3-nitrobenzyl)amino]-3-phenylpropanoic acid
-
-
(2S,4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)pyrrolidine-2,4-dicarboxylic acid
-
-
(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
-
-
(2S,4S,5R)-2-(2-methylpropyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]pyrrolidine-2,4-dicarboxylic acid
-
-
(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
-
-
(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
-
-
(2Z)-2-(benzoylamino)-3-(5-phenyl-2-furyl)acrylic acid
-
-
(2Z)-2-(benzoylamino)-3-[4-(2-bromophenoxy)phenyl]acrylic acid
-
-
(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
-
-
(4R,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(ethoxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
(4R,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(hydroxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
(4S,5R)-1-[(3-bromo-4-tert-butylphenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
(4S,5R)-1-[(4-tert-butyl-3-chlorophenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(ethoxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(hydroxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(methoxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-methoxy-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-4-(phenylcarbamoyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
(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
-
-
(4S,5R)-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-1-[[4-(trifluoromethyl)phenyl]carbonyl]-L-proline
-
-
(4S,5R)-4-carbamoyl-2-(2-methylpropyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]-L-proline
-
-
(4S,5R)-4-[(1-methylethyl)carbamoyl]-2-(2-methylpropyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]-L-proline
-
-
(4S,5R)-4-[(methoxysulfinyl)carbamoyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-1-[[4-(trifluoromethyl)phenyl]carbonyl]-L-proline
-
-
(4S,5R)-4-[(methoxysulfinyl)carbamoyl]-2-(2-methylpropyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]-L-proline
-
-
(4S,5R)-4-[[(benzyloxy)sulfinyl]carbamoyl]-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
(5,7-difluoro-1-propyl-2,3,4,9-tetrahydro-1H-carbazol-1-yl)acetic acid
-
-
(5,8-dicyano-1-propyl-2,3,4,9-tetrahydro-1H-carbazol-1-yl)acetic acid
-
-
(5-cyano-6-fluoro-8-methyl-1-propyl-3,4-dihydro-1H-[1]benzothieno[2,3-c]pyran-1-yl)acetic acid
-
-
(5-cyano-8-fluoro-1-propyl-2,3,4,9-tetrahydro-1H-carbazol-1-yl)acetic acid
-
-
(5-cyano-8-methyl-1-propyl-1,3,4,9-tetrahydropyrano[3,4-b]indol-1-yl)acetic acid
-
-
(5-cyano-8-methyl-1-propyl-2,3,4,9-tetrahydro-1H-carbazol-1-yl)acetic acid
-
-
(5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(methoxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
(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
-
-
(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
-
-
(NH4)2SO4
-
above 60 mM
([[(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]oxy]methyl)phosphonic acid
-
-
1,3-bis-(4-chloro-1H(3H)-triazolo[4,5-g]quinoline)propan-2-one
-
moderate antiproliferative activity for the cell lines tested
1,3-dimethyl-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-1H-pyrazole-5-carboxamide
-
-
1-(1-methylethyl)-N-[4-[(2-methylpiperidin-1-yl)sulfonyl]phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
-
1-(2,5-difluorophenyl)-3-(2,5-difluorophenyl)triazene
-
-
1-(2,5-difluorophenyl)-3-(2,5-difluorophenyl)triazene
P19711
-
1-(2,5-difluorophenyl)-3-(3'-trifluoromethylphenyl)triazene
-
-
1-(2,5-difluorophenyl)-3-(3'-trifluoromethylphenyl)triazene
P19711
-
1-(2,5-difluorophenyl)-3-phenyltriazene
-
-
1-(2,5-difluorophenyl)-3-phenyltriazene
P19711
-
1-(2,5-difluorophenyl)azopyrrolidine
-
-
1-(2,5-difluorophenyl)azopyrrolidine
P19711
-
1-(2-cyclopropylethyl)-3-(1,1-dioxido-4H-1,2,4-benzothiadiazin-3-yl)-6-fluoro-4-hydroxyquinolin-2(1H)-one
-
-
1-(3,4-dichlorophenyl)azopyrrolidine
-
-
1-(3,4-dichlorophenyl)azopyrrolidine
P19711
-
1-(3-bromophenyl)azopiperidine
-
-
1-(3-bromophenyl)azopiperidine
P19711
-
1-(3-bromophenyl)azopyrrolidine
-
-
1-(3-bromophenyl)azopyrrolidine
P19711
-
1-(3-chloro)-3-phenyltriazene N-methyl
-
-
1-(3-chloro)-3-phenyltriazene N-methyl
P19711
-
1-(3-chlorophenyl)azopiperidine
-
-
1-(3-chlorophenyl)azopiperidine
P19711
-
1-(3-chlorophenyl)azopyrrolidine
-
-
1-(3-chlorophenyl)azopyrrolidine
P19711
-
1-(3-nitrophenyl)-3-(3'-nitrophenyl)triazene
-
-
1-(3-nitrophenyl)-3-(3'-nitrophenyl)triazene
P19711
-
1-(3-nitrophenyl)-3-methyl-3-phenyltriazene
-
-
1-(3-nitrophenyl)-3-methyl-3-phenyltriazene
P19711
-
1-(3-nitrophenyl)-3-phenyltriazene
-
-
1-(3-nitrophenyl)-3-phenyltriazene
P19711
-
1-(3-nitrophenyl)azopiperidine
-
-
1-(3-nitrophenyl)azopiperidine
P19711
-
1-(3-nitrophenyl)azopyrrolidine
-
-
1-(3-nitrophenyl)azopyrrolidine
P19711
-
1-(3-trifluoromethylphenyl)azopyrrolidine
-
-
1-(3-trifluoromethylphenyl)azopyrrolidine
P19711
-
1-(4-bromophenyl)azopiperidine
-
-
1-(4-bromophenyl)azopiperidine
P19711
-
1-(4-bromophenyl)azopyrrolidine
-
-
1-(4-bromophenyl)azopyrrolidine
P19711
-
1-(4-chlorophenyl)azopiperidine
-
-
1-(4-chlorophenyl)azopiperidine
P19711
-
1-(4-chlorophenyl)azopyrrolidine
-
-
1-(4-chlorophenyl)azopyrrolidine
P19711
-
1-(4-methoxyphenyl)azopyrrolidine
-
-
1-(4-methoxyphenyl)azopyrrolidine
P19711
-
1-(4-methylphenyl)-3-methyl-3-phenyltriazene
-
-
1-(4-methylphenyl)-3-methyl-3-phenyltriazene
P19711
-
1-(4-nitrophenyl)azopyrrolidine
-
-
1-(4-nitrophenyl)azopyrrolidine
P19711
-
1-(cyclobutylamino)-3-(1,1-dioxido-4H-1,2,4-benzothiadiazin-3-yl)-4-hydroxyquinolin-2(1H)-one
-
-
1-benzyl-N-[4-[(2-methylpiperidin-1-yl)sulfonyl]phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
-
1-cyclohexyl-2-(2-fluoro-4-[[2-(3-oxomorpholin-4-yl)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-2-(2-fluoro-4-[[2-(4-hydroxypiperidin-1-yl)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
-
-
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
-
-
1-cyclohexyl-2-(2-fluoro-4-[[5-(2-oxopyrrolidin-1-yl)-2-piperidin-1-ylbenzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-2-(3-furyl)-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-2-(4-[[2-morpholin-4-yl-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-indole-5-carboxylic acid
-
-
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-phenyl-1H-benzimidazole-5-carboxylic acid
-
-
1-cyclohexyl-2-phenyl-1H-indole-5-carboxylic acid
-
-
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-(2,5-difluorophenylazo)piperazine
-
-
1-methyl-4-(2,5-difluorophenylazo)piperazine
P19711
-
1-methyl-4-(phenylazo)piperazine
-
-
1-methyl-4-(phenylazo)piperazine
P19711
-
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-3-(3'-trifluoromethylphenyl)triazene
-
-
1-phenyl-3-(3'-trifluoromethylphenyl)triazene
P19711
-
1-phenyl-3-benzyltriazene
-
-
1-phenyl-3-benzyltriazene
P19711
-
1-phenyl-3-methyl-3-benzyltriazene
-
-
1-phenyl-3-methyl-3-benzyltriazene
P19711
-
1-phenyl-3-phenyltriazene
-
-
1-phenyl-3-phenyltriazene
P19711
-
1-phenyl-azopiperidine
-
-
1-phenyl-azopiperidine
P19711
-
1-phenyl-azopyrrolidine
-
-
1-phenyl-azopyrrolidine
P19711
-
1-phenyl-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
-
1-phenylazo-4-oxopiperidine
-
-
1-phenylazo-4-oxopiperidine
P19711
-
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-(2,5-difluorophenyl)-3-(3-trifluoromethylphenyl)-triazen-3-yl]-N,N-dimethyl-3-propanamine
P19711
-
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
P19711
-
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
P19711
-
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
P19711
-
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
P19711
-
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
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'-C-ethynylcytidine
-
-
2'-C-ethynylcytidine
P19711
-
2'-C-methyl-3'-O-L-valylcytidine
-
-
2'-C-methyladenosine
-
-
2'-C-methylcytidine
-
-
2'-C-methylguanosine
-
-
2'-C-methylguanosine
-
-
2'-C-methylguanosine
P19711
-
2'-deoxy-2'-fluoro-2'-methylcytidine
-
-
2'-deoxy-2'-fluorocytidine
-
-
2'-deoxycytidine triphosphate
-
inhibition is higher in presence of Mn2+ than in presence of Mg2+
2'-dGTP
-
inhibition is higher in presence of Mn2+ than in presence of Mg2+
2'-O-methylcytidine
-
-
2,3-bis(4-fluorophenyl)quinoxaline-6-carboxylic acid
-
-
2,3-bis(4-methylphenyl)quinoxaline-6-carboxylic acid
-
-
2,3-di-2-furylquinoxaline-6-carboxylic acid
-
-
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
P19711
-
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
P19711
-
2,3-dimethyl-N-{[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl}-4-{(E)-[3-(trifluoromethyl)phenyl]diazenyl}aniline
-
-
2,3-diphenylquinoxaline-6-carboxylic acid
-
-
2,4-dioxo-4-phenylbutanoic acid
-
specific inhibitor
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-benzylphenyl)-3-cyclohexyl-1-methyl-1H-indole-6-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-([[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-bromo-5-methoxy-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]benzamide
-
-
2-chloro-4-nitro-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]benzamide
-
-
2-cyano-N'-[(1Z)-(3,4,5-trihydroxyphenyl)methylene]acetohydrazide
-
-
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]-1-cyclopentyl-1H-benzimidazole-5-carboxamide
-
-
2-[4-(benzyloxy)phenyl]-1-cyclopentyl-1H-benzimidazole-5-carboxylic acid
-
-
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'-deoxy-5'-O-([2-[(2,2-dimethyl-1-methylidenepropyl)sulfanyl]ethoxy][2-[(2,2-dimethylpropanoyl)sulfanyl]ethoxy]phosphoryl)cytidine
-
-
3'-deoxycytidine
-
-
3'-dGTP
Q6DLV0
-
3,4,5-trihydroxybenzaldehyde O-methyloxime
-
-
3-(1,1-dioxido-4H-1,2,4-benzothiadiazin-3-yl)-4-hydroxy-1-(3-methylbutyl)quinolin-2(1H)-one
-
-
3-(2-C-methyl-b-D-ribofuranosyl)pyrido[2,3-d]pyrimidine-2,7(3H,8H)-dione
-
-
3-(3-nitrophenylazo)cytisine
-
-
3-(3-nitrophenylazo)cytisine
P19711
-
3-(4-chlorophenylazo)cytisine
-
-
3-(4-chlorophenylazo)cytisine
P19711
-
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-(3-furyl)-1-methyl-1H-indole-6-carboxylic acid
-
-
3-cyclohexyl-2-(3-furyl)-1H-indole-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-cyclohexyl-2-phenyl-1H-indole-6-carboxylic acid
-
-
3-cyclohexyl-2-phenyl-1H-pyrrolo[2,3-b]pyridine-6-carboxylic acid
-
-
3-cyclohexyl-2-phenyl-1H-pyrrolo[3,2-b]pyridine-6-carboxylic acid
-
-
3-cyclohexyl-2-phenyl-3H-thieno[2,3-d]imidazole-5-carboxylic acid
-
-
3-cyclohexyl-2-phenylquinoline-6-carboxylic acid
-
-
3-oxo-3-[(2Z)-2-(3,4,5-trihydroxybenzylidene)hydrazino]propanoic acid
-
-
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-[(1S,9aR)-octahydro-2H-quinolizin-1-ylmethyl]-1-phenyl-3-(trifluoromethylphenyl)triazene
P19711
-
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-D-arabinofuranosylcytosine
-
-
4'-azidocytidine
-
R-1479, potent and highly selective inhibitor
4'-azidocytidine
-
-
4-(2-C-methyl-b-D-ribofuranosyl)-3-oxo-3,4-dihydropyrazine-2-carboxamide
-
-
4-(chloromethyl)-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]benzamide
-
-
4-amino-2-chloro-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]benzamide
-
-
4-bromo-1-methyl-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-3-(trifluoromethyl)-1H-pyrazole-5-carboxamide
-
-
4-bromo-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]benzamide
-
-
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-fluoro-N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]benzamide
-
-
4-methyl-N-((5Z)-5-[(5-methyl-2-furyl)methylene]-4-oxo-4,5-dihydro-1,3-thiazol-2-yl)benzenesulfonamide
-
-
4-phenylazo-1-(phenyl)piperazine
-
-
4-phenylazo-1-(phenyl)piperazine
P19711
-
4-phenylazo-1-(pyrimidin-2'-yl)piperazine
-
-
4-phenylazo-1-(pyrimidin-2'-yl)piperazine
P19711
-
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}
P19711
-
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}
P19711
-
4-[(E)-(2,5-difluorophenyl)diazenyl]-N-[[(1S,9aR)-9a-methyloctahydro-2H-quinolizin-1-yl]methyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
-
-
5'-formylpyrogallol
-
-
5'-O-([2-[(2,2-dimethyl-1-methylidenepropyl)sulfanyl]ethoxy][2-[(2,2-dimethylpropanoyl)sulfanyl]ethoxy]phosphoryl)-2'-O-methylcytidine
-
-
5,6-dihydroxy-2-(1,3-thiazol-5-yl)pyrimidine-4-carboxylic acid
-
-
5,6-dihydroxy-2-(2-thienyl)pyrimidine-4-carboxylic acid
-
-
5,6-dihydroxy-2-phenylpyrimidine-4-carboxylic acid
-
-
5,6-dihydroxy-2-[4-(([(1-naphthylsulfonyl)amino]carbonyl)amino)-3-thienyl]pyrimidine-4-carboxylic acid
-
-
5,8-dichloro-1-propyl-2,3,4,9-tetrahydro-1H-carbazole-1-carboxylic acid
-
-
5,8-dichloro-3-propyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
5-((Z)-[(4-methylpiperazin-1-yl)imino]methyl)benzene-1,2,3-triol
-
-
5-(2-amino-2-oxoethoxy)-N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
-
-
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-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-[(3,5-dichlorophenyl)amino]-3-hydroxyisothiazole-4-carbonitrile
-
-
5-[(4-bromophenyl)methyl]-2-phenyl-5H-imidazo[4,5-c]pyridine
P19711
-
5-[(Z)-(morpholin-4-ylimino)methyl]benzene-1,2,3-triol
-
-
5-[(Z)-(phenylimino)methyl]benzene-1,2,3-triol
-
-
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-azauridine
-
-
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-cyclohexyl-5-phenyl-4H-thieno[3,2-b]pyrrole-2-carboxylic acid
-
-
6-ethoxy-9-(2-C-methyl-b-D-ribofuranosyl)-9H-purine
-
-
6-furan-3-yl-9-b-D-ribofuranosyl-9H-purine
-
-
6-methoxy-9-(2-C-methyl-b-D-ribofuranosyl)-9H-purine
-
-
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
-
-
7-(2-C-methyl-beta-D-ribofuranosyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine
-
-
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-(5,6-dideoxy-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
-
-
acycloguanosine
-
-
acycloguanosine
P19711
-
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
-
ATP
Human rhinovirus 16
-
IC50: 0.0053 mM
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
benzyl 1-[[4-([[1-methyl-4-(trifluoromethyl)-1H-pyrrol-2-yl]carbonyl]amino)phenyl]sulfonyl]prolinate
-
-
beta-D-2'-deoxy-2'-fluoro-2'-C-methylcytidine
B6EAV7
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
Ca2+
-
; no activity at 3 mM
CTP
Human rhinovirus 16
-
IC50: 0.0015 mM
CTP
-
reaction at the A-incorporation site is inhibited with inhibition constants of 2.7 mM
cyclohexyl 4-([[1-methyl-3-(trifluoromethyl)-1H-pyrazol-5-yl]carbonyl]amino)benzenesulfonate
-
-
cyclosporine A
-
inhibits HCV replication
dATP
Human rhinovirus 16
-
IC50 above 0.5 mM
dCTP
Human rhinovirus 16
-
IC50: 0.04 mM
ddATP
Human rhinovirus 16
-
IC50 above 1 mM
ddCTP
Human rhinovirus 16
-
IC50 above 1 mM
ddGTP
Human rhinovirus 16
-
IC50: above 0.2 mM
ddTTP
Human rhinovirus 16
-
IC50 above 0.5 mM
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
dGTP
Human rhinovirus 16
-
IC50: 0.1 mM
dimethyl (2S,4S,5R)-2-(2-methylpropyl)-5-thiophen-2-yl-1-[[4-(trifluoromethyl)phenyl]carbonyl]pyrrolidine-2,4-dicarboxylate
-
-
dTTP
Human rhinovirus 16
-
IC50 above 0.5 mM
ErbB3-binding protein 1
-
specifically interacts with the catalytic subunit PB1 of influenza virus RNA polymerase near the catalytic site for RNA polymerization
-
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
P19711
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
Ethyl 4-(phenylazo)-piperazincarboxylate
-
-
Ethyl 4-(phenylazo)-piperazincarboxylate
P19711
-
Fructus Ligustri Lucidi aqueous extract
-
0.005 mg/ml, inhibits intracellular NS5B-catalyzed RNA synthesis
-
GDP
-
competitive with GTP
gliotoxin
Human rhinovirus 16
-
IC50: 0.15 mM
gliotoxin
-
in presence of MnCl2 the IC50 value is 0.036 mM, in presence of Mn2+ the IC50 value is 0.202 mM
GTP
-
competitive inhibitor of initiation but not of elongation
GTP
Human rhinovirus 16
-
IC50: 0.0002 mM
guanidine
-
blocks the initiation step of RNA synthesis in vitro
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
heparin
-
0.0005 mM, 50% inhibition
heparin
-
IC50: 80 ng/ml
heparin
-
100 nM heparin rapidly inactivates 3Dpol by inhibiting reinitiation
HgCl2
-
inhibition is reversed by incubation with an excess amount of dithiothreitol and 2-mercaptoethanol
JTK-109
-
potent inhibitor
K+
Human rhinovirus 16
-
above 10 mM
KCl
-
reversible inhibition at high concentrations
KCl
-
100 mM, slight decrease in activity
KCl
Human rhinovirus 2
-
50 mM, 90% inhibition
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-diphenylquinoxalin-6-yl)carbonyl]-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
-
-
Mg2+
-
12.5 mM, replicase activity is reduced by 50%
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
Mn2+
-
above 2 mM
Mycophenolic acid
-
-
Mycophenolic acid
P19711
-
N'-[4-(2,5-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
-
N'-[4-(2,5-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
P19711
-
N'-[4-(2,6-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
-
-
N'-[4-(2,6-difluorophenylazo)phenyl]-N,N-dimethylpropane-1,3-diamine
P19711
-
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,N-dimethyl-1-(1,3-diphenyltriazen-3-yl)-3-propanamine
-
-
N,N-dimethyl-1-(1,3-diphenyltriazen-3-yl)-3-propanamine
P19711
-
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
P19711
-
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
P19711
-
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
P19711
-
N,N-dimethyl-N'-4-(4'-tolylazo)phenylpropane-1,3-diamine
-
-
N,N-dimethyl-N'-4-(4'-tolylazo)phenylpropane-1,3-diamine
P19711
-
N,N-dimethyl-N'-[4-(3-nitrophenylazo)phenyl]propane-1,3-diamine
-
-
N,N-dimethyl-N'-[4-(3-nitrophenylazo)phenyl]propane-1,3-diamine
P19711
-
N,N-dimethyl-N'-[4-(4-nitrophenylazo)phenyl]propane-1,3-diamine
-
-
N,N-dimethyl-N'-[4-(4-nitrophenylazo)phenyl]propane-1,3-diamine
P19711
-
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
P19711
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-difuran-2-ylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophan
-
-
N-[(2,3-difuran-2-ylquinoxalin-6-yl)carbonyl]-L-tryptophan
-
-
N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophan
-
-
N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-6-hydroxy-L-tryptophan
-
-
N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-L-tryptophan
-
-
N-[(2,3-dipyridin-2-ylquinoxalin-6-yl)carbonyl]-L-tryptophan
-
-
N-[(2,3-ditetrahydrofuran-2-ylquinoxalin-6-yl)carbonyl]-6-hydroxy-L-tryptophan
-
-
N-[(2,3-ditetrahydrofuran-2-ylquinoxalin-6-yl)carbonyl]-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-[(2-cyclohexyl-3-phenylquinoxalin-6-yl)carbonyl]-L-tryptophan
-
-
N-[(3-cyclohexyl-2-phenylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophan
-
-
N-[(3-cyclohexyl-2-phenylquinoxalin-6-yl)carbonyl]-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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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-(pyrrolidin-1-ylsulfonyl)phenyl]-2-(trifluoromethyl)benzamide
-
-
N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-3-(trifluoromethyl)benzamide
-
-
N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]-4-(trifluoromethyl)benzamide
-
-
N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]furan-2-carboxamide
-
-
N-[4-(pyrrolidin-1-ylsulfonyl)phenyl]thiophene-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)-phenyldiazenyl]-5,6,7,8-tetrahydronaphthalen-1-amine}
P19711
-
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}
P19711
-
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(3-methoxyphenyl)quinoxalin-6-yl]carbonyl]-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-fluorophenyl)quinoxalin-6-yl]carbonyl]-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-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-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
-
-
NaCl
-
slight decrease in activity
NaCl
-
at high concentrations
NaCl
-
150 mM or above, about 90% of acctivity is lost
NEM
-
0.1 mM, reduces the transcription activity down to 10%
NTP
-
3Dpol is inhibited by NTP concentrations higher than 2 mM
p-Hydroxymercuriphenylsulfonate
-
0.1 mM, reduces the transcription activity down to 10%
pancreatic RNase
-
0.006 mg/ml, marked inhibition
-
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
-
-
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
-
polylysine
-
IC50: 250 ng/ml
ppGpp
-
competitive inhibitor of initiation but not of elongation
ppGpp
-
competitive with GTP
R7128
B6EAV7
is the prodrug of PSI-6130, inhibits the enzyme and viral replication
ribavirin
-
-
RNA
-
inhibited by high non-template RNA concentrations. This inhibition indicates feedback regulation of minus-strand synthesis
RNase
-
completely eliminates incorporation
-
RNase
-
RNAse A, 0.01 mg/ml, or Rnase T1, 0.002 mg/ml, inhibit the reaction by 90-95%
-
RNase
-
pancreatic RNAse and T1 RNAse
-
Sodium diphosphate
-
10 mM, decreases incorporation down to 5%
spermine
-
1 mM, 50% inhibition
tert-butyl 1-[[4-([[1-methyl-4-(trifluoromethyl)-1H-pyrrol-2-yl]carbonyl]amino)phenyl]sulfonyl]piperidine-2-carboperoxoate
-
-
UTP
Human rhinovirus 16
-
IC50: 0.0023 mM
UTP
-
reaction at the A-incorporation site is inhibited with inhibition constants of 3.2 mM
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
Zn2+
-
complete inhibition at concentrations above 1.25 mM ZnCl2
Zn2+
Human rhinovirus 16
-
IC50: 0.0006 mM, suppression of inhibition by dithiothreitol
[(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
-
-
[(2Z)-2-(3,4,5-trihydroxybenzylidene)hydrazino]acetic acid
-
-
[N,N-dimethyl-N'-(4-phenylazophenyl)]propane-1,3-diamine
-
-
[N,N-dimethyl-N'-(4-phenylazophenyl)]propane-1,3-diamine
P19711
-
Mn2+
Human rhinovirus 16
-
polymerase activity drops sharply at 3 mM
additional information
-
activity is depressed by increasing monovalent ion concentrations
-
additional information
-
activity is lowered at ionic strength of 0.1
-
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
Human rhinovirus 16
-
the enzyme is resistant to 0.02 mg/ml rifampicin
-
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
-
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
-
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
O92972
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
B6EAV7
inhibitor efficiency with wild-type and mutant enzymes, overview
-
additional information
P26663
5,5- and 6,6-dialkyl-5,6-dihydro-1H-pyridin-2-ones as potent inhibitors of HCV NS5B polymerase, overview
-
additional information
-
RdRp inhibition and antiviral potencies of the inhibitor compounds, overview
-
additional information
P19711
RdRp inhibition and antiviral potencies of the inhibitor compounds, overview
-
additional information
-
RdRp inhibition and antiviral potencies of the inhibitor compounds, overview
-
additional information
Q0G9P7
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
-
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
-
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
-
not inhibitory: rifamycin
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5-chlorosalicylic acid
B3SND7, -
2 mM, induction of RdRp gene expression
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
-
GTP
P19711
required for de novo (primer-independent) initiation
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
-
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
salicylic acid
B3SND7, -
2 mM, induction of RdRp gene expression
Sodium diethyldithiocarbamate
-
5 mM, great stimulation of template-dependent activity and to a lesser extent template-independent activity
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
-
host factor
-
hexameric host-coded protein of 12500 Da subunits is required for in vitro Qbeta RNA replication
-
additional information
B3SND7, -
RdRp is induced by fungal infection of Rhizoctonia solani
-
additional information
-
RdRp phosphorylation by PRK2 is required for activation and RNA replication
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0029
-
ATP
-
pH 7.5, 23C, reaction with heteropolymeric template T500, C-terminally truncated enzyme form NS5B(DELTA21)
0.0047
-
ATP
-
pH 8.0, 25C, HCV JFH1a de novo transcription
0.008
-
ATP
Human rhinovirus 16
-
pH 7.0, 30C, sshRNA as template
0.0108
-
ATP
-
pH 7.5, 22C, HCV 3'-end as template
0.0332
-
ATP
-
pH 8.0, 25C, Influenza ApG-primed transcription
0.00026
-
CTP
Human rhinovirus 16
-
pH 7.0, 30C, sshRNA as template
0.00028
-
CTP
-
pH 7.5, 22C, HCV 3'-end as template
0.0006
-
CTP
-
pH 7.5, 23C, reaction with heteropolymeric template T500, C-terminally truncated enzyme form NS5B(DELTA21)
0.0027
-
CTP
-
pH 8.0, 25C, HCV JFH1a de novo transcription
0.0289
-
CTP
-
pH 8.0, 25C, Influenza ApG-primed transcription
0.039
-
CTP
AJ242654
pH 7.5, 30C
0.00019
-
GTP
-
pH 7.5, 23C, deletion mutant DELTAC21, poly(C)-oligo(G)18 as template
0.00027
-
GTP
-
pH 7.5, 23C, full-length enzyme, poly(C)-oligo(G)18 as template
0.00054
-
GTP
-
pH 7.5, 22C, HCV 3'-end as template
0.001
-
GTP
Human rhinovirus 16
-
pH 7.0, 30C, sshRNA as template
0.0014
-
GTP
-
pH 7.5, 23C, reaction with heteropolymeric template T500, C-terminally truncated enzyme form NS5B(DELTA21)
0.0029
-
GTP
-
pH 7.5, 22C, HCV 3'-end as template
0.00297
-
GTP
-
pH 7.5, 22C, poly(C)/oligo(G) as template
0.0035
-
GTP
-
pH 8.2, 25C, enzyme form DELTA21 that lacks the C-terminal 21 hydrophobic residues
0.007
-
GTP
Human rhinovirus 16
-
pH 7.0, 30C, poly(C) as template
0.0107
-
GTP
-
pH 8.0, 25C, Influenza ApG-primed transcription
0.02
-
GTP
-
30C, cross-linked enzyme
0.052
-
GTP
-
poly(C)-oligo(G) as template
0.087
-
GTP
-
pH 8.0, 25C, HCV JFH1a de novo transcription
5.05
-
GTP
-
pH 8.2, 25C, mutant enzyme
10.1
-
GTP
-
pH 8.2, 25C, mutant enzyme
11.25
-
GTP
-
pH 8.2, 25C, mutant enzyme
15.3
-
GTP
-
pH 8.2, 25C, mutant enzyme R158A
25.9
-
GTP
-
pH 8.2, 25C, mutant enzyme
0.0006
-
UTP
-
pH 7.5, 23C, reaction with heteropolymeric template T500, C-terminally truncated enzyme form NS5B(DELTA21)
0.0021
-
UTP
Human rhinovirus 16
-
pH 7.0, 30C, sshRNA as template
0.004
-
UTP
-
in presence of 0.3 mM each of ATP, CTP and GTP
0.0049
-
UTP
-
pH 7.5, 23C, full-length enzyme, poly(A)-oligo(U)18 as template
0.005
-
UTP
-
30C, pH 8.0
0.0054
-
UTP
-
pH 7.5, 23C, deletion mutant DELTAC21, poly(A)-oligo(U)18 as template
0.0057
-
UTP
-
pH 7.5, 23C, C-terminally truncated enzyme form NS5B(DELTA21), reaction with dT16/poly(rA)
0.0075
-
UTP
-
pH 8.0, 25C, HCV JFH1a de novo transcription
0.012
-
UTP
Human rhinovirus 16
-
pH 7.0, 30C, poly(A) as template
0.013
-
UTP
-
pH 7.5, 23C, full-length enzyme, reaction with dT16/poly(rA)
0.022
-
UTP
-
pH 7.5, 22C, poly(A)/oligo(U) as template
0.022
-
UTP
-
pH 8.0, 25C, Influenza ApG-primed transcription
0.03
-
UTP
-
pH 8.2, 29C
33.8
-
GTP
-
pH 8.2, 25C, mutant enzyme
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
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.000105
-
ATP
-
pH 7.5, 23C, reaction with heteropolymeric template T500, C-terminally truncated enzyme form NS5B(DELTA21)
0.000617
-
ATP
Human rhinovirus 16
-
pH 7.0, 30C, sshRNA as template
0.000133
-
CTP
-
pH 7.5, 23C, reaction with heteropolymeric template T500, C-terminally truncated enzyme form NS5B(DELTA21)
0.000505
-
CTP
Human rhinovirus 16
-
pH 7.0, 30C, sshRNA as template
16
-
CTP
AJ242654
pH 7.5, 30C
0.000383
-
GTP
-
pH 7.5, 23C, reaction with heteropolymeric template T500, C-terminally truncated enzyme form NS5B(DELTA21)
0.0005
-
GTP
-
pH 7.5, 23C, full-length enzyme, poly(C)-oligo(G)18 as template
0.00108
-
GTP
-
pH 7.5, 23C, deletion mutant DELTAC21, poly(C)-oligo(G)18 as template
0.00375
-
GTP
Human rhinovirus 16
-
pH 7.0, 30C, sshRNA as template
0.005
-
GTP
-
poly(C)-oligo(G) as template
0.000167
-
UTP
-
pH 7.5, 23C, reaction with heteropolymeric template T500, C-terminally truncated enzyme form NS5B(DELTA21)
0.00167
-
UTP
-
pH 7.5, 23C, full-length enzyme, reaction with dT16/poly(rA)
0.00373
-
UTP
-
pH 7.5, 23C, full-length enzyme, poly(A)-oligo(U)18 as template
0.00478
-
UTP
Human rhinovirus 16
-
pH 7.0, 30C, sshRNA as template
0.00583
-
UTP
-
pH 7.5, 23C, deletion mutant DELTAC21, poly(A)-oligo(U)18 as template
0.0272
-
UTP
-
pH 7.5, 23C, C-terminally truncated enzyme form NS5B(DELTA21), reaction with dT16/poly(rA)
0.23
-
UTP
Human rhinovirus 16
-
pH 7.0, 30C, poly(A) as template
0.0211
-
GTP
Human rhinovirus 16
-
pH 7.0, 30C, poly(C) as template
additional information
-
additional information
-
the enzyme is able to copy long heteropolymeric templates with an elongation rate of 150-200 nucleotides per min at 22C
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
410
-
CTP
AJ242654
pH 7.5, 30C
8829
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.000016
-
2'-C-methylcytidine
B6EAV7
clinical isolate GT-1a
0.000017
-
2'-C-methylcytidine
B6EAV7
clinical isolate GT-1b
0.00058
-
2'-C-methylcytidine
B6EAV7
mutant S282T
0.000021
-
aptamer F38
-
-
-
0.000018
-
aptamer F47
-
-
-
0.000075
-
aptamer F52
-
-
-
0.000034
-
beta-D-2'-deoxy-2'-fluoro-2'-C-methylcytidine
B6EAV7
clinical isolate GT-1a
0.00004
-
beta-D-2'-deoxy-2'-fluoro-2'-C-methylcytidine
B6EAV7
clinical isolate GT-1b
0.000044
-
beta-D-2'-deoxy-2'-fluoro-2'-C-methylcytidine
B6EAV7
mutant S282T
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
-
0.23
-
gliotoxin
-
-
additional information
-
additional information
-
kinetics of inhibition of VPg uridylylation, overview
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
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
-
-
0.0013
-
(2E)-3-(4-[[(2-cyclohexyl-3-phenylquinoxalin-6-yl)carbonyl]amino]phenyl)prop-2-enoic acid
-
-
0.00069
-
(2E)-3-[4-([[1-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
-
-
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
-
-
0.0051
-
(2E)-3-[4-([[1-([[2-cyclohexyl-3-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
-
-
0.0013
-
(2E)-3-[4-([[1-([[3-cyclohexyl-2-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
-
-
0.017
-
(2E)-3-[4-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)phenyl]prop-2-enoic acid
-
-
0.0041
-
(2E)-3-[4-([[2-cyclohexyl-3-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)phenyl]prop-2-enoic acid
-
-
0.0046
-
(2E)-3-[4-([[3-cyclohexyl-2-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)phenyl]prop-2-enoic acid
-
-
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
-
-
0.0031
-
(2S)-1-[(2-amino-4-chloro-5-methylphenyl)sulfonyl]pyrrolidine-2-carboxylic acid
-
-
0.00008
-
(2S)-1-[(3,4,5-trichloro-2-hydroxyphenyl)sulfonyl]pyrrolidine-2-carboxylic acid
-
-
0.00077
-
(2S)-1-[(3,5-dichloro-2-hydroxyphenyl)sulfonyl]pyrrolidine-2-carboxylic acid
-
-
0.0007
-
(2S)-2-[(2,4-dichlorobenzoyl)(3-nitrobenzyl)amino]-3-phenylpropanoic acid
-
-
0.0038
-
(2S,4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)pyrrolidine-2,4-dicarboxylic acid
-
full-length enzyme
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
-
-
0.00019
-
(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-(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
-
full-length enzyme
0.0067
-
(2Z)-2-(benzoylamino)-3-(5-phenyl-2-furyl)acrylic acid
-
-
0.0001
-
(2Z)-2-(benzoylamino)-3-[4-(2-bromophenoxy)phenyl]acrylic acid
-
-
0.0051
-
(2Z)-3-[4-([[1-([[2-cyclohexyl-3-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
-
-
0.0013
-
(2Z)-3-[4-([[1-([[3-cyclohexyl-2-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoic acid
-
-
0.0032
-
(4R,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(ethoxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
0.001
-
(4R,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(hydroxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
0.000014
-
(4S,5R)-1-[(3-bromo-4-tert-butylphenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
0.00002
-
(4S,5R)-1-[(4-tert-butyl-3-chlorophenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
0.00043
-
(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(ethoxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
0.00073
-
(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(hydroxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
0.00044
-
(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(methoxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
0.000005
-
(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
0.000019
-
(4S,5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-methoxy-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
0.0031
-
(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-4-(phenylcarbamoyl)-5-(1,3-thiazol-2-yl)-L-proline
-
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
-
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
-
full-length enzyme
0.00097
-
(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
0.0044
-
(4S,5R)-1-[(4-tert-butylphenyl)carbonyl]-4-carbamoyl-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
full-length enzyme
0.068
-
(4S,5R)-4-(benzylcarbamoyl)-1-[(4-tert-butylphenyl)carbonyl]-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
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
-
full-length enzyme
0.03
-
(5,7-difluoro-1-propyl-2,3,4,9-tetrahydro-1H-carbazol-1-yl)acetic acid
-
-
0.0023
-
(5,8-dicyano-1-propyl-2,3,4,9-tetrahydro-1H-carbazol-1-yl)acetic acid
-
-
0.000055
-
(5-cyano-6-fluoro-8-methyl-1-propyl-3,4-dihydro-1H-[1]benzothieno[2,3-c]pyran-1-yl)acetic acid
-
-
0.0021
-
(5-cyano-8-fluoro-1-propyl-2,3,4,9-tetrahydro-1H-carbazol-1-yl)acetic acid
-
-
0.00057
-
(5-cyano-8-methyl-1-propyl-1,3,4,9-tetrahydropyrano[3,4-b]indol-1-yl)acetic acid
-
-
0.0021
-
(5-cyano-8-methyl-1-propyl-2,3,4,9-tetrahydro-1H-carbazol-1-yl)acetic acid
-
-
0.0023
-
(5R)-1-[(4-tert-butyl-3-methoxyphenyl)carbonyl]-4-(methoxymethyl)-2-(2-methylpropyl)-5-(1,3-thiazol-2-yl)-L-proline
-
-
0.0004
-
1,3-bis-(4-chloro-1H(3H)-triazolo[4,5-g]quinoline)propan-2-one
-
pH 7.0, 22C
0.00001
-
1-(2-cyclopropylethyl)-3-(1,1-dioxido-4H-1,2,4-benzothiadiazin-3-yl)-6-fluoro-4-hydroxyquinolin-2(1H)-one
-
-
0.00011
-
1-(cyclobutylamino)-3-(1,1-dioxido-4H-1,2,4-benzothiadiazin-3-yl)-4-hydroxyquinolin-2(1H)-one
-
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
-
polymerase from 1 a genotype
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
-
-
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
-
-
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
-
-
0.00041
-
1-cyclohexyl-2-(2-fluoro-4-[[2-methoxy-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
-
-
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
-
-
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
-
-
0.00015
-
1-cyclohexyl-2-(2-fluoro-4-[[5-(2-oxopyrrolidin-1-yl)-2-piperidin-1-ylbenzyl]oxy]phenyl)-1H-benzimidazole-5-carboxylic acid
-
-
0.0016
-
1-cyclohexyl-2-(3-furyl)-1H-benzimidazole-5-carboxylic acid
-
-
0.00003
-
1-cyclohexyl-2-(4-[[2-morpholin-4-yl-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]phenyl)-1H-indole-5-carboxylic acid
-
-
0.00064
-
1-cyclohexyl-2-(4-[[4-(dimethylcarbamoyl)phenyl](phenyl)methoxy]-2-fluorophenyl)-1H-benzimidazole-5-carboxylic acid
-
-
0.000071
-
1-cyclohexyl-2-(4-[[5-(1,1-dioxidoisothiazolidin-2-yl)-2-morpholin-4-ylbenzyl]oxy]-2-fluorophenyl)-1H-benzimidazole-5-carboxylic acid
-
-
0.000068
-
1-cyclohexyl-2-(4-[[5-(dimethylcarbamoyl)-2-morpholin-4-ylbenzyl]oxy]-2-fluorophenyl)-1H-benzimidazole-5-carboxylic acid
-
-
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
-
-
0.0065
-
1-cyclohexyl-2-phenyl-1H-benzimidazole-5-carboxylic acid
-
-
0.0004
-
1-cyclohexyl-2-phenyl-1H-indole-5-carboxylic acid
-
-
0.000048
-
1-cyclohexyl-2-[2-fluoro-4-([5-[(1-methylethyl)carbamoyl]-2-morpholin-4-ylbenzyl]oxy)phenyl]-1H-benzimidazole-5-carboxylic acid
-
-
0.000099
-
1-cyclohexyl-2-[2-fluoro-4-([5-[(methoxyacetyl)(methyl)amino]-2-morpholin-4-ylbenzyl]oxy)phenyl]-1H-benzimidazole-5-carboxylic acid
-
-
0.00013
-
1-cyclohexyl-2-[2-fluoro-4-[(2-morpholin-4-ylbenzyl)oxy]phenyl]-1H-benzimidazole-5-carboxylic acid
-
-
0.00014
-
12-cyclohexylindolo[1,2-c][1,3]benzoxazine-9-carboxylic acid
-
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
-
-
0.000009
-
13-cyclohexyl-5-(2-piperidin-1-ylethyl)-6,7-dihydro-5H-indolo[1,2-d][1,4]benzodiazepine-10-carboxylic acid
-
-
0.000021
-
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
0.000077
-
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
0.000038
-
13-cyclohexyl-6,7-dihydroindolo[1,2-d][1,4]benzothiazepine-10-carboxylic acid
-
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
-
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
-
dihedral angle between the C2-aryl group and the indole ring is 61
0.0019
-
2'-C-methyladenosine
-
-
0.00009
-
2'-C-methylcytidine
B6EAV7
clinical isolate GT-1a
0.00018
-
2'-C-methylcytidine
B6EAV7
clinical isolate GT-1b
0.0012
-
2'-C-methylcytidine
-
-
0.01
-
2'-C-methylcytidine
B6EAV7
mutant S282T
0.00013
-
2'-C-methylguanosine
-
-
0.0038
-
2'-O-methylcytidine
-
-
0.0055
-
2,3-bis(4-fluorophenyl)quinoxaline-6-carboxylic acid
-
-
0.04
-
2,3-bis(4-methylphenyl)quinoxaline-6-carboxylic acid
-
-
0.017
-
2,3-di-2-furylquinoxaline-6-carboxylic acid
-
-
0.079
-
2,3-diphenylquinoxaline-6-carboxylic acid
-
-
0.004
-
2,4-dioxo-4-phenylbutanoic acid
-
30C, pH 8.0
0.0015
-
2-(3-[[(2-chlorobenzyl)carbamoyl]amino]thiophen-2-yl)-5,6-dihydroxypyrimidine-4-carboxylic acid
-
-
0.00012
-
2-(4-benzylphenyl)-3-cyclohexyl-1-methyl-1H-indole-6-carboxylic acid
-
-
0.000009
-
2-(4-chlorophenyl)-3-cyclohexyl-1-[2-[4-(diethylamino)piperidin-1-yl]-2-oxoethyl]-1H-indole-6-carboxylic acid
-
-
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
-
-
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
-
-
0.00023
-
2-(4-[[2-(4-chlorophenoxy)-5-(2-oxopyrrolidin-1-yl)benzyl]oxy]-2-fluorophenyl)-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
-
-
0.000017
-
2-(4-[[4'-chloro-4-(2-oxopyrrolidin-1-yl)biphenyl-2-yl]methoxy]-2-fluorophenyl)-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
-
-
0.00007
-
2-(4-[[5-(acetylamino)-2-morpholin-4-ylbenzyl]oxy]-2-fluorophenyl)-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
-
-
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
-
-
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
-
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
-
polymerase from 1 a genotype
0.0001
-
2-amino-7-(2-C-methyl-beta-D-ribofuranosyl)-3,7-dihydro-4H-pyrrolo[2,3-d]pyrimidin-4-one
-
-
0.007
-
2-cyano-N'-[(1Z)-(3,4,5-trihydroxyphenyl)methylene]acetohydrazide
-
-
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
-
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
-
wild type enzyme
0.0032
-
2-[4-(benzyloxy)phenyl]-1-cyclopentyl-1H-benzimidazole-5-carboxylic acid
-
-
0.000006
-
2-[4-(benzyloxy)phenyl]-3-cyclohexyl-1-[2-(dimethylamino)-2-oxoethyl]-1H-indole-6-carboxylic acid
-
-
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
-
-
0.000042
-
2-[4-([5-[acetyl(1-methylethyl)amino]-2-morpholin-4-ylbenzyl]oxy)-2-fluorophenyl]-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
-
-
0.000051
-
2-[4-([5-[acetyl(methyl)amino]-2-morpholin-4-ylbenzyl]oxy)-2-fluorophenyl]-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
-
-
0.0001
-
2-[4-[(5-chloro-2-morpholin-4-ylbenzyl)oxy]-2-fluorophenyl]-1-cyclohexyl-1H-benzimidazole-5-carboxylic acid
-
-
0.0012
-
3'-deoxycytidine
-
-
0.00022
-
3'-dGTP
Q6DLV0
-
0.012
-
3,4,5-trihydroxybenzaldehyde O-methyloxime
-
-
0.000032
-
3-(1,1-dioxido-4H-1,2,4-benzothiadiazin-3-yl)-4-hydroxy-1-(3-methylbutyl)quinolin-2(1H)-one
-
-
0.000017
-
3-(benzyloxy)-13-cyclohexyl-6,7-dihydroindolo[1,2-d][1,4]benzoxazepine-10-carboxylic acid
-
-
0.008
-
3-(isopropyl[(4-methylphenyl)sulfonyl]amino)-5-phenylthiophene-2-carboxylic acid
-
-
0.0014
-
3-([(2,4-dimethylphenyl)sulfonyl]amino)-5-phenylthiophene-2-carboxylic acid
-
-
0.012
-
3-([(4-chloro-2,5-dimethylphenyl)sulfonyl]amino)-5-phenylthiophene-2-carboxamide
-
-
0.0012
-
3-allyl-5,8-dichloro-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
0.0145
-
3-allyl-8-cyano-5-fluoro-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
0.011
-
3-allyl-8-cyano-5-methyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
0.0063
-
3-allyl-8-cyano-7-fluoro-5-methyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
0.0012
-
3-benzyl-5-chloropyrido[3,2-g]quinoxalin-2(1H)-one
-
pH 7.0, 22C
0.0019
-
3-butyl-5,8-dichloro-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
0.0054
-
3-butyl-8-cyano-5-fluoro-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
0.0046
-
3-butyl-8-cyano-5-methyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
0.0015
-
3-butyl-8-cyano-7-fluoro-5-methyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
0.00003
-
3-cyclohexyl-1-(2-oxo-2-piperidin-1-ylethyl)-2-phenyl-1H-indole-6-carboxylic acid
-
-
0.000018
-
3-cyclohexyl-1-(2-[methyl[(1-methylpiperidin-3-yl)methyl]amino]-2-oxoethyl)-2-phenyl-1H-indole-6-carboxylic acid
-
-
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
-
-
0.000018
-
3-cyclohexyl-1-[2-(dimethylamino)-2-oxoethyl]-2-(4-methoxyphenyl)-1H-indole-6-carboxylic acid
-
-
0.00006
-
3-cyclohexyl-1-[2-(dimethylamino)-2-oxoethyl]-2-phenyl-1H-indole-6-carboxylic acid
-
-
0.00032
-
3-cyclohexyl-1-[2-(dimethylamino)-2-oxoethyl]-2-phenyl-1H-pyrrolo[2,3-b]pyridine-6-carboxylic acid
-
-
0.000016
-
3-cyclohexyl-2-(3-furyl)-1-methyl-1H-indole-6-carboxylic acid
-
-
0.00003
-
3-cyclohexyl-2-(3-furyl)-1H-indole-6-carboxylic acid
-
-
0.000015
-
3-cyclohexyl-2-furan-3-yl-1-[2-oxo-2-(4-pyrrolidin-1-ylpiperidin-1-yl)ethyl]-1H-indole-6-carboxylic acid
-
-
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
-
-
0.000046
-
3-cyclohexyl-2-phenyl-1H-indole-6-carboxylic acid
-
-
0.00015
-
3-cyclohexyl-2-phenyl-1H-pyrrolo[2,3-b]pyridine-6-carboxylic acid
-
-
0.0019
-
3-cyclohexyl-2-phenyl-1H-pyrrolo[3,2-b]pyridine-6-carboxylic acid
-
-
0.0138
-
3-cyclohexyl-2-phenyl-3H-thieno[2,3-d]imidazole-5-carboxylic acid
-
-
0.0048
-
3-cyclohexyl-2-phenylquinoline-6-carboxylic acid
-
-
0.003
-
3-oxo-3-[(2Z)-2-(3,4,5-trihydroxybenzylidene)hydrazino]propanoic acid
-
-
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
-
-
0.0015
-
3-[[(trans-4-methylcyclohexyl)carbonyl](1-methylethyl)amino]-5-phenylthiophene-2-carboxylic acid
-
-
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
-
-
0.00006
-
4-chloro-2-(4-nitrophenyl)-3H-imidazo[4,5-g]quinoline
-
pH 7.0, 22C
0.0008
-
4-chloro-2-(4-nitrophenyl)-3H-imidazo[4,5-g]quinoline
-
pH 7.0, 22C
0.0021
-
4-methyl-N-((5Z)-5-[(5-methyl-2-furyl)methylene]-4-oxo-4,5-dihydro-1,3-thiazol-2-yl)benzenesulfonamide
-
-
1
-
5'-formylpyrogallol
-
-
0.00076
-
5,6-dihydroxy-2-(1,3-thiazol-5-yl)pyrimidine-4-carboxylic acid
-
-
0.0026
-
5,6-dihydroxy-2-(2-thienyl)pyrimidine-4-carboxylic acid
-
-
0.03
-
5,6-dihydroxy-2-phenylpyrimidine-4-carboxylic acid
-
-
0.00003
-
5,6-dihydroxy-2-[4-(([(1-naphthylsulfonyl)amino]carbonyl)amino)-3-thienyl]pyrimidine-4-carboxylic acid
-
-
0.0032
-
5,8-dichloro-1-propyl-2,3,4,9-tetrahydro-1H-carbazole-1-carboxylic acid
-
-
0.00055
-
5,8-dichloro-3-propyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
0.0021
-
5,8-dichloro-3-propyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
0.005
-
5-((Z)-[(4-methylpiperazin-1-yl)imino]methyl)benzene-1,2,3-triol
-
-
0.0032
-
5-(2-amino-2-oxoethoxy)-N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
-
-
0.00044
-
5-(4-bromophenylmethylene)-3-(benzenesulfonylamino)-4-oxo-2-thionothiazolidine
-
37C, pH 7.5
0.00054
-
5-(4-chlorophenylmethylene)-3-(benzenesulfonylamino)-4-oxo-2-thionothiazolidine
-
37C, pH 7.5
0.00027
-
5-(4-cyanophenyl)-3-([(2-methylphenyl)sulfonyl]amino)thiophene-2-carboxylic acid
-
-
0.0018
-
5-(4-[[(2-cyclohexyl-3-phenylquinoxalin-6-yl)carbonyl]amino]phenyl)furan-2-carboxylic acid
-
-
0.0016
-
5-(4-[[(3-cyclohexyl-2-phenylquinoxalin-6-yl)carbonyl]amino]phenyl)furan-2-carboxylic acid
-
-
0.000027
-
5-(carboxymethoxy)-N-[(1-cyclohexyl-2-furan-3-yl-1H-benzimidazol-5-yl)carbonyl]-L-tryptophan
-
-
0.0059
-
5-([3,5-bis(trifluoromethyl)phenyl]amino)-3-hydroxyisothiazole-4-carbonitrile
-
-
0.001
-
5-chloro-3-phenylpyrido[3,2-g]quinoxalin-2(1H)-one
-
pH 7.0, 22C
0.01
-
5-cyano-8-fluoro-1-propyl-2,3,4,9-tetrahydro-1H-carbazole-1-carboxylic acid
-
-
0.015
-
5-cyano-8-methyl-1-propyl-2,3,4,9-tetrahydro-1H-carbazole-1-carboxylic acid
-
-
0.015
-
5-hydroxy-N-[[3-(3-methoxyphenyl)-2-(4-methoxyphenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
-
-
0.0002
-
5-[(3,5-dichlorophenyl)amino]-3-hydroxyisothiazole-4-carbonitrile
-
-
0.01
-
5-[(Z)-(morpholin-4-ylimino)methyl]benzene-1,2,3-triol
-
-
0.5
-
5-[(Z)-(phenylimino)methyl]benzene-1,2,3-triol
-
-
0.0032
-
6-(2-amino-2-oxoethoxy)-N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
-
-
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
-
-
0.00006
-
6-cyclohexyl-4-[2-(dimethylamino)-2-oxoethyl]-5-phenyl-4H-thieno[3,2-b]pyrrole-2-carboxylic acid
-
-
0.00007
-
6-cyclohexyl-5-phenyl-4H-thieno[3,2-b]pyrrole-2-carboxylic acid
-
-
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
-
-
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
-
wild type enzyme
0.00012
-
7-(2-C-methyl-beta-D-ribofuranosyl)-7H-pyrrolo[2,3-d]pyrimidin-4-amine
-
-
0.0000715
-
8,8'-[carbonylbis(iminobenzene-3,1-diylcarbonylimino)]dinaphthalene-1,3,5-trisulfonic acid
-
wild-type, pH 7.5, 30C
0.00028
-
8,8'-[carbonylbis(iminobenzene-3,1-diylcarbonylimino)]dinaphthalene-1,3,5-trisulfonic acid
-
mutant Y41A, pH 7.5, 30C
0.0058
-
8-chloro-1-propyl-5-(trifluoromethyl)-2,3,4,9-tetrahydro-1H-carbazole-1-carboxylic acid
-
-
0.0081
-
8-cyano-5-fluoro-3-propyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
0.0047
-
8-cyano-5-methyl-3-propyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
0.0018
-
8-cyano-7-fluoro-5-methyl-3-propyl-1,2,3,4-tetrahydrocyclopenta[b]indole-3-carboxylic acid
-
-
0.0000003
-
A-837093
-
polymerase from 1 b genotype
0.0000007
-
A-837093
-
polymerase from 1 b genotype
0.0000158
-
aptamer F38
-
-
-
0.0000106
-
aptamer F47
-
-
-
0.0000164
-
aptamer F52
-
-
-
0.0053
-
ATP
Human rhinovirus 16
-
IC50: 0.0053 mM
0.00011
-
beta-D-2'-deoxy-2'-fluoro-2'-C-methylcytidine
B6EAV7
clinical isolate GT-1b
0.00013
-
beta-D-2'-deoxy-2'-fluoro-2'-C-methylcytidine
B6EAV7
clinical isolate GT-1a
0.0007
-
beta-D-2'-deoxy-2'-fluoro-2'-C-methylcytidine
B6EAV7
mutant S282T
0.0015
-
CTP
Human rhinovirus 16
-
IC50: 0.0015 mM
0.5
-
dATP
Human rhinovirus 16
-
IC50 above 0.5 mM
0.04
-
dCTP
Human rhinovirus 16
-
IC50: 0.04 mM
1
-
ddATP
Human rhinovirus 16
-
IC50 above 1 mM
1
-
ddCTP
Human rhinovirus 16
-
IC50 above 1 mM
0.2
-
ddGTP
Human rhinovirus 16
-
IC50: above 0.2 mM
0.5
-
ddTTP
Human rhinovirus 16
-
IC50 above 0.5 mM
0.1
-
dGTP
Human rhinovirus 16
-
IC50: 0.1 mM
0.5
-
dTTP
Human rhinovirus 16
-
IC50 above 0.5 mM
0.037
-
ethyl (2E)-3-[4-([[1-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclobutyl]carbonyl]amino)phenyl]prop-2-enoate
-
-
0.1
-
ethyl (2E)-3-[4-([[1-([[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]amino)cyclopentyl]carbonyl]amino)phenyl]prop-2-enoate
-
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
-
IC50 above 0.1 mM
0.15
-
gliotoxin
Human rhinovirus 16
-
IC50: 0.15 mM
0.202
-
gliotoxin
-
in presence of MnCl2 the IC50 value is 0.036 mM, in presence of Mn2+ the IC50 value is 0.202 mM
0.0002
-
GTP
Human rhinovirus 16
-
IC50: 0.0002 mM
0.000017
-
JTK-109
-
-
0.0086
-
methyl 5-(2-amino-2-oxoethoxy)-N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophanate
-
-
0.0086
-
methyl 6-(2-amino-2-oxoethoxy)-N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophanate
-
-
0.026
-
methyl N-[(2,3-difuran-2-ylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophanate
-
-
0.072
-
methyl N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophanate
-
-
0.072
-
methyl N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-6-hydroxy-L-tryptophanate
-
-
0.1
-
methyl N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-L-tryptophanate
-
IC50 above 0.1 mM
0.1
-
methyl N-[(2,3-dipyridin-2-ylquinoxalin-6-yl)carbonyl]-L-tryptophanate
-
IC50 above 0.1 mM
0.026
-
methyl N-[(2,3-ditetrahydrofuran-2-ylquinoxalin-6-yl)carbonyl]-6-hydroxy-L-tryptophanate
-
-
0.1
-
methyl N-[(2,3-ditetrahydrofuran-2-ylquinoxalin-6-yl)carbonyl]-L-tryptophanate
-
IC50 above 0.1 mM
0.1
-
methyl N-[[2,3-bis(3-methoxyphenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophanate
-
IC50 above 0.1 mM
0.1
-
methyl N-[[2,3-bis(3-methoxyphenyl)quinoxalin-6-yl]carbonyl]-L-tryptophanate
-
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
-
-
0.0055
-
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophanate
-
-
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
-
-
0.1
-
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-(2-methoxy-2-oxoethoxy)-L-tryptophanate
-
-
0.0055
-
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophanate
-
-
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
-
-
0.1
-
methyl N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophanate
-
IC50 above 0.1 mM
0.049
-
methyl N-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophanate
-
-
0.049
-
methyl N-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophanate
-
-
0.1
-
methyl N-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-L-tryptophanate
-
IC50 above 0.1 mM
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
-
-
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
-
-
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
-
-
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
-
-
0.000046
-
N-[(13-cyclohexyl-6,7-dihydroindolo[1,2-d][1,4]benzoxazepin-10-yl)carbonyl]-2-methylalanine
-
-
0.016
-
N-[(2,3-difuran-2-ylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophan
-
-
0.033
-
N-[(2,3-difuran-2-ylquinoxalin-6-yl)carbonyl]-L-tryptophan
-
-
0.01
-
N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophan
-
-
0.011
-
N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-6-hydroxy-L-tryptophan
-
-
0.015
-
N-[(2,3-diphenylquinoxalin-6-yl)carbonyl]-L-tryptophan
-
-
0.1
-
N-[(2,3-dipyridin-2-ylquinoxalin-6-yl)carbonyl]-L-tryptophan
-
IC50 above 0.1 mM
0.016
-
N-[(2,3-ditetrahydrofuran-2-ylquinoxalin-6-yl)carbonyl]-6-hydroxy-L-tryptophan
-
-
0.033
-
N-[(2,3-ditetrahydrofuran-2-ylquinoxalin-6-yl)carbonyl]-L-tryptophan
-
-
0.0017
-
N-[(2,4-dichlorophenyl)carbonyl]-N-[3-(trifluoromethyl)benzyl]-L-phenylalanine
-
-
0.005
-
N-[(2-cyclohexyl-3-phenylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophan
-
-
0.0037
-
N-[(2-cyclohexyl-3-phenylquinoxalin-6-yl)carbonyl]-L-tryptophan
-
-
0.0006
-
N-[(3-cyclohexyl-2-phenylquinoxalin-6-yl)carbonyl]-5-hydroxy-L-tryptophan
-
-
0.0018
-
N-[(3-cyclohexyl-2-phenylquinoxalin-6-yl)carbonyl]-L-tryptophan
-
-
0.0002
-
N-[(5Z)-5-((5-[2-chloro-5-(trifluoromethyl)phenyl]-2-furyl)methylene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]benzenesulfonamide
-
-
0.00028
-
N-[(5Z)-5-(3,4-dichlorobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]benzenesulfonamide
-
-
0.00044
-
N-[(5Z)-5-(4-bromobenzylidene)-4-oxo-2-thioxo-1,3-thiazolidin-3-yl]benzenesulfonamide
-
-
0.0027
-
N-[(Z)-2-[4-(2-bromophenoxy)phenyl]-1-[(2-hydroxyethyl)carbamoyl]ethenyl]benzamide
-
-
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
P26663
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
-
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
P26663
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
P26663
-
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
P26663
-
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
-
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
-
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
-
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
-
-
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
-
polymerase from 1 b genotype
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
-
-
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
-
-
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
-
-
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
-
-
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
-
-
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
-
-
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
-
-
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
P26663
-
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
P26663
-
0.015
-
N-[[2,3-bis(3-methoxyphenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophan
-
-
0.1
-
N-[[2,3-bis(3-methoxyphenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
-
IC50 above 0.1 mM
0.0017
-
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-(carboxymethoxy)-L-tryptophan
-
-
0.0013
-
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophan
-
-
0.0022
-
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-[[(2E)-3-carboxyprop-2-en-1-yl]oxy]-L-tryptophan
-
-
0.0017
-
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-(carboxymethoxy)-L-tryptophan
-
-
0.0013
-
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophan
-
-
0.0022
-
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-6-[[(2E)-3-carboxyprop-2-en-1-yl]oxy]-L-tryptophan
-
-
0.0019
-
N-[[2,3-bis(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
-
-
0.0061
-
N-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophan
-
-
0.0061
-
N-[[2,3-bis(4-methylphenyl)quinoxalin-6-yl]carbonyl]-6-hydroxy-L-tryptophan
-
-
0.0041
-
N-[[2-cyclohexyl-3-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophan
-
-
0.0034
-
N-[[2-cyclohexyl-3-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
-
-
0.0046
-
N-[[3-cyclohexyl-2-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-5-hydroxy-L-tryptophan
-
-
0.0016
-
N-[[3-cyclohexyl-2-(4-fluorophenyl)quinoxalin-6-yl]carbonyl]-L-tryptophan
-
-
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
-
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
-
polymerase from 1 a genotype
0.01
-
pyrogallol
-
-
0.0000246
-
suramin
-
wild-type, pH 7.5, 30C
0.00007
-
suramin
-
wild-type, pH 7.5, 30C
0.00014
-
suramin
-
mutant Y41A, pH 7.5, 30C
0.0002
-
suramin
-
mutant Y41A, pH 7.5, 30C
0.0023
-
UTP
Human rhinovirus 16
-
IC50: 0.0023 mM
0.0006
-
Zn2+
Human rhinovirus 16
-
IC50: 0.0006 mM, suppression of inhibition by dithiothreitol
0.00033
-
[(1R)-5-cyano-8-methyl-1-propyl-1,3,4,9-tetrahydropyrano[3,4-b]indol-1-yl]acetic acid
-
-
0.003
-
[(1R)-8-chloro-5-ethyl-1-propyl-1,3,4,9-tetrahydropyrano[3,4-b]indol-1-yl]acetic acid
-
-
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
-
-
0.09
-
[(2Z)-2-(3,4,5-trihydroxybenzylidene)hydrazino]acetic acid
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00000016
-
-
-
0.000000188
-
-
-
0.000000289
-
-
-
0.00035
-
-
-
0.00088
-
-
reaction with CMV RNA
0.0015
-
-
reaction with poly(C)
0.00196
-
Human rhinovirus 2
-
-
0.0057
-
-
-
0.012
-
-
activity with CMV RNA
0.025
-
-
truncated enzyme form NS5B(DELTA21)
0.13
-
-
activity with poly(C)
additional information
-
-
-
additional information
-
B6EAV7
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
-
-
activities of wild-type and deletion and point mutation mutant enzymes on HP1 RNA substrate, overview
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
-
-
assay at
7
8.5
-
wild-type enzyme, broad optimum
7.3
-
Human rhinovirus 16
-
poly(A) as template and biotinylated oligo(dU)15 as the primer
7.5
-
-
assay at
7.6
-
Human rhinovirus 2
-
-
8
-
-
in Hepes-NaOH buffer or Tris hydrochloride buffer
8
-
-
recombinant viral enzyme purified from insect cells
8
-
Q0G9P7
assay at
8
-
P03433
assay at
8
-
P31343
assay at
8.9
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
Human rhinovirus 16
-
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
Human rhinovirus 2
-
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
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
recombinant viral enzyme purified from insect cells
28
-
-
assay at
30
-
Human rhinovirus 16
-
poly(A) as template and biotinylated oligo(dU)15 as the primer
30
-
-
-
30
-
Q0G9P7
assay at
30
-
-
assay at
32
-
-
assay at
37
-
P31343
assay at
37
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
42
-
28.7% at 4C and 13.4% at 42C of the activity at 25C, no activity at 0C
17
37
Human rhinovirus 16
-
17C: about 20% of maximal activity, dramatic drecrease in activity between 32C and 37C, 37C: no activity, poly(A) as template and biotinylated oligo(dU)15 as the primer
18
37
-
18C: about 50% of maximal activity, 37C: about 50% of maximal activity
22
37
-
when the assay temperature is increased from 22C to 37C the turnover number is significantly increased
25
40
-
25C: about 55% of maximal activty, 40C: about 20% of maximal activity
27
37
-
27C: about 50% of maximal activity, 37C: optimum
30
45
-
30C: optimum, 45C: 50-80% of maximal activity
35
-
-
sharp decrease in activity above
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8.06
-
B3SND7, -
calculated from sequence of cDNA
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
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
Manually annotated by BRENDA team
-
CD4+ human T cells containing an integrated HTLV-1 genome
Manually annotated by BRENDA team
-
expression is specifically localized in phloem cell layers in roots
Manually annotated by BRENDA team
Caenorhabditis elegans Bristol N2
-
-
-
Manually annotated by BRENDA team
-
mock-infected
Manually annotated by BRENDA team
additional information
-
leaf of Zea mays infected with Maize dwarf mosaic virus
Manually annotated by BRENDA team
additional information
-
cells of Drosophila melanogaster infected with Black beetle virus
Manually annotated by BRENDA team
additional information
La France isometric virus
-
tissue of Agaricus bisporus
Manually annotated by BRENDA team
additional information
-
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
Manually annotated by BRENDA team
additional information
-
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
Manually annotated by BRENDA team
additional information
-
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
Manually annotated by BRENDA team
additional information
-
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
Manually annotated by BRENDA team
additional information
-
RdRp activity is associated with heavy cytoplasmic membrane fractions in the host cell
Manually annotated by BRENDA team
additional information
P06935
RdRp activity is associated with heavy cytoplasmic membrane fractions in the host cell
Manually annotated by BRENDA team
additional information
-
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
Manually annotated by BRENDA team
additional information
Dengue virus DENV
-
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
-
Manually annotated by BRENDA team
additional information
Japanese encephalitis virus JEV, St. Louis encephalitis virus SLEV
-
RdRp activity is associated with heavy cytoplasmic membrane fractions in the host cell
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
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
Manually annotated by BRENDA team
-
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
-
Manually annotated by BRENDA team
-
3AB is a membrane-binding protein responsible for the localization of the polymerase to the membranous vesicles at which replication occurs
Manually annotated by BRENDA team
-
the enzyme is associated with the cores of the virus
Manually annotated by BRENDA team
additional information
-
the enzyme is closely associated with the smooth membranes of infected BHK-21 cells
-
Manually annotated by BRENDA team
additional information
-
cellular membrane of brome mosaic virus infected Hordeum vulgare
-
Manually annotated by BRENDA team
additional information
Foxtail mosaic potexvirus
-
membrane fraction of Chenopodium guinoa infected with foxtail mosaic potexvirus
-
Manually annotated by BRENDA team
additional information
-
membranes of infected mouse cells
-
Manually annotated by BRENDA team
additional information
Human rhinovirus 2
-
enzyme is localized in the soluble phase of infected Hela cells
-
Manually annotated by BRENDA team
additional information
-
the enzyme is associated with particulate fraction of Zea mays leaf infected with Maize dwarf mosaic virus
-
Manually annotated by BRENDA team
additional information
-
in soluble and particulate fractions of extract of Cucumis sativus infected with Cucumber mosaic virus
-
Manually annotated by BRENDA team
additional information
-
particulate material of cells of Drosophila melanogaster infected with Black beetle virus
-
Manually annotated by BRENDA team
additional information
-
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
-
Manually annotated by BRENDA team
additional information
-
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
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Avian infectious bursal disease virus
Avian infectious bursal disease virus
Avian infectious bursal disease virus
Avian infectious bursal disease virus
Avian infectious bursal disease virus
Bluetongue virus 10 (isolate USA)
Bovine viral diarrhea virus (strain CP7)
Crimean-Congo hemorrhagic fever virus (strain Nigeria/IbAr10200/1970)
Crimean-Congo hemorrhagic fever virus (strain Nigeria/IbAr10200/1970)
Crimean-Congo hemorrhagic fever virus (strain Nigeria/IbAr10200/1970)
Escherichia coli (strain K12)