Information on EC 2.7.7.49 - RNA-directed DNA polymerase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY
2.7.7.49
-
RECOMMENDED NAME
GeneOntology No.
RNA-directed DNA polymerase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
deoxynucleoside triphosphate + DNAn = diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
nucleotidyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
deoxynucleoside-triphosphate:DNA deoxynucleotidyltransferase (RNA-directed)
Catalyses RNA-template-directed extension of the 3'- end of a DNA strand by one deoxynucleotide at a time. Cannot initiate a chain de novo. Requires an RNA or DNA primer. DNA can also serve as template. See also EC 2.7.7.7 DNA-directed DNA polymerase.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
CS5 pol
-
chimeric DNA polymerase, termed CS5 pol, constructed from T. Z05 pol and Tma pol
CS5 pol
Thermus sp. Z05
-
chimeric DNA polymerase, termed CS5 pol, constructed from T. Z05 pol and Tma pol
-
DNA nucleotidyltransferase (RNA-directed)
-
-
-
-
DNA polymerase
-
-
DNA polymerase I
-
-
DNA polymerase I
-
-
-
DNA polymerase I
-
-
FV Pol
prototype foamy virus, Simian foamy virus
-
-
FV reverse transcriptase
-
-
Gag-Pol
-
reverse transcriptase precursor
HIV reverse transcriptase
-
-
HIV-1 reverse transcriptase
AF324493, Q8Q2U5, Q8Q2V9
-
HIV-1 reverse transcriptase
Human immunodeficiency virus 1 BG05
Q8Q2U5
-
-
HIV-1 reverse transcriptase
Human immunodeficiency virus 1 M01
Q8Q2V9
-
-
HIV-1 RT
AF324493, Q8Q2U5, Q8Q2V9
-
HIV-1 RT
Human immunodeficiency virus 1 BG05
Q8Q2U5
-
-
HIV-1 RT
Human immunodeficiency virus 1 M01
Q8Q2V9
-
-
HIV-reverse transcriptase
-
-
human hepatitis B virus polymerase
-
-
human immunodeficiency virus type 1 reverse transcriptase
-
-
iScript enzyme
-
commercial name
K4 polymerase
-
-
K4 polymerase
Thermotoga petrophila K4
-
-
-
K4PolI
Thermotoga petrophila K4
-
-
-
M-MuLV reverse transcriptase
-
-
Moloney Murine leukemia virus reverse transcriptase
-
-
Moloney murine leukemia virus RT
-
-
MX162-RT
-
-
-
-
MX65-RT
-
-
-
-
nucleoside reverse transcriptase
-
-
nucleotidyltransferase, deoxyribonucleate, RNA-dependent
-
-
-
-
P72
-
-
-
-
PFV RT
prototype foamy virus
-
-
polymerase/reverse transcriptase
-
-
prototype foamy virus reverse transcriptase
prototype foamy virus
-
-
R2-RT
-
-
reverse transcriptase
-
-
-
-
reverse transcriptase
-
-
reverse transcriptase
-
multifunctional enzyme but mainly used as RNA-directed DNA polymerase
reverse transcriptase
-
-
reverse transcriptase
-
-
reverse transcriptase
-
-
reverse transcriptase
-
-
reverse transcriptase
-
-
reverse transcriptase
-
-
reverse transcriptase
-
-
reverse transcriptase
-
exhibits DNA polymerase activity and RNase H activity
reverse transcriptase
-
reverse transcriptase is synthesized as part of the Gag-Pol precursor protein, which is cleaved by the virally encoded protease into the structural proteins and the replication enzymes reverse transcriptase, protease, and integrase
reverse transcriptase
O12158
-
reverse transcriptase
-
-
reverse transcriptase
-
reverse transcriptases of retroviruses have two enzymatic activities, a DNA polymerase (that copies both RNA and DNA templates) and the ribonuclease H activity that hydrolyzes the RNA in DNA-RNA hybrids, the ribonuclease H level of HIV-2 RT is lower than that of HIV-1 reverse transcriptase, while the DNA polymerase of both reverse transcriptases is similar
reverse transcriptase
-
multifunctional enzyme but mainly used as RNA-directed DNA polymerase
reverse transcriptase
-
-
reverse transcriptase
-
-
reverse transcriptase
-
-
reverse transcriptase
-
-
reverse transcriptase
-
-
reverse transcriptase
Simian immunodeficiency virus mneCl8
-
-
-
reverse transcriptase
-
-
reverse transcriptase
-
-
reverse transcriptase
-
-
reverse transcriptase
Thermotoga petrophila K4
-
-
-
reverse transcriptase
-
-
reverse transcriptase/RNA dependent DNA polymerase
-
-
reverse-transcriptase
-
-
revertase
-
-
-
-
RNA dependent DNA polymerase
-
-
RNA revertase
-
-
-
-
RNA-dependent DNA polymerase
-
-
-
-
RNA-dependent DNA polymerase
-
-
RNA-dependent DNA polymerase
-
-
-
RNA-instructed DNA polymerase
-
-
-
-
RT
-
-
-
-
simian foamy virus reverse transcriptase
-
-
SuperScript I reverse transcriptase
-
commercial preparation
Superscript II
-
commercial preparation
SUPERSCRIPT II reverse transcriptase
-
-
SUPERSCRIPT II reverse transcriptase
-
commercial preparation
T. Z05 pol
Thermus sp. Z05
-
-
-
telomerase
-
telomerase is composed of three essential components: the telomerase reverse transcriptase, the telomerase RNA component, and the TERC-binding protein dyskerin
telomerase
-
telomerase lengthens telomeres by its reverse transcriptase activity
telomerase
-
telomeres are synthesized and maintained by telomerase, a heterodimeric enzyme with an RNA template subunit (TERC) and a catalytic protein component (TERT)
telomerase
-
-
telomerase
-
-
telomerase catalytic subunit
-
-
-
-
telomerase reverse transcriptase
-
-
-
-
telomerase reverse transcriptase
Q6A548
-
telomerase reverse transcriptase
-
catalytic subunit of telomerase
telomerase reverse transcriptase
-
-
telomerase reverse transcriptase
-
-
telomerase reverse transcriptase
-
-
TERT
Q6A548
catalytic subunit of telomerase
TERT
-
catalytic protein component of telomerase
TERT
-
catalytic subunit of telomerase
xenotropic murine leukemia virus-related virus reverse transcriptase
Xenotropic MLV-related virus
A1Z651
-
XMRV RT
Xenotropic MLV-related virus
A1Z651
-
additional information
-
DNA polymerase with reverse-transcriptase activity
additional information
Caldibacillus cellulovorans CompA.2
-
DNA polymerase with reverse-transcriptase activity
-
additional information
-
DNA polymerase (PolA) and topoisomerase I (TopA) proteins exhinit highly efficient reverse transcriptase activity in addition to their predicted functions
additional information
Streptomyces coelicolor M145
-
DNA polymerase (PolA) and topoisomerase I (TopA) proteins exhinit highly efficient reverse transcriptase activity in addition to their predicted functions
-
CAS REGISTRY NUMBER
COMMENTARY
9068-38-6
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
wild-type and 3'-azido-3'-deoxythymidine resistant strain D67N/K70R/T215Y/K219Q
-
-
Manually annotated by BRENDA team
Avian myeloblastosis virus AMV
AMV
-
-
Manually annotated by BRENDA team
Avian myeloblastosis virus BAI
BAI strain
-
-
Manually annotated by BRENDA team
B77 strain grown in duck embryo fibroblasts
-
-
Manually annotated by BRENDA team
strain EA1
SwissProt
Manually annotated by BRENDA team
Bacillus caldolyticus EA1
EA1
-
-
Manually annotated by BRENDA team
Bacillus caldolyticus EA1
strain EA1
SwissProt
Manually annotated by BRENDA team
Caldibacillus cellulovorans CompA.2
CompA.2
-
-
Manually annotated by BRENDA team
Chicken syncytial virus
-
-
-
Manually annotated by BRENDA team
encoded by retrotransposon 1731
-
-
Manually annotated by BRENDA team
isolated from liver of ducks
-
-
Manually annotated by BRENDA team
encoded by group II intron-type open reading frame
-
-
Manually annotated by BRENDA team
Hamster leukemia virus
-
-
-
Manually annotated by BRENDA team
Hamster leukemia virus
HaLV
-
-
Manually annotated by BRENDA team
Hamster leukemia virus HaLV
HaLV
-
-
Manually annotated by BRENDA team
DNA polymerase Pol gamma also catalyzes reverse transcription with a slightly higher efficiency than HIV-1 reverse transcriptase
-
-
Manually annotated by BRENDA team
human LINE-1 ORF2, which encodes reverse transcriptase, is inserted into a baculovirus shuttle vector and expressed in SF21 cells
-
-
Manually annotated by BRENDA team
HTLV-III
-
-
-
Manually annotated by BRENDA team
Escherichia coli BL21 transfected with pET 21a(+)/HIV-1 PR-RT
-
-
Manually annotated by BRENDA team
group O and M virus, Group O infection is restricted to Cameroon and neighboring countries in West Central Africa, while Group M infection is spread all over the world
-
-
Manually annotated by BRENDA team
subtype B
AF324493
GenBank
Manually annotated by BRENDA team
Human immunodeficiency virus 1 BG05
subtype C
UniProt
Manually annotated by BRENDA team
Human immunodeficiency virus 1 M01
subtype C
UniProt
Manually annotated by BRENDA team
Human T-cell lymphotropic virus/lymphadenopathy-associated virus
-
-
-
Manually annotated by BRENDA team
Lymphadenopathy associated virus
human T-lymphocytes infected with
-
-
Manually annotated by BRENDA team
BR6 milk-transmitted strain
-
-
Manually annotated by BRENDA team
mouse mammary tumor virus BR6
BR6 milk-transmitted strain
-
-
Manually annotated by BRENDA team
Japanese medaka
-
-
Manually annotated by BRENDA team
prototype foamy virus
gene pol
-
-
Manually annotated by BRENDA team
strain PAO1
-
-
Manually annotated by BRENDA team
Reticuloendotheliosis virus T
strain T
-
-
Manually annotated by BRENDA team
long terminal repeat-containing retrotransposon Ty3
-
-
Manually annotated by BRENDA team
mutant version of reverse trancriptase from retrotransposon Ty1, in which one of the three active site aspartates is changed to asparagine, D211N
-
-
Manually annotated by BRENDA team
LTR retrotransposon of Schizosaccharomyces pombe, Tf1
-
-
Manually annotated by BRENDA team
gene pol
-
-
Manually annotated by BRENDA team
TYO-7, isolated from an African monkey
-
-
Manually annotated by BRENDA team
Simian immunodeficiency virus mneCl8
strain mneCl8
-
-
Manually annotated by BRENDA team
strain NEM316
-
-
Manually annotated by BRENDA team
Thermotoga petrophila K4
-
-
-
Manually annotated by BRENDA team
strain Z05
-
-
Manually annotated by BRENDA team
Thermus sp. Z05
strain Z05
-
-
Manually annotated by BRENDA team
Xenotropic MLV-related virus
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
-
the enzyme belongs to the family B polymerases
evolution
-
K4PolI is a family A DNA polymerase, phylogenetic tree
evolution
Thermotoga petrophila K4
-
K4PolI is a family A DNA polymerase, phylogenetic tree
-
malfunction
-
Thg1p is required for tRNAHis guanylylation in vivo, because cells depleted of Thg1p lack G(-1) in their tRNAHis
malfunction
-
depletion of Saccharomyces cerevisiae tRNA(His) guanylyltransferase Thg1p leads to uncharged tRNAHis with additional m(5)C
malfunction
-
the normally lethal phenotype of thg1-DELTA strains is bypassed by overexpression of both histidyl-tRNA synthetase and tRNAHis. This result demonstrates that, despite its widespread conservation, the G(-1) residue of tRNAHis is not essential in vivo. The only essential Thg1 function is its G(-1) addition activity
malfunction
-
mutations in a loop in the fingers domain leads to a decrease accuracy of the arhcaeal enzyme
malfunction
-
kinetics of mismatch incorporation, overview
physiological function
-
the yeast tRNAHis guanylyltransferase (Thg1) is an essential enzyme in yeast. Thg1 adds a single guanine residue to the 5' end of tRNAHis, which serves as a crucial determinant for aminoacylation of tRNAHis
physiological function
-
Thg1p interacts with the origin recognition complex and is required for the G2/M phase transition
physiological function
-
all tRNAHis possess an essential extra G1 guanosine residue at their 5' end. This extra guanylate residue can be generated via two different processes. In Escherichia coli and in chloroplasts, the G1 is genome-encoded and retained during tRNA maturation because of an unusual cleavage of the pre-tRNAHis at the (-1) position by RNase P. In Saccharomyces cerevisiae as well as in Drosophila melanogaster the G1 is not genome-encoded and must be post-transcriptionally added at the 5' terminus of the nuclear-encoded tRNAHis by a specific tRNAHis guanylyltransferase. In plant mitochondria, although trnH genes possess a G1 tRNAHis guanylyltransferase activity is present in plant mitochondria
physiological function
-
HIV-1 reverse transcriptase has two associated activities, DNA polymerase and RNase H, both essential for viral replication
physiological function
-
HIV-1 reverse transcriptase plays an essential role in the life cycle of the virus
physiological function
-
hepatitis B virus polymerase plays a critical role during HBV life cycle, and polymerase/reverse transcriptase activities are critical for HBV-pol during viral replication
physiological function
-
reverse transcriptase is the enzyme that catalyzes DNA polymerization using RNA as a template, i.e. RNA-dependent DNA polymerase
physiological function
-
during viral replication, HIV-1 reverse transcriptase plays a pivotal role in converting genomic RNA into proviral DNA
physiological function
Thermotoga petrophila K4
-
reverse transcriptase is the enzyme that catalyzes DNA polymerization using RNA as a template, i.e. RNA-dependent DNA polymerase
-
malfunction
Xenotropic MLV-related virus
A1Z651
kinetics of mismatch incorporation, overview
additional information
-
the purified recombinant reverse transcriptase domain is a stable protein and shows a low selective polymerase activity, substrate binding by computational molecular modeling, overview
additional information
-
in family B polymerases, the fingers domain interacts with dNTPs and undergoes a catalytically essential conformational change that depends on correct pairing of the dNTP with its templating base
additional information
-
the BIV reverse transcriptase is not stringent in the reaction parameters for clamp activity, such as the minimal complementarity length between the primer and functional template termini that sustains stable clamps, the effects of gaps between the two template strands on the clamp activity of the tested RTs, the effects of template end phosphorylations on the RT-associated clamp activities, and clamp activity with a long hairpin double-stranded primer comprising both the primer and the complementary non-functional template strands, overview. BIV is active with a single-nucleotide clamp substrate although its activity is substantially lower relative to the two-nucleotide clamp. The enzyme from BIV is able to stabilize even a single-nucleotide complementarity between the duplexed P/T2
additional information
-
the HIV-1 reverse transcriptase is stringent in the reaction parameters for clamp activity, such as the minimal complementarity length between the primer and functional template termini that sustains stable clamps, the effects of gaps between the two template strands on the clamp activity of the tested RTs, the effects of template end phosphorylations on the RT-associated clamp activities, and clamp activity with a long hairpin double-stranded primer comprising both the primer and the complementary non-functional template strands, overview. HIV-1 RT loses all apparent activity when tested with a single-nucleotide clamp substrate. The enzyme from HIV is not able to stabilize a single-nucleotide complementarity between the duplexed P/T2
additional information
-
the MLV reverse transcriptase is stringent in the reaction parameters for clamp activity, such as the minimal complementarity length between the primer and functional template termini that sustains stable clamps, the effects of gaps between the two template strands on the clamp activity of the tested RTs, the effects of template end phosphorylations on the RT-associated clamp activities, and clamp activity with a long hairpin double-stranded primer comprising both the primer and the complementary non-functional template strands, overview. MLV RT loses all apparent activity when tested with s single-nucleotide clamp substrate. The enzyme from MIV is not able to stabilize a single-nucleotide complementarity between the duplexed P/T2
additional information
-
structure modeling of K4 polymerase, overview
additional information
-
while the biologically relevant form of RT is the p66-p51 heterodimer, two recombinant homodimer forms of RT, p66-p66 and p51-p51, are also catalytically active. The apparent binding affinity of p51-p51 for its DNA substrate is to a great extent time-dependent when compared to that of p66-p66 and p66-p51, and is more likely determined by the dimer dissociation into its constituent monomers rather than the intrinsic binding affinity of dimeric enzyme
additional information
-
specifically the active site aspartates in motifs A and C, D150, D224, D225 in MoMLV RT, are conserved in the RT
additional information
Xenotropic MLV-related virus
A1Z651
the enzyme is less efficient in DNA synthesis and in unblocking chain-terminated primers but has higher fidelity. Specifically the active site aspartates in motifs A and C, D150, D224, D225 in XMRV RT are conserved in the RT, molecular model of XMRV RT, overview
additional information
AF324493, Q8Q2U5, Q8Q2V9
although p51 provides RT with essential structural and conformational stability, p66 is the catalytically active subunit and includes the N-terminal polymerase domain (residues 1-321) and C-terminal RNase H domain (residues 441-560), linked by a connection domain; although p51 provides RT with essential structural and conformational stability, p66 is the catalytically active subunit and includes the N-terminal polymerase domain (residues 1-321) and C-terminal RNase H domain (residues 441-560), linked by a connection domain; although p51 provides RT with essential structural and conformational stability, p66 is the catalytically active subunit and includes the N-terminal polymerase domain (residues 1-321) and C-terminal RNase H domain (residues 441-560), linked by a connection domain
additional information
-
active site structure, and structures of open, transition, and closed conformations along the enzyme reaction and specificity, molecular modeling, calculation, and molecular dynamics simulations, modeling of the p66 subunit of HIV-reverse transcriptase enzyme shown in open and closed conformations, overview
additional information
Human immunodeficiency virus 1 BG05, Human immunodeficiency virus 1 M01
-
although p51 provides RT with essential structural and conformational stability, p66 is the catalytically active subunit and includes the N-terminal polymerase domain (residues 1-321) and C-terminal RNase H domain (residues 441-560), linked by a connection domain
-
additional information
Thermotoga petrophila K4
-
structure modeling of K4 polymerase, overview
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
((1s,3s)-3-(7-amino-2H-2,3,5,6-tetraazabenzo[cd]azulen-2-yl)cyclobutyl)methyl tetrahydrogen triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
(-)-beta-2',3'-dideoxy-3'-thiacytidine triphosphate + DNAn
diphosphate + ?
show the reaction diagram
-
-
-
-
?
2',3'-dideoxy-CTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
2'-deoxyadenosine 5'-triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
2'-deoxycytosine 5'-triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
2'-deoxyguanosine 5'-triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
2'-deoxyribonucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
enzyme mutant N483Q/S486Q/T539N/Y545Q/D547T/P548Q/A570Q/D578Q/A597T/W604R/S612N/V730L/R736Q/S739N/M747R
-
-
?
2'-deoxythymidine 5'-triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
2'-fluoro-N-cyclobutyladenosine triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
3'-azido-2',3'-dideoxy-2,6-diaminopurine triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
incorporation activity of the enzyme with the enzyme inhibitor as A analogue or G analogue
-
-
?
3'-azido-2',3'-dideoxy-2-amino-6-chloropurine triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
incorporation activity of the enzyme with the enzyme inhibitor as A analogue or G analogue
-
-
?
3'-azido-2',3'-dideoxy-2-amino-6-methoxypurine triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
incorporation activity of the enzyme with the enzyme inhibitor as A analogue or G analogue
-
-
?
3'-azido-2',3'-dideoxy-2-amino-6-N-allylaminopurine triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
incorporation activity of the enzyme with the enzyme inhibitor as A analogue or G analogue
-
-
?
3'-azido-2',3'-dideoxyadenosine triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
incorporation activity of the enzyme with the enzyme inhibitor as A analogue or G analogue
-
-
?
dATP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
dATP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
enzyme mutant N483Q/S486Q/T539N/Y545Q/D547T/P548Q/A570Q/D578Q/A597T/W604R/S612N/V730L/R736Q/S739N/M747R
-
-
?
dATP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
RNA-dependent DNA synthesis
-
-
?
dCTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
-
dCTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
dCTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
enzyme mutant N483Q/S486Q/T539N/Y545Q/D547T/P548Q/A570Q/D578Q/A597T/W604R/S612N/V730L/R736Q/S739N/M747R
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
-
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Hamster leukemia virus
-
-
-
-
-
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Hamster leukemia virus
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Human T-cell lymphotropic virus/lymphadenopathy-associated virus
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Lymphadenopathy associated virus
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Q6A548
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
O12158
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
prototype foamy virus
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
AF324493, Q8Q2U5, Q8Q2V9
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Xenotropic MLV-related virus
A1Z651
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
DNA synthesis of the recombinant enzyme is higher on poly(rA)*oligo(dT)12 than on poly(rC)*oligo(dG). The activity on poly[d(A-T)] is noticeably lower than that on poly(rA)*oligo(dT)12
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
DNA polymerase Pol gamma also catalyzes reverse transcription with a slightly higher efficiency than HIV-1 reverse transcriptase
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
HTLV-III
-
the enzyme transcribs (rA)n*(dT)12, (rAm)n*(dT)12, (rC)n*(dG)12 and (rCm)n*(dG)12. The enzyme catalyzes transcription of the 70S RNA from SSAV. (RC)n*(dG)12-dependent activity is several fold higher than that catalyzed by (rA)n*(dT)12 and is strictly Mg2+-dependent
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
the enzyme synthesizes full-length cDNA copies of in vitro transcripts beginning at the 3'-end and has a preference for transcripts having the 3'tRNA-like structure. The enzyme begins cDNA synthesis directly opposite the 3'-terminal nucleotide of the template RNA. The activity with poly(rC) alone is about 5% of that with poly(rC)*oligo(dG), efficient use of the substrate is dependent on the primer
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
P03366
with RNA-directed DNA synthesis, the rate-limiting step occurs after the phosphodiester bond formation while with DNA template it occurs at the dNTP binding step
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
efficiency of natural and synthetic templates
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
the enzyme shows both RNA-dependent and DNA-dependent DNA synthesis activity and an associated RNAse H activity
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
the enzyme accepts a variety of natural RNA templates, but shows a preference for oncogenic virus RNA. RNA from other oncogenic viruses is as efficient as AMV RNA. Homopolymeric duplexes are exceptionally good templates, stimulating synthesis 100fold greater than natural RNA or DNA. The enzyme requires a primer
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
the enzyme exhibits both synthetic and degradative activity, DNA polymerase and RNAse H
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
RNA-dependent and DNA-dependent DNA polymerase activity. The p66/p51 heterodimer can perform strand displacement DNA synthesis of approximately 300 bases. The homodimer p66 alone can carry out limited strand displacement DNA synthesis, but this activity is stimulated by the p51 subunit at a molar ratio of one molecule of p55 to five molecules of p51. The homodimer p51 itself is unable to fill a small gap of 26 nucleotides in a double-stranded DNA substrate and is not active by itself in strand displacement DNA synthesis
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
affinity of the enzyme for (U)n and a series of (U)n analogs
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
the polymerase requires a primer strand with free 3'-hydroxyl group and a template strand to direct DNA synthesis
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
the enzyme prefers the template-primer poly(rA)*oligo(dT) over poly(rC)*oligo(dG). With poly(rCm)*oligo(dG) only marginal activity is detected, and no activity is measured with poly(dA)*oligo(dT)
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
enzyme requires a 3'-OH group on a primer and carrying out synthesis from the 5' to the 3' end of the molecule, that is by addition of nucleoside monophosphates at the 3'-OH end of the primer. Poly(rA) is almost totally inactive as a template until a primer, either poly(dT) or oligo(dT) is added
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
all four deoxyribonucleotide triphosphates are required for full activity, some activity is present when only three deoxyribonucleotide triphosphates are added and 10-20% of full activity is still present with only two deoxyribonucleotide triphosphates
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
the purified enzyme can synthesize DNA using RNA as a template and a synthetic oligodeoxynucleotide as a primer: cDNA can be synthesized using the Escherichi coli 5S RNA as template and a 15-base synthetic oligonucleotide complementary to the 3'-end of the 5S RNA as a primer. The enzyme can also produce a full-length cDNA using a 50-base synthetic DNA as a template and a synthetic oligonucleotide complementary to the 3'-end of the template as a primer
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
the alpha enzyme form is more active in the single-strand cDNA-directed synthesis of double-stranded cDNA-directed synthesis of double-stranded DNA than the other 2 enzyme forms
-
-
-
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
the alpha enzyme form is more active in the single-strand cDNA-directed synthesis of double-stranded cDNA-directed synthesis of double-stranded DNA than the other 2 enzyme forms
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
the enzyme appears to be required very early after infection to synthesize proviral DNA
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
the enzyme might play a role in normal differentiation
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
enzyme plays a central role during the life cycle of a retrovirus. Temperature-sensitive mutants with a lesion in the reverse transcriptase are unable to establish infections
-
-
-
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
DNA polymerase Pol gamma also catalyzes reverse transcription with a slightly higher efficiency than HIV-1 reverse transcriptase. RNA-primed DNA synthesis activity is required for initiation of mtDNA replication. Poly gamma holoenzyme is capable of performing this reaction at a physiologically releavant rate
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
the enzyme plays a central role in transposition of retroelements
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
bis-(2'-deoxynucleoside)5,5'-tetraphosphates and bis-(2'-deoxynucleoside)5',5'-triphosphates are effective substrates for DNA elongation
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
DNA polymerase (PolA) and topoisomerase I (TopA) proteins exhibit highly efficient reverse transcriptase activity in addition to their predicted functions
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
DNA polymerase shows significant reverse-transcriptase activity in presence of Mg2+
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
due to its low dNTP binding affinity, the dNTP binding step becomes rate-limiting in the multiple rounds of the dNTP incorporation by MuLV RT. The active site of MuLV RT has an intrinsically low dNTP binding affinity, compared with HIV-1 RT. In addition, instead of the misinsertion step, the mismatch extension step, which varies between MuLV and HIV-1 RTs, contributes to their fidelity differences
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
mechenism
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
P04585
poly(rA)noligo(dT)12-18
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
A2TD24, -
poly(rC)*p(dG)(12-18)
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
R2-RT is capable of efficiently utilizing single-stranded DNA (ssDNA) as a template. The processivity of the enzyme on ssDNA templates is higher than its processivity on RNA templates. This finding suggests that R2-RT is also capable of synthesizing the second DNA strand during retrotransposition
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
reverse transcriptase has RNA-dependent and DNA-dependent DNA polymerase activity
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
telomerase is the cellular RNA-dependent DNA polymerase that uses an integral RNA template to synthesize telomeric DNA repeats at the ends of linear chromosomes. Dimerization as a functionally conserved feature of the RNA templates utilized by reverse transcriptases
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
P03355
wild-type Moloney murine leukemia virus reverse transcriptase selectively uses deoxyribonucleotides over ribonucleotides as substrates
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
RNA-dependent DNA synthesis
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
Ext-T DNA 23-mer primer annealed to the RNA 40-mer template
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Simian foamy virus, prototype foamy virus
-
heteropolymeric single stranded M13 substrate
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
poly(dA)/oligo(dT)12-18 and poly(rA)/oligo(dT)12-18 as template-primers
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
RNA-dependent DNA polymerase activity by enzyme mutants T326A, L329A, Q384A, F388A, M408A, Y438A, L329A/Q384A, L329A/Y438A, and Q384A/Y438A, not by the wild-type enzyme
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
Td26/50-Cy3-Pd18b
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Xenotropic MLV-related virus
A1Z651
Td26/50-Cy3-Pd18b
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Avian myeloblastosis virus AMV
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Human immunodeficiency virus 1 M01
Q8Q2V9
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Caldibacillus cellulovorans CompA.2, Bacillus caldolyticus EA1
-
DNA polymerase shows significant reverse-transcriptase activity in presence of Mg2+
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Bacillus caldolyticus EA1
A2TD24
poly(rC)*p(dG)(12-18)
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
mouse mammary tumor virus BR6
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Avian myeloblastosis virus BAI
-
the enzyme accepts a variety of natural RNA templates, but shows a preference for oncogenic virus RNA. RNA from other oncogenic viruses is as efficient as AMV RNA. Homopolymeric duplexes are exceptionally good templates, stimulating synthesis 100fold greater than natural RNA or DNA. The enzyme requires a primer
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Reticuloendotheliosis virus T
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Reticuloendotheliosis virus T
-
the enzyme appears to be required very early after infection to synthesize proviral DNA
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Simian immunodeficiency virus mneCl8
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Human immunodeficiency virus 1 BG05
Q8Q2U5
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Thermotoga petrophila K4
-
-, RNA-dependent DNA polymerase activity by enzyme mutants T326A, L329A, Q384A, F388A, M408A, Y438A, L329A/Q384A, L329A/Y438A, and Q384A/Y438A, not by the wild-type enzyme
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Hamster leukemia virus HaLV
-
-
-
-
-
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Hamster leukemia virus HaLV
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Streptomyces coelicolor M145
-
DNA polymerase (PolA) and topoisomerase I (TopA) proteins exhibit highly efficient reverse transcriptase activity in addition to their predicted functions
-
-
?
dGTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
dGTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
RNA-dependent DNA synthesis
-
-
?
dTTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
AF324493, Q8Q2U5, Q8Q2V9
-
-
-
?
dTTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
enzyme mutant N483Q/S486Q/T539N/Y545Q/D547T/P548Q/A570Q/D578Q/A597T/W604R/S612N/V730L/R736Q/S739N/M747R
-
-
?
dTTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
Simian foamy virus, prototype foamy virus
-
homopolymeric substrate poly(rA)/oligo(dT)
-
-
?
dTTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
incorporation of dTTP into poly(rA)-p(dT)15
-
-
?
dTTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
incorporation of dTTP into poly(rA)-p(dT)45
-
-
?
dTTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
Human immunodeficiency virus 1 M01
Q8Q2V9
-
-
-
?
dTTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
Human immunodeficiency virus 1 BG05
Q8Q2U5
-
-
-
?
dTTP + poly(rA)/(dT)18
?
show the reaction diagram
-
-
-
-
-
dTTP + poly(rA)/(dT)18
?
show the reaction diagram
P03355
-
-
-
?
dTTP + poly(rA)/(dT)18
?
show the reaction diagram
-
-
-
-
-
dTTP + poly(rA)/(dT)18
?
show the reaction diagram
-
-
-
-
-
dTTP + poly(rA)/(dT)18
?
show the reaction diagram
-
-
-
-
-
dTTP + poly(rA)/(dT)18
?
show the reaction diagram
-
-
-
-
-
dTTP + poly(rA)/(dT)18
?
show the reaction diagram
-
-
-
-
-
N-cyclobutyladenosine triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
N-cyclobutyladenosine-phosphonyl diphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
tenofovir diphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
thymidine-5'-O-1-thiotriphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
enzyme exhibits a strong preference to incorporate Sp-TTP alphaS isomer over Rp-TTP alphaS isomer in the presence of Mg2+. This stereoselective preference is decreased when Mg2+ is replaced with Mn2+ and Co2+. The enzyme exhibited no phosphorothioate elemental effects for the incorporation of Sp-TTP alphaS, but large elemental effects were calculated for Rp-TTP alphaS for each of the metals tested
-
-
?
dTTP + poly(rA)/(dT)18
?
show the reaction diagram
mouse mammary tumor virus BR6
-
-
-
-
-
additional information
?
-
-
bis-(2'-deoxynucleoside)5,5'-tetraphosphates and bis-(2'-deoxynucleoside)5',5'-triphosphates are effective substrates for DNA elongation
-
-
-
additional information
?
-
-
the reverse transcriptase activity of DNA polymerase gamma is not likely to contribute significantly to the biology of mitochondrial DNA replication, the reverse transcriptase activity of DNA polymerase gamma: in comparison with the kinetic parameters observed with a DNA template, the rate of correct deoxynucleotide incorporation is reduced 25fold, whereas the dissociation constant for nucleotide binding is increased 4fold
-
-
-
additional information
?
-
-
can use both RNA and DNA as a template for DNA synthesis and can cleave RNA within an RNA/DNA hybrid (RNase H activity)
-
-
-
additional information
?
-
-
elongates telomeres to tolerate mutations in the telomeric template
-
-
-
additional information
?
-
-
reverse transcriptase supports RNA-directed DNA synthesis, DNA-directed DNA synthesis and DNA-directed RNA hydrolysis, the enzyme adopts opposite binding orientations on duplexes containing DNA or RNA primers, directing DNA synthesis or RNA hydrolysis activity respectively, binding orientation determines enzymatic activity of reverse transcriptase
-
-
-
additional information
?
-
-
telomerase function comprises lengthening of telomeres, enhancement of DNA repair, promotion of cell growth, modulation of mitochondrial functions under oxidative stress, inhibition of apoptosis, promotion of stem cell proliferation, suppression of DNA damage checkpoints
-
-
-
additional information
?
-
-
uses the cellular tRNALys,3 molecule as primer
-
-
-
additional information
?
-
-
no saturation is observed for extension on DNA templates
-
-
-
additional information
?
-
-
DNA-dependent DNA polymerase commonly accepts DNA and dNTP and excludes RNA and rNTP, but some enzyme mutants also show RNA-dependent DNA polymerase activity as reverse transcriptases, overview. Reverse transcriptase is the enzyme that catalyzes DNA polymerization using RNA as a template, i.e. RNA-dependent DNA polymerase, see for EC 2.7.7.49
-
-
-
additional information
?
-
-
ribonucleoside triphosphate are efficiently incorporated into DNA in the macrophage but not in the T cell environment, detailed overview. HIV-1 RT initiates both (-)- and (+)-proviral DNA synthesis using RNA primers (e.g. tRNA3Lys and polypurine tract RNA primer) containing 3'-end ribonucleoside monophosphates during viral replication
-
-
-
additional information
?
-
-
the enzyme performs DNA-dependent DNA synthesis and RNA-dependent DNA synthesis, see also EC 2.7.7.7
-
-
-
additional information
?
-
-
the viral DNA polymerase activity can be both RNA and DNA dependent, see also EC 2.7.7.7
-
-
-
additional information
?
-
-
HIV-1 RT has high substrate affinity and low susceptibility to formamide
-
-
-
additional information
?
-
-
HIV-1 RT has high substrate affinity and low susceptibility to formamide, and low fidelity. Extremely high fidelity is not required for detection of a target RNA in RT-polymerase chain reaction and RNA-specific amplification, and an isothermal reaction that is widely used in clinical diagnosis, in which RT synthesizes promoter-bearing double-stranded DNA with the help of its RNase H activity
-
-
-
additional information
?
-
-
N-cyclobutyladenosine analogues can act as substrates for incorporation by HIV-1 RT and be a potential scaffold for HIV inhibitors, overview
-
-
-
additional information
?
-
AF324493, Q8Q2U5, Q8Q2V9
recombinant subtype B and C HIV-1 reverse transcriptases show similar enzyme activities and efficiency of tRNA-primed (-) ssDNA synthesis, processivity, fidelity and RNase H activity, as well as susceptibilities to drugs, overview. The enzyme also exhibits RNase H activity, EC 3.1.13.2
-
-
-
additional information
?
-
AF324493, Q8Q2U5, Q8Q2V9
recombinant subtype B and C HIV-1 reverse transcriptases show similar enzyme activities and efficiency of tRNA-primed (-) ssDNA synthesis, processivity, fidelity and RNase H activity, as well as susceptibilities to drugs, overview.. The enzyme also exhibits RNase H activity, EC 3.1.13.2
-
-
-
additional information
?
-
AF324493, Q8Q2U5, Q8Q2V9
recombinant subtype B and C HIV-1 reverse transcriptases show similar enzyme activities and efficiency of tRNA-primed (-)ssDNA synthesis, processivity, fidelity and RNase H activity, as well as susceptibilities to drugs, overview. The enzyme also exhibits RNase H activity, EC 3.1.13.2
-
-
-
additional information
?
-
-
reverse transcriptases perform template switches when there is a very short (two-nucleotide) complementarity between the 3' ends of the primer (donor) strand and the DNA or RNA template acceptor strands. Combined two-step clamp/DNA polymerase activity, where the initial clamp is followed by DNA synthesis, overview
-
-
-
additional information
?
-
-
RNA-DNA hybrid substrate preparation by annealing the RNA oligonucleotide LA-237 with a 1.2fold excess of the complementary DNA oligonucleotide JV-08
-
-
-
additional information
?
-
-
the mutant enzyme shows single nucleotide additions with dCTP, dATP and dTTP, but not with dGTP as it results in addition of two successive base incorporations on the chosen template 2 hybridised to the DNA primer 1, thereby invalidating the single-turnover kinetic model, Michaelis-Menten mechanism, overview
-
-
-
additional information
?
-
-
the N-terminal protease domain of the reverse transcriptase also shows polymerase activity
-
-
-
additional information
?
-
Human immunodeficiency virus 1 M01
Q8Q2V9
recombinant subtype B and C HIV-1 reverse transcriptases show similar enzyme activities and efficiency of tRNA-primed (-) ssDNA synthesis, processivity, fidelity and RNase H activity, as well as susceptibilities to drugs, overview.. The enzyme also exhibits RNase H activity, EC 3.1.13.2
-
-
-
additional information
?
-
Human immunodeficiency virus 1 BG05
Q8Q2U5
recombinant subtype B and C HIV-1 reverse transcriptases show similar enzyme activities and efficiency of tRNA-primed (-) ssDNA synthesis, processivity, fidelity and RNase H activity, as well as susceptibilities to drugs, overview. The enzyme also exhibits RNase H activity, EC 3.1.13.2
-
-
-
additional information
?
-
-
no saturation is observed for extension on DNA templates
-
-
-
additional information
?
-
Thermotoga petrophila K4
-
DNA-dependent DNA polymerase commonly accepts DNA and dNTP and excludes RNA and rNTP, but some enzyme mutants also show RNA-dependent DNA polymerase activity as reverse transcriptases, overview. Reverse transcriptase is the enzyme that catalyzes DNA polymerization using RNA as a template, i.e. RNA-dependent DNA polymerase, see for EC 2.7.7.49
-
-
-
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
2'-deoxyribonucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
enzyme mutant N483Q/S486Q/T539N/Y545Q/D547T/P548Q/A570Q/D578Q/A597T/W604R/S612N/V730L/R736Q/S739N/M747R
-
-
?
dATP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
dATP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
RNA-dependent DNA synthesis
-
-
?
dCTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
-
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Hamster leukemia virus
-
-
-
-
-
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
prototype foamy virus
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
AF324493, Q8Q2U5, Q8Q2V9
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Xenotropic MLV-related virus
A1Z651
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
the alpha enzyme form is more active in the single-strand cDNA-directed synthesis of double-stranded cDNA-directed synthesis of double-stranded DNA than the other 2 enzyme forms
-
-
-
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
the enzyme appears to be required very early after infection to synthesize proviral DNA
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
the enzyme might play a role in normal differentiation
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
enzyme plays a central role during the life cycle of a retrovirus. Temperature-sensitive mutants with a lesion in the reverse transcriptase are unable to establish infections
-
-
-
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
DNA polymerase Pol gamma also catalyzes reverse transcription with a slightly higher efficiency than HIV-1 reverse transcriptase. RNA-primed DNA synthesis activity is required for initiation of mtDNA replication. Poly gamma holoenzyme is capable of performing this reaction at a physiologically releavant rate
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
the enzyme plays a central role in transposition of retroelements
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
RNA-dependent DNA synthesis
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Human immunodeficiency virus 1 M01
Q8Q2V9
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Reticuloendotheliosis virus T
-
the enzyme appears to be required very early after infection to synthesize proviral DNA
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Human immunodeficiency virus 1 BG05
Q8Q2U5
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Thermotoga petrophila K4
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
Hamster leukemia virus HaLV
-
-
-
-
-
dGTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
?
dGTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
-
RNA-dependent DNA synthesis
-
-
?
additional information
?
-
-
the reverse transcriptase activity of DNA polymerase gamma is not likely to contribute significantly to the biology of mitochondrial DNA replication
-
-
-
additional information
?
-
-
can use both RNA and DNA as a template for DNA synthesis and can cleave RNA within an RNA/DNA hybrid (RNase H activity)
-
-
-
additional information
?
-
-
elongates telomeres to tolerate mutations in the telomeric template
-
-
-
additional information
?
-
-
reverse transcriptase supports RNA-directed DNA synthesis, DNA-directed DNA synthesis and DNA-directed RNA hydrolysis, the enzyme adopts opposite binding orientations on duplexes containing DNA or RNA primers, directing DNA synthesis or RNA hydrolysis activity respectively, binding orientation determines enzymatic activity of reverse transcriptase
-
-
-
additional information
?
-
-
telomerase function comprises lengthening of telomeres, enhancement of DNA repair, promotion of cell growth, modulation of mitochondrial functions under oxidative stress, inhibition of apoptosis, promotion of stem cell proliferation, suppression of DNA damage checkpoints
-
-
-
additional information
?
-
-
uses the cellular tRNALys,3 molecule as primer
-
-
-
additional information
?
-
-
DNA-dependent DNA polymerase commonly accepts DNA and dNTP and excludes RNA and rNTP, but some enzyme mutants also show RNA-dependent DNA polymerase activity as reverse transcriptases, overview. Reverse transcriptase is the enzyme that catalyzes DNA polymerization using RNA as a template, i.e. RNA-dependent DNA polymerase, see for EC 2.7.7.49
-
-
-
additional information
?
-
-
ribonucleoside triphosphate are efficiently incorporated into DNA in the macrophage but not in the T cell environment, detailed overview. HIV-1 RT initiates both (-)- and (+)-proviral DNA synthesis using RNA primers (e.g. tRNA3Lys and polypurine tract RNA primer) containing 3'-end ribonucleoside monophosphates during viral replication
-
-
-
additional information
?
-
-
the enzyme performs DNA-dependent DNA synthesis and RNA-dependent DNA synthesis, see also EC 2.7.7.7
-
-
-
additional information
?
-
-
the viral DNA polymerase activity can be both RNA and DNA dependent, see also EC 2.7.7.7
-
-
-
additional information
?
-
Thermotoga petrophila K4
-
DNA-dependent DNA polymerase commonly accepts DNA and dNTP and excludes RNA and rNTP, but some enzyme mutants also show RNA-dependent DNA polymerase activity as reverse transcriptases, overview. Reverse transcriptase is the enzyme that catalyzes DNA polymerization using RNA as a template, i.e. RNA-dependent DNA polymerase, see for EC 2.7.7.49
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Co2+
-
enzyme exhibits a strong preference to incorporate Sp-TTP alphaS isomer over Rp-TTP alphaS isomer in the presence of Mg2+. This stereoselective preference is decreased when Mg2+ is replaced with Mn2+ and Co2+
K+
-
monovalent cation is not required for activity, 20 mM KCl causes 15% stimulation
K+
-
100 mM KCl, 2fold stimulation
K+
-
5 mM, 50% stimulation of activity with poly(dA-dT)
K+
-
5 mM, stimulates rate of DNA synthesis by 20%
K+
-
monovalent cations are not required, but afforded a severalfold stimulation, optimal concentration is 100 mM
K+
-
optimal activity at 50 mM KCl with poly(rA)*oligo(dT) and 10-100 mM KCl for poly(rC)*oligo(dG)
K+
-
optimal activity with the 1.6 kb in vitro transcript corresponding to the 3' end of the plasmid RNA (pVXN15/NsiI, CCA transcript) at 300 mM KCl, optimal activity with poly(rC)-oligo(dG)12-18 at 200 mM
K+
-
maximal incorporation of dTTP into poly(rA) template primed with oligo(dT)12 with 50 mM KCl
Mg2+
-
absolute requirement, optimal concentration: 10 mM
Mg2+
-
optimal concentration is 6 mM with poly(A)-oligo(dT), poly(C)-oligo(dG) or poly(dC)-oligo(dG) as template-primer
Mg2+
-
optimal concentration is 2 mM with poly(A)-oligo(dT) as template-primer and 10 mM with poly(C)-oligo(dG) or poly(dC)-oligo(dG) as template-primer
Mg2+
-
optimal Mg2+ concentration is 10 mM, reaction with AMV RNA
Mg2+
-
Km: 2.5 mM, reaction with poly(dA-dT)
Mg2+
-
optimal Mg2+ concentration is 15 mM
Mg2+
-
requires Mg2+ for activity with DNA or AMV RMA. Optimal activity at 10 mM
Mg2+
-
absolute requirement for a divalent cation, optimal concentration: 5-9 mM
Mg2+
-
marked preference for Mg2+ over Mn2+
Mg2+
-
highest activity is obtained at 5 mM Mg2+ with poly(rA)*oligo(dI) and at about 15 mM Mg2+ with poly(rC)*oligo(dG) and at 15 mM Mg2+ with poly(rC)*oligo(dG)
Mg2+
-
optimal activity with the 1.6 kb in vitro transcript corresponding to the 3' end of the plasmid RNA (pVXN15/NsiI, CCA transcript) at1 mM Mg2+, optimal activity with poly(rC)-oligo(dG)12-18 at 5-10 mM Mg2+
Mg2+
-
optimal activity at 10 mM Mg2+ or Mn2+
Mg2+
-
divalent cation required, Mg2+ supports DNA synthesis to a much lower degree than Mn2+, optimal activity at 0.5 mM
Mg2+
HTLV-III
-
except for the transcription of 2'-O-methylated templates, (rAm)n and (rCm)n, all other template-primers requires Mg2+ for optimal activity
Mg2+
Lymphadenopathy associated virus
-
required
Mg2+
-
divalent metal ion required, enzyme has a preference for Mg2+ over Mn2+. Activity on poly(rA)*oligo(dT)12 is almost 3fold higher with Mg2+ than with Mn2+
Mg2+
-
DNA polymerase shows significant reverse-transcriptase activity in presence of Mg2+
Mg2+
-
enzyme exhibits a strong preference to incorporate Sp-TTP alphaS isomer over Rp-TTP alphaS isomer in the presence of Mg2+. This stereoselective preference is decreased when Mg2+ is replaced with Mn2+ and Co2+
Mg2+
-
5 mM, enzyme shows high activity in presence of
Mg2+
-
reverse transcription of poly(rA) in the presence of 3.5 mM ATP, initial velocity smoothly decreases between 3 and 7 mM MgCl2 and sharply drops below 3 mM. Addition of 3.5 mM ATP shifts the optimal MgCl2 concentration from 1 to 3 mM. At low Mg2+ concentration, reverse transcription of a natural template strongly increases despite a dramatically reduced intrinsic polymerase activity under such conditions. Low Mg2+ concentrations affect the RNA stability and indirectly decreased its degradation by the RNase H activity
Mg2+
-
DNA polymerase activity shows preference to Mn2+ or Mg2+, depending on the substrate used
Mg2+
-
required
Mg2+
-
required
Mg2+
-
required
Mg2+
Xenotropic MLV-related virus
A1Z651
required
Mg2+
AF324493, Q8Q2U5, Q8Q2V9
required; required; required
Mg2+
-
two catalytic Mg2+ ions
Mn2+
-
can partially substitute for Mg2+
Mn2+
-
MnCl2 can substitute for MgCl2
Mn2+
-
optimal concentration is 1.0 mM with poly(A)-oligo(dT) as template-primer and 0.1 mM with poly(C)-oligo(dG) or poly(dC)-oligo(dG) as template-primer
Mn2+
-
optimal concentration is 1.0 mM with poly(A)-oligo(dT) as template-primer and 2.0 mM with poly(C)-oligo(dG) or poly(dC)-oligo(dG) as template-primer
Mn2+
-
Mg2+ can partially be replaced by 1 mM Mn2+
Mn2+
-
1 mM, 30% of the activity obtained with optimal concentrations of Mg2+
Mn2+
-
can partially replace Mg2+
Mn2+
-
absolute requirement for a divalent cation, optimal concentration: 0.8 mM
Mn2+
-
almost no activity is detected in the presence of Mn2+
Mn2+
-
optimal activity at 10 mM Mg2+ or Mn2+
Mn2+
-
divalent cation required, maximal activity at 0.5-1.0 mM MnCl2
Mn2+
-
divalent metal ion required, enzyme has a preference for Mg2+ over Mn2+. Activity on poly(rA)*oligo(dT)12 is almost 3fold higher with Mg2+ than with Mn2+. Maximal dTTP incorporation into poly(rA)*oligo(dT)12 occurs between 0.3 and 0.6 mM MnCl2
Mn2+
-
substitution of Mg2+ by Mn2+ increases the efficiency of incorporation of dNTP analogs
Mn2+
-
enzyme exhibits a strong preference to incorporate Sp-TTP alphaS isomer over Rp-TTP alphaS isomer in the presence of Mg2+. This stereoselective preference is decreased when Mg2+ is replaced with Mn2+ and Co2+
Mn2+
-
enzyme can effectively use Mn2+ at 0.05 mM
Mn2+
-
enzyme can effectively use Mn2+ at 0.05 mM, enzyme does not efficiently use Mg2+
Mn2+
-
DNA polymerase activity shows preference to Mn2+ or Mg2+, depending on the substrate used
NaCl
-
weak stimulation
NaCl
-
maximal DNA synthesis on poly(rA)*oligo(dT) occurs in presence of 60-80 mM NaCl
NaCl
-
maximal incorporation of dTTP into poly(rA) template primed with oligo(dT)12 at 100 mM NaCl
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
((1s,3s)-3-(7-amino-2H-2,3,5,6-tetraazabenzo[cd]azulen-2-yl)cyclobutyl)methyl tetrahydrogen triphosphate
-
-
(-)-epigallocatechin-3-gallate
-
exposure to (-)-epigallocatechin-3-gallate reduces cellular proliferation and induced apoptosis in both MCF-7 and HL60 cells in vitro, although TERT mRNA expression is decreased only in MCF-7 cells
(2-amino-5-chlorophenyl)(2-chlorophenyl)methanone
-
-
(2-amino-5-chlorophenyl)(2-fluorophenyl)methanone
-
-
(2-amino-5-chlorophenyl)(phenyl)methanone
-
-
(4S)-6-chloro-4-(cyclopropylethynyl)-4-(trifluoromethyl)-3,4-dihydroquinazolin-2(1H)-one
-
-
(R)-9-(2-phosphonomethoxypropyl)adenine
-
-
-
([[(2R,5R)-5-(6-amino-7H-purin-7-yl)-2,5-dihydrofuran-2-yl]oxy]methyl)phosphonic acid
-
-
([[(2R,5R)-5-(6-amino-7H-purin-7-yl)-4-fluoro-2,5-dihydrofuran-2-yl]oxy]methyl)phosphonic acid
-
-
([[(2S,5S)-5-(6-amino-7H-purin-7-yl)-2,5-dihydrofuran-2-yl]oxy]methyl)phosphonic acid
-
-
-999 {more}
-
EC50 values, molecular modeling, overview
-
1,10-di-2',3'-dideoxy-3'-thiacytidine-decanoate
-
-
-
1,10-di-3'-azido-2',3'-dideoxythymidine-decanoate
-
-
-
1,10-di-3'-fluoro-2',3'-dideoxythymidine-decanoate
-
-
-
1,10-phenanthroline
-
-
1,12-di-2',3'-dideoxy-3'-thiacytidine-dodecanoate
-
-
-
1,12-di-3'-azido-2',3'-dideoxythymidine-dodecanoate
-
-
-
1,12-di-3'-fluoro-2',3'-dideoxythymidine-dodecanoate
-
-
-
1,14-di-2',3'-dideoxy-3'-thiacytidine-tetradecanoate
-
-
-
1,14-di-3'-azido-2',3'-dideoxythymidine-tetradecanoate
-
-
-
1,14-di-3'-fluoro-2',3'-dideoxythymidine-tetradecanoate
-
-
-
1,2-bis(2-oxopropoxy)anthracene-9,10-dione
-
-
1,2-bis[(3-oxobutan-2-yl)oxy]anthracene-9,10-dione
-
-
1,4-di-2',3'-dideoxy-3'-thiacytidine-succinate
-
-
-
1-[2',5'-bis-O-(t-butyldimethylsilyl)beta-D-ribofuranosyl]-3'-spiro-5''-(4''amino-1'',2''-oxathiole-2'',2''-dioxide)-3-ethylthymine
-
-
12-(deoxyadenosin-N1-yl)nevirapine
-
-
12-(deoxyadenosin-N6-yl)nevirapine
-
-
12-(deoxycytidin-N3-yl)nevirapine
-
-
12-(deoxyguanosin-O6-yl)nevirapine
-
-
12-hydroxy-nevirapine
-
-
2',3'-dehydro-2',3'-deoxythymidine triphosphate
-
i.e. stavudine triphosphate
-
2',3'-dehydro-2',3'-deoxythymidine triphosphate
Xenotropic MLV-related virus
A1Z651
i.e. stavudine triphosphate
-
2',3'-Didehydro-2',3'-dideoxycytidine 5'-triphosphate
-
-
2',3'-didehydro-2',3'-dideoxythymidine
-
-
2',3'-didehydro-2',3'-dideoxythymidine 5'-triphosphate
-
strong but nonspecific inhibitor
2',3'-dideoxy-2',3'-dehydrothymidine 5'-triphosphate
-
terminates synthesis of DNA
2',3'-dideoxy-3'-thiacytidine
-
-
-
2',3'-dideoxy-5-fluoro-3'-thiacytidine
-
-
2',3'-dideoxyguanosine triphosphate
-
-
2',3'-dideoxythymidine 5'-triphosphate
-
-
2',3'-dideoxythymidine 5'-triphosphate
-
Mn2+ is requisite for the compound to exhibit inhibition, competitive with dTTP
2',5'-Oligoadenylate
-
mixed type inhibition, not strictly competitive with dTTP. Inhibition is most dramatic in the absence of sulfhydryl reagents and is reduced when either dithiothreitol or 2-mercaptoethanol are included in the reaction. Partial protection at 0.1 mM dithiothreitol, significant protection at 1 mM or above
2'-deoxyxylofuranosylthymidine 5'-triphosphate
-
Mn2+ is requisite for the compound to exhibit inhibition, competitive with dTTP
2'-fluoro-N-cyclobutyladenosine triphosphate
-
-
-
2,4,6-trichloroquinoline
-
-
2-amino-4-(3-benzoylphenyl)thiazole-5-carboxamide
P04585
-
2-amino-4-(3-bromo-4-chlorophenyl)thiazole-5-carboxamide
P04585
-
2-amino-4-(3-chlorophenyl)thiazole-5-carboxamide
P04585
-
2-amino-4-(3-iodophenyl)thiazole-5-carboxamide
P04585
-
2-amino-4-(3-phenylphenyl)thiazole-5-carboxamide
P04585
-
2-amino-4-phenylthiazole-5-carboxamide
P04585
-
2-hydroxy-6-pentadecylbenzoic acid
-
isolated from the CH2Cl2 extracts of the sacrotestas of Ginkgo biloba
2-hydroxy-6-[(8Z)-pentadec-8-en-1-yl]benzoic acid
-
isolated from the CH2Cl2 extracts of the sacrotestas of Ginkgo biloba
2-naphthalenesulfonic acid
-
in the ternary enzyme-DNA-inhibitor complex, incorporation of the next nucleotide onto the primer is blocked. KM-1 can bind to the enzyme in both the absence and presence of DNA but weakens the affinity for DNA 140fold so that it favors DNA dissociation. KM-1 distorts enzyme conformation and misaligns DNA at the active site
2-pyridin-3-yl-1-(3,4,5-trimethoxybenzoyl)-1H-benzimidazole
-
-
2-pyridin-3-yl-1H-benzimidazole
-
-
2-[(10Z)-heptadec-10-en-1-yl]-6-hydroxybenzoic acid
-
isolated from the CH2Cl2 extracts of the sacrotestas of Ginkgo biloba
2-[2-(4-bromophenyl)-2-oxoethoxy]-9,10-dioxo-9,10-dihydroanthracen-1-yl acetate
-
-
2-[2-(biphenyl-4-yl)-2-oxoethoxy]-9,10-dioxo-9,10-dihydroanthracen-1-yl acetate
-
-
3'-azido-2',3'-dideoxy-2,6-diaminopurine triphosphate
-
-
-
3'-azido-2',3'-dideoxy-2-amino-6-chloropurine triphosphate
-
-
-
3'-azido-2',3'-dideoxy-2-amino-6-methoxypurine triphosphate
-
-
-
3'-azido-2',3'-dideoxy-2-amino-6-N,N-dimethylaminopurine triphosphate
-
-
-
3'-azido-2',3'-dideoxy-2-amino-6-N-allylaminopurine triphosphate
-
-
-
3'-azido-2',3'-dideoxyadenosine triphosphate
-
-
-
3'-azido-2',3'-dideoxyguanosine triphosphate
-
-
-
3'-azido-2',3'-dideoxythymidine
-
-
3'-Azido-2',3'-dideoxythymidine 5'-diphosphate
-
-
3'-Azido-2',3'-dideoxythymidine 5'-triphosphate
-
-
3'-Azido-2',3'-dideoxythymidine 5'-triphosphate
-
; most potent and selective inhibitor
3'-Azido-2',3'-dideoxythymidine 5'-triphosphate
-
Mn2+ is requisite for the compound to exhibit inhibition, competitive with dTTP
3'-Azido-2',3'-dideoxythymidine 5'-triphosphate
-
inhibits the enzyme from the group M strain BH10 isolate and the enzyme from the Spanish HIV-1 group O isolate
3'-azido-3'-deoxythymidine
-
-
3'-azido-3'-deoxythymidine
-
-
3'-azido-3'-deoxythymidine
Xenotropic MLV-related virus
A1Z651
-
3'-azido-3'-dideoxythymidine triphosphate
-
-
-
3'-azido-3'deoxythymidine 5'-triphosphate
-
IC50: 0.042 mM
-
3'-azido-3'deoxythymidine 5'-triphosphate
-
IC50: 0.06 mM
-
3'-deoxyadenosine
-
inhibits HIV-1 proviral DNA synthesis in human macrophages more efficiently than in CD4+ T cells
3'-dideoxythymidine triphosphate
-
-
-
3'-fluoro-2',3'-dideoxythymidine
-
-
3'-gluoro-5'-(2-valyloxypropanoyl)-2',3'-dideoxyguanosine
-
-
3'-hydroxymethyl 2'-dATP
-
highly specific inhibitor
3'-hydroxymethyl 2'-dCTP
-
highly specific inhibitor
3'-hydroxymethyl 2'-dGTP
-
highly specific inhibitor
3'-hydroxymethyl 2'-dUTP
-
highly specific inhibitor
3-(2,4-dinitrophenylhydrazonomethyl) rifamycin SV
-
-
3-(2-cyanoacetyl)phenyl diethyl phosphate
P04585
-
3-(3-chlorophenyl)-3-oxopropanenitrile
P04585
-
3-(3-iodophenyl)-3-oxopropanamide
P04585
-
3-(3-methylbut-2-en-1-yl)-4-[(3-methylbut-2-en-1-yl)oxy]quinolin-2(1H)-one
-
-
3-([3-bromo-2-oxo-5-[(pyridin-3-yloxy)methyl]-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
-
-
3-([3-bromo-2-oxo-5-[(pyridin-4-yloxy)methyl]-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
-
-
3-([3-bromo-5-fluoro-2-oxo-6-[2-(pyridin-4-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
-
-
3-([3-bromo-6-[2-(3-chlorophenyl)ethyl]-5-fluoro-2-oxo-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
-
-
3-([6-[2-(1,3-benzoxazol-2-yl)ethyl]-3-chloro-2-oxo-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
-
-
3-benzoyl-3-oxopropanenitrile
P04585
-
3-chloro-5-([3-chloro-2-oxo-6-[2-(pyridin-2-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
-
-
3-chloro-5-([3-chloro-2-oxo-6-[2-(pyridin-3-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
-
-
3-chloro-5-([3-chloro-2-oxo-6-[2-(pyridin-4-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
-
-
3-chloro-5-([3-chloro-6-methyl-2-oxo-5-[2-(pyridin-3-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
-
-
3-chloro-5-([3-chloro-6-[2-(3,4-dihydroisoquinolin-2(1H)-yl)-2-oxoethyl]-5-fluoro-2-oxo-1,2-dihydropyridin-4-yl]oxy)benzonitrile
-
-
3-chloro-5-([3-chloro-6-[2-(3-chlorophenyl)ethyl]-2-oxo-1,2-dihydropyridin-4-yl]oxy)benzonitrile
-
-
3-chloro-5-([6-[2-(3,4-dihydroisoquinolin-2(1H)-yl)-2-oxoethyl]-3-(dimethylamino)-5-fluoro-2-oxo-1,2-dihydropyridin-4-yl]oxy)benzonitrile
-
-
3-chloro-5-[[3-chloro-2-oxo-6-(2-phenylethyl)-1,2-dihydropyridin-4-yl]oxy]benzonitrile
-
-
3-chloro-5-[[3-chloro-5-fluoro-2-oxo-6-(2-phenylethyl)-1,2-dihydropyridin-4-yl]oxy]benzonitrile
-
-
3-chloro-5-[[3-chloro-6-methyl-2-oxo-5-(phenoxymethyl)-1,2-dihydropyridin-4-yl]oxy]benzonitrile
-
-
3-cyclic amine derivative of rifamycin SV
-
0.2 mg/ml, more than 90% inhibition
-
3-pentadecylphenol
-
isolated from the CH2Cl2 extracts of the sacrotestas of Ginkgo biloba
3-phenyl-3-oxopropanenitrile
P04585
-
3-piperazinoiminomethyl rifamycin SV
-
-
3-tridecylphenol
-
isolated from the CH2Cl2 extracts of the sacrotestas of Ginkgo biloba
3-[(10Z)-heptadec-10-en-1-yl]phenol
-
isolated from the CH2Cl2 extracts of the sacrotestas of Ginkgo biloba
3-[(5-benzyl-3-bromo-2-oxo-1,2-dihydropyridin-4-yl)oxy]-5-chlorobenzonitrile
-
-
3-[(5-benzyl-3-bromo-6-methyl-2-oxo-1,2-dihydropyridin-4-yl)oxy]-5-chlorobenzonitrile
-
-
3-[(8Z)-pentadec-8-en-1-yl]phenol
-
isolated from the CH2Cl2 extracts of the sacrotestas of Ginkgo biloba
3-[6-bromo-3-[2-(3,4-dihydroisoquinolin-2(1H)-yl)-2-oxoethyl]-2-fluorophenoxy]-5-chlorobenzonitrile
-
-
3-[[3-bromo-2-oxo-5-(pyridin-4-ylmethoxy)-1,2-dihydropyridin-4-yl]oxy]-5-chlorobenzonitrile
-
-
4'-ethynyl-2-amino-2'-deoxyadenosine triphosphate
-
-
-
4'-ethynyl-2-amino-2'-deoxyadenosine triphosphate
Xenotropic MLV-related virus
A1Z651
-
-
4'-ethynyl-2-fluoro-2'-deoxyadenosine
-
a translocation defective RT inhibitor, able to inhibit both WT and multi-drug resistant strains of HIV several orders of magnitude, modeling of the ternary complex of HIV-1 RT/DNA/inhibitor, overview. The 4'-ethynyl group is stabilized in a hydrophobic pocket formed by enzyme residues Ala114, Tyr115, Phe160, Met184, and the aliphatic segment of Asp185
-
4'-ethynyl-2-fluoro-2'-deoxyadenosine triphosphate
-
-
-
4'-ethynyl-2-fluoro-2'-deoxyadenosine triphosphate
Xenotropic MLV-related virus
A1Z651
-
-
4-(3-benzoylphenyl)thiazole-5-carboxamide
P04585
-
4-(3-bromo-4-chlorophenyl)-1H-imidazole-5-carboxamide
P04585
-
4-(3-bromo-4-chlorophenyl)thiazole-5-carboxamide
P04585
-
4-(3-chlorophenyl)-1H-imidazole-5-carboxamide
P04585
-
4-(3-iodophenyl)-3-oxobutanenitrile
P04585
-
4-amino-5-fluoro-1-[(2R,5S)-2-(hydroxymethyl)-1,3-oxathiolan-5-yl]pyrimidin-2-one
-
-
4-phenyl-1H-imidazole-5-carboxamide
P04585
-
4-phenylthiazole-5-carboxamide
P04585
-
4-[(3,5-dimethylphenyl)sulfanyl]quinolin-2(1H)-one
-
-
5-benzyl-6-aminouracil
-
competitive with template-primer
5-tridecylbenzene-1,3-diol
-
isolated from the CH2Cl2 extracts of the sacrotestas of Ginkgo biloba
5-[(8Z)-pentadec-8-en-1-yl]benzene-1,3-diol
-
isolated from the CH2Cl2 extracts of the sacrotestas of Ginkgo biloba
6,6-bieckol
-
selective inhibitor, 96.33% inhibition at 0.01 mM
6-chloro-1-(2,6-dichlorobenzyl)-1,3-dihydro-2H-benzimidazol-2-one
-
-
6-chloro-4-(2-fluorophenyl)quinolin-2(1H)-one
-
-
6-chloro-4-(3,5-dimethylphenoxy)quinolin-2(1H)-one
-
-
6-chloro-4-(phenylsulfanyl)quinolin-2(1H)-one
-
-
6-chloro-4-(phenylsulfinyl)quinolin-2(1H)-one
-
-
6-chloro-4-(phenylsulfonyl)quinolin-2(1H)-one
-
-
6-chloro-4-phenoxyquinolin-2(1H)-one
-
-
6-chloro-4-phenylquinolin-2(1H)-one
-
-
6-chloro-4-[(3,5-dimethylphenyl)sulfanyl]quinolin-2(1H)-one
-
-
6-chloro-4-[(3,5-dimethylphenyl)sulfinyl]quinolin-2(1H)-one
-
-
6-chloro-4-[(3,5-dimethylphenyl)sulfonyl]-3,4-dihydroquinoxalin-2(1H)-one
-
-
6-chloro-4-[(3,5-dimethylphenyl)sulfonyl]quinolin-2(1H)-one
-
-
9,10-dioxo-2-(2-oxo-2-phenylethoxy)-9,10-dihydroanthracen-1-yl acetate
-
-
9,10-dioxo-2-(2-oxopropoxy)-9,10-dihydroanthracen-1-yl acetate
-
noncompetitive inhibitor, KNA-53 inhibits the RNase H function and is inactive on the polymerase function of enzyme mutant Y181C
9,10-dioxo-2-(prop-2-en-1-yloxy)-9,10-dihydroanthracen-1-yl acetate
-
-
9,10-dioxo-2-(prop-2-yn-1-yloxy)-9,10-dihydroanthracen-1-yl acetate
-
-
9,10-dioxo-2-[(2-oxopentan-3-yl)oxy]-9,10-dihydroanthracen-1-yl acetate
-
-
9,10-dioxo-2-[(3-oxobutan-2-yl)oxy]-9,10-dihydroanthracen-1-yl acetate
-
-
9,10-dioxo-9,10-dihydroanthracene-1,2-diyl diacetate
-
-
9,10-dioxo-9,10-dihydroanthracene-1,2-diyl dibenzoate
-
noncompetitive inhibitor
adefovir diphosphate
-
-
adefovir diphosphate
Xenotropic MLV-related virus
A1Z651
-
alpha-amomeric oligonucleotides
-
inhibit reaction with either homopolymeric or heteropolymeric substrates
-
alpha-d(A)15
-
0.032 mM, inhibits 50% of the RNA dependent DNA polymerase activity, reaction with poly(U) as template
-
alpha-d(T)16
-
0.08 mM, 50% inhibition of RNA dependent DNA polymerase activity when 0.0075 mM beta-pd(T)12-18 as primer, poly(A) as template
-
azidothymidine
prototype foamy virus
-
inhibits foamy virus replication
azidothymidine
-
inhibits FV replication
azidothymidine triphosphate
-
-
capravirine
-
HIV reverse transcriptase contains two distinct protein domains catalyzing DNA polymerase and RNase H activities. Inhibits 5'-RNA directed HIV RNase H activity of reverse transcriptase. Potency of RNase H inhibition correlats with the respective potencies of DNA polymerase inhibition
dATP
-
replacement of dATP by ATP completely prevents synthesis
ddATP
-
competitive with respect to dATP, noncompetitive with respect to dCTP, dGTP and dTTP
ddTTP
-
inhibits the enzyme from the group M strain BH10 isolate and the enzyme from the Spanish HIV-1 group O isolate
Dextran sulfate
-
IC50: 0.0044 mg/ml
-
early growth response-1
-
overexpressio nof early growth response-1 decreases TERT protein production as well TERT mRNA transcription
-
efaverenz
AF324493, Q8Q2U5, Q8Q2V9
-
-
efavirenz
-
HIV reverse transcriptase contains two distinct protein domains catalyzing DNA polymerase and RNase H activities. Inhibits 5'-RNA directed HIV RNase H activity of reverse transcriptase. Potency of RNase H inhibition correlats with the respective potencies of DNA polymerase inhibition
flavanonol
-
low inhibition
-
flavone
-
low inhibition
GW8248
-
HIV reverse transcriptase contains two distinct protein domains catalyzing DNA polymerase and RNase H activities. Inhibits 5'-RNA directed HIV RNase H activity of reverse transcriptase. Potency of RNase H inhibition correlats with the respective potencies of DNA polymerase inhibition
heparin
-
IC50: 0.0740 mg/ml
KCl
-
80 mM, 60% inhibition
KCl
-
80 mM, 50% inhibition
lamivudine triphosphate
-
-
-
lamivudine triphosphate
-
-
-
lamivudine triphosphate
Xenotropic MLV-related virus
A1Z651
-
-
loviride
-
IC50: 0.0082-0.16 mM, depending on the substrate used.The enzyme from the group M strain BH10 isolate is sensitive. The enzyme from the Spanish HIV-1 group O isolate shows high-level resistance with IC50 above 0.2 mM
Mg2+
-
above 0.5 mM. Addition of Mg2+ to a reaction mixture that already contains Mn2+ does not inhibit the Mn2+-dependent synthesis
morpholinocytosine
-
-
-
N-(4-chlorophenyl)acetamide
-
-
N-cyclobutyladenosine triphosphate
-
-
-
N-cyclobutyladenosine-phosphonyl diphosphate
-
-
-
N-methylisatin beta-thiosemicarbazone
-
0.4 mM, 88% inhibition with a 70S RSV RNA template-primer and 50% inhibition with a calf thymus DNA template-primer in the presence of 1% 2-mercaptoethanol
N2-benzylguanine
-
the enzyme is strongly blocked, ethyl or larger groups cause preferential misincorporation and strong blockage of replicative polymerase activity
-
N2-ethylguanine
-
the enzyme is strongly blocked, ethyl or larger groups cause preferential misincorporation and strong blockage of replicative polymerase activity
N2-isobutylguanine
-
the enzyme is strongly blocked, ethyl or larger groups cause preferential misincorporation and strong blockage of replicative polymerase activity
-
N2-methyl(9-anthracenyl)guanine
-
the enzyme is strongly blocked, ethyl or larger groups cause preferential misincorporation and strong blockage of replicative polymerase activity
-
NaCl
-
IC50: 40-50 mM
naldixic acid
-
noncompetitive with respect to TTP and polyriboadenylic acid. Inhibitory effect is higher with polyriboadenylic acid than with polyribocytidylic acid as a synthetic substrate
NEM
-
2 mM, 82% loss of activity
nevirapine
-
the enzyme from the group M strain BH10 isolate is sensitive, the enzyme from the Spanish HIV-1 group O isolate shows high-level resistance with IC50 above 0.2 mM
nevirapine
-
HIV reverse transcriptase contains two distinct protein domains catalyzing DNA polymerase and RNase H activities. Inhibits 5'-RNA directed HIV RNase H activity of reverse transcriptase. Potency of RNase H inhibition correlats with the respective potencies of DNA polymerase inhibition
nevirapine
-
neviparine is 11-cyclopropyl-5,11-dihydro-4-methyl-6H-dipyrido[3,2-b:2',3'-e][1,4]diazepin-6-one
p-mercuribenzoate
-
0.02 mM, 96% loss of activity
phosphate
-
5 mM, reduced to 73% of maximal activity. 40 mM, reduced to 14% of maximal activity
Phosphonoformate
-
-
PHP protein
-
a dimeric 16 kDa antifungal protein, isolated from the seeds of Peganum harmala by cationic exchange chromatography and gel filtration, inhibitor isoelectric point is about 8.4. Inhibits the viral polymerase to 69.1%. The protein has also inhibitory effect on cell proliferation and fungal growth, overview
-
propan-2-yl 7-methoxy-2-[(methylsulfanyl)methyl]-3-thioxo-3,4-dihydroquinoxaline-1(2H)-carboxylate
-
-
RNA aptamer
-
RNA aptamers suppress viral replication by cumulative inhibition of reverse transcriptase at every stage of genome replication
-
stavudine
-
potent inhibitor
Streptonigrin
-
acts on the enzyme molecule in an enzyme-template primer complex by a series of reactions including oxidation-reduction
Tenofovir
-
9-[(2-phosphonomethoxy)propyl]adenine
Tenofovir
Xenotropic MLV-related virus
A1Z651
-
tenofovir diphosphate
-
-
tenofovir diphosphate
Xenotropic MLV-related virus
A1Z651
-
TMC-125
-
HIV reverse transcriptase contains two distinct protein domains catalyzing DNA polymerase and RNase H activities. Inhibits 5'-RNA directed HIV RNase H activity of reverse transcriptase. Potency of RNase H inhibition correlats with the respective potencies of DNA polymerase inhibition
TMC278
-
nonnucleoside reverse transcriptase inhibitor
zidovudine triphosphate
-
-
Mn2+
-
above 1 mM MnCl2
additional information
-
simultaneous presence of free hydroxyl groups at position 3 and 4' enhance the reverse transcriptase inhibitory activity. Replacement of the 3-hydroxyl group with a monosaccharide or of the 4'-hydroxyl group with a Me group reduces inhibitory activity. The double bond at position 2 and 3 of the flavonoids pyrone ring is not essential for inhibiting reverse transcriptase activity
-
additional information
-
the anti-HIV-1 effect of glycyrrhetinic acid may be involved in the selective inhibition of the human casein kinase II mediated stimulation of HIV-1 RT at the cellular level
-
additional information
-
inhibitors of reverse transcriptase belong to two main classes acting by distinct mechanisms. Nucleoside inhibitors of reverse transcriptase lack a 3' hydroxyl group on their ribose or ribose mimic moiety and thus act as chain terminators. Non-nucleoside inhibitors of reverse transcriptase bind into a hydrophobic pocket close to the polymerase active site and inhibit the chemical step of the polymerization reaction
-
additional information
-
targeted disruption of aromatase results in significant inhibition of telomerase activity
-
additional information
-
not inhibited by didanosine, lamivudine, stavudine, and zidovudine
-
additional information
-
inhibition of feline immunodeficiency virus proviral DNA synthesis is not observed in cells expressing short hairpin RNA that targets the gag gene of feline immunodeficiency virus
-
additional information
-
heat shock perturbes owl monkey TRIMCyp and rhesus TRIM5alpha-mediated restriction of human immunodeficiency virus type 1 late reverse trans products and 2-long terminal repeat circles
-
additional information
-
decreased telomerase activity and normal expression of telomere-binding proteins in the absence of Dicer
-
additional information
-
alizarine derivatives as dual inhibitors of the HIV-1 reverse transcriptase-associated DNA polymerase and RNase H activities effective also on the RNase H activity of non-nucleoside resistant reverse transcriptases, molecular docking and molecular dynamic simulation, overview
-
additional information
-
N-cyclobutyladenosine analogues can act as substrates for incorporation by HIV-1 RT and be a potential scaffold for HIV inhibitors, cyclobutyl derivatives of 2-deoxyadenosine 5-triphosphate as inhibitors of HIV-1 reverse transcriptase, overview
-
additional information
-
inhibitor structure-activity relationships, overview
-
additional information
-
nucleoside reverse transcriptase inhibitors mimic the natural dNTP substrate of the enzyme and bind to the 3'-primer terminus in the polymerase active site acting as chain terminators. A lack of a 3'-OH group promotes effective chain termination, but it also imparts a negative effect on the potency of the NRTI, including a diminished binding affinity for the RT target and decreased ability to be activated by cellular kinases. nucleoside reverse transcriptase inhibitors with 4'-substitutions and a 3'-OH are very effective at inhibiting both wild-type and multi-drug resistant strains of HIV, structure-function analysis, overview
-
additional information
-
ribonucleoside chain terminators may be a class of anti-HIV-1 agents specifically targeting viral macrophage infection
-
additional information
-
synthesis and inhibitory potencies of pyridone diaryl ether non-nucleoside inhibitors of HIV-1 reverse transcriptase, structure-based drug design, overview
-
additional information
-
synthesis and inhibitory activities of quinolin-2-one alkaloid derivatives against HIV-1 reverse transcriptase, molecular docking study, overview
-
additional information
-
the enzyme is highly susceptible to some nucleoside RT inhibitors, including translocation deficient RT inhibitors, but not to non-nucleoside RT inhibitors, e.g. TMC-125 and efavirenz, due to lack of two tyrosine residues involved in binding in enzymes from other virus
-
additional information
Xenotropic MLV-related virus
A1Z651
the enzyme is highly susceptible to some nucleoside RT inhibitors, including translocation deficient RT inhibitors, but not to non-nucleoside RT inhibitors, e.g. TMC-125 and efavirenz, due to lack of two tyrosine residues involved in binding in enzymes from other virus
-
additional information
AF324493, Q8Q2U5, Q8Q2V9
comparison of inhibitor susceptibilities of HIV-1 subtype B and subtype C recombinant reverse transcriptases, overview; comparison of inhibitor susceptibilities of HIV-1 subtype B and subtype C recombinant reverse transcriptases, overview; comparison of inhibitor susceptibilities of HIV-1 subtype B and subtype C recombinant reverse transcriptases, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
betapapillomavirus E6 protein 16E6
-
activates telomerase, NFX1-91 protein is important for telomerase activation by betapapillomavirus E6 protein 16E6
-
betapapillomavirus E6 protein 38E6
-
activates telomerase
-
betapapillomavirus E6 protein E6AP
-
important for telomerase activation by betapapillomavirus E6 protein 16E6
-
borano-3TCTP
-
alpha-Boranophosphate nucleoside analogs enhance 38fold the binding of Mg2+ ions to the active site of the enzyme-DNA-dNTP complex and alleviate the requirement of critical amino acids involved in phosphodiester bond formation
borano-dTTP
-
100fold decrease in polymerase activity caused by the R72A substitution is restored to wild-type levels using borano-dTTP. alpha-Boranophosphate nucleoside analogs enhance 38fold the binding of Mg2+ ions to the active site of the enzyme-DNA-dNTP complex and alleviate the requirement of critical amino acids involved in phosphodiester bond formation
dithiothreitol
-
strong stimulation
dithiothreitol
-
-
dithiothreitol
-
to observe full activity of the enzyme, it is necessary to treat the virions with a non-ionic detergent. If the treatment is at 40C the presence of dithiothreitol is necessary to recover activity
dithiothreitol
-
sulfhydryl reagents required for optimal activity: dithiothreitol or 2-mercaptoethanol
dithiothreitol
-
maximal incorporation of dTTP into poly(rA) template primed with oligo(dT)12 with 10 mM dithiothreitol
DMSO
-
activation at 5-15% v/v
Epidermal growth factor
-
exogenous epidermal growth factor activates TERT gene transcription, epidermal growth factor-induced TERT activity is ERK 1/2-dependent
NFX-91
-
complex formation between betapapillomavirus E6 proteins E6, E6AP, and NFX1-91 is a critical step in mediating telomerase activation
-
Nonionic detergent
-
to observe full activity of the enzyme, it is necessary to treat the virions with a non-ionic detergent. If the treatment is at 40C the presence of dithiothreitol is necessary to recover activity
-
Nonionic detergent
Lymphadenopathy associated virus
-
a critical concentration of nonionic detergent, 0.05%-1%, is required for optimal activity
-
pontin
-
pontin interacts with TERT and dyskerin and is critical for telomerase activity and for the accumulation of TERC and dyskerin
-
reptin
-
reptin interacts with TERT and dyskerin and is critical for telomerase activity and for the accumulation of TERC and dyskerin
-
Stimulatory protein
-
increases the rate and yield of DNA synthesis in reactions containing viral RNA and purified viral polymerase
-
Estrogen
-
administration of estrogen for 3 weeks restores TERT gene expression and telomerase activity in estrogen-deficient mice, telomerase expression is reduced in the absence of estrogen
additional information
-
sulfhydryl reducing agent is required for maximal activity, optimal concentration is 100 mM
-
additional information
-
beta-E6 proteins 5E6, 8E6, 20E6, and 22E6, exhibit low or background levels of telomerase activity
-
additional information
-
frequent activation of TERT expression is not associated with gene amplification
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.01123
-
(-)-beta-2',3'-dideoxy-3'-thiacytidine triphosphate
-
wild-type enzyme
0.0156
-
(-)-beta-2',3'-dideoxy-3'-thiacytidine triphosphate
-
mutant enzyme Y1152-naphthyl-Tyr
0.0275
-
(-)-beta-2',3'-dideoxy-3'-thiacytidine triphosphate
-
mutant enzyme Y115aminomethyl-Phe
0.00217
-
2',3'-dideoxy-CTP
-
wild-type enzyme
0.003
-
2',3'-dideoxy-CTP
-
mutant enzyme Y115aminomethyl-Phe
0.00358
-
2',3'-dideoxy-CTP
-
mutant enzyme Y1152-naphthyl-Tyr
0.0021
-
2'-Deoxyadenosine 5'-triphosphate
-
at 37C
0.00035
-
2'-deoxycytosine 5'-triphosphate
-
at 37C
0.028
-
2'-deoxyguanosine 5'-triphosphate
-
at 37C
0.0046
-
2'-deoxythymidine 5'-triphosphate
-
at 37C
0.00029
-
3'-azido-2',3'-dideoxy-2,6-diaminopurine triphosphate
-
pH 7.5, 37C, wild-type enzyme
-
0.034
-
3'-azido-2',3'-dideoxy-2,6-diaminopurine triphosphate
-
pH 7.5, 37C, wild-type enzyme
-
0.00092
-
3'-azido-2',3'-dideoxy-2-amino-6-chloropurine triphosphate
-
pH 7.5, 37C, wild-type enzyme
-
0.0018
-
3'-azido-2',3'-dideoxy-2-amino-6-chloropurine triphosphate
-
pH 7.5, 37C, wild-type enzyme
-
0.012
-
3'-azido-2',3'-dideoxy-2-amino-6-methoxypurine triphosphate
-
pH 7.5, 37C, wild-type enzyme
-
0.0163
-
3'-azido-2',3'-dideoxy-2-amino-6-methoxypurine triphosphate
-
pH 7.5, 37C, wild-type enzyme
-
0.0048
-
3'-azido-2',3'-dideoxy-2-amino-6-N-allylaminopurine triphosphate
-
pH 7.5, 37C, wild-type enzyme
-
0.00032
-
3'-azido-2',3'-dideoxyadenosine triphosphate
-
pH 7.5, 37C, wild-type enzyme
-
0.00033
-
dATP
-
pH 7.5, 37C, wild-type enzyme
0.003
-
dATP
-
pH 7.6, 37C
0.004674
-
dATP
-
-
0.0087
-
dATP
-
pH and temperature not specified in the publication
0.015
-
dATP
-
reaction with poly(dA-dT)
0.0291
-
dATP
-
pH and temperature not specified in the publication, wild-type enzyme
0.099
-
dATP
-
pH 9.0, 37C, recombinant mutant enzyme N483Q/S486Q/T539N/Y545Q/D547T/P548Q/A570Q/D578Q/A597T/W604R/S612N/V730L/R736Q/S739N/M747R
0.0014
-
dCTP
-
wild-type enzyme
0.00273
-
dCTP
-
wild-type enzyme
0.0047
-
dCTP
-
pH 7.6, 37C
0.00682
-
dCTP
-
mutant enzyme Y115aminomethyl-Phe
0.155
-
dCTP
-
pH and temperature not specified in the publication
0.167
-
dCTP
-
pH 9.0, 37C, recombinant mutant enzyme N483Q/S486Q/T539N/Y545Q/D547T/P548Q/A570Q/D578Q/A597T/W604R/S612N/V730L/R736Q/S739N/M747R
0.045
-
Deoxynucleoside triphosphate
prototype foamy virus
-
determined for dNTPs on a heteropolymeric single stranded M13 substrate, pH and temperature not specified in the publication, recombinant His-tagged protease domain
0.046
-
Deoxynucleoside triphosphate
-
determined for dNTPs on a heteropolymeric single stranded M13 substrate, pH and temperature not specified in the publication, recombinant His-tagged protease domain
0.00017
-
dGTP
-
pH 7.5, 37C, wild-type enzyme
0.000936
-
dGTP
-
-
0.0034
-
dGTP
-
pH 7.5, 37C
0.0055
-
dGTP
-
pH 7.6, 37C
0.059
-
dGTP
-
pH and temperature not specified in the publication
0.0013
-
DNAn
-
pH 8.3, 25C, recombinant enzyme, HIV-1 O RT
0.0014
-
DNAn
-
pH 8.3, 25C, recombinant enzyme, HIV-1 M RT
0.0056
-
DNAn
-
pH 8.3, 25C, recombinant enzyme
0.0056
-
DNAn
-
pH 8.2, 37C, recombinant enzyme, substrate is poly(rA)-p(dT)45
0.0028
-
dTTP
-
pH 7.6, 37C
0.004
-
dTTP
-
pH 8.0, 37C, reaction with poly(rA)*oligo(dT)20, enzyme from group O
0.0045
-
dTTP
-
pH 7.5, 37C
0.0067
-
dTTP
-
pH 8.0, 37C, reaction with poly(rA)*oligo(dT)20, enzyme from group M
0.01005
-
dTTP
P03355
mutant enzyme Q84A
0.01137
-
dTTP
P03355
mutant enzyme Q84A
0.01294
-
dTTP
P03355
mutant enzyme F155H
0.01304
-
dTTP
P03355
wild-type enzyme
0.02
-
dTTP
-
pH 8.3, 25C, recombinant enzyme, HIV-1 M RT
0.026
-
dTTP
-
reaction with poly(dA-dT)
0.03
-
dTTP
-
pH 8.5, 37C
0.03
-
dTTP
-
pH 8.3, 25C, recombinant enzyme, HIV-1 O RT
0.0401
-
dTTP
prototype foamy virus
-
determined for TTP on the homopolymeric substrate poly(rA)/oligo(dT), pH and temperature not specified in the publication, recombinant His-tagged protease domain
0.045
-
dTTP
-
determined for TTP on the homopolymeric substrate poly(rA)/oligo(dT), pH and temperature not specified in the publication, recombinant His-tagged protease domain
0.25
-
dTTP
-
pH 8.3, 25C, recombinant enzyme
0.25
-
dTTP
-
pH 8.2, 37C, recombinant enzyme
0.0047
-
N-cyclobutyladenosine-phosphonyl diphosphate
-
pH and temperature not specified in the publication, wild-type enzyme
-
0.00503
-
poly(rA)/(dT)18
P03355
mutant enzyme Q84A
-
0.01171
-
poly(rA)/(dT)18
P03355
wild-type enzyme
-
0.0066
-
tenofovir diphosphate
-
pH and temperature not specified in the publication, wild-type enzyme
0.379
-
dTTP
-
pH 9.0, 37C, recombinant mutant enzyme N483Q/S486Q/T539N/Y545Q/D547T/P548Q/A570Q/D578Q/A597T/W604R/S612N/V730L/R736Q/S739N/M747R
additional information
-
additional information
-
Km-value for deoxynucleoside triphosphates is 0.01-0.03 mM
-
additional information
-
additional information
-
Km-value for poly(rA)n*oligo(dT)12-18 is 0.004 mg/ml, Km-value for poly(rC)n*oligo(dG)12-18 is 0.0036 mg/ml, measured at pH 7.5 and 37C
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
Michaelis-Menten kinetics, overview
-
additional information
-
additional information
-
Michaelis-Menten kinetics
-
additional information
-
additional information
-
pre-steady state kinetic analysis of 2-deoxyadenosine 5-triphosphate compounds with wild-type and mutant K65R enzymes, overview
-
additional information
-
additional information
-
steady-state kinetic analysis of HIV-1 RT rNTP incorporation
-
additional information
-
additional information
-
dissociation/association rate constants and equilibrium dissociation constants for the three dimeric enzyme forms and their nucleic acid substrates
-
additional information
-
additional information
-
kinetic constants for DNA-dependent and RNA-dependent DNA polymerization Michaelis-Menten mechanism and kinetic model of the mutant enzyme, overview
-
additional information
-
additional information
-
steady-state kinetics of nucleotide incorporation and DNA binding affinity using pre-steady state kinetics, DNA binding affinity using pre-steady state kinetics, overview
-
additional information
-
additional information
Xenotropic MLV-related virus
A1Z651
steady-state kinetics of nucleotide incorporation and DNA binding affinity using pre-steady state kinetics, overview
-
additional information
-
additional information
-
pre-steady-state incorporation of 6-modified 3'-azido-ddGTP nucleotides by HIV-1 RT, steady-state kinetics, overview
-
additional information
-
additional information
-
kinetics of binding of TTP and dATP to the enzyme-DNA complex, the kinetics of mismatch dATP binding are complexoverview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.042
-
(-)-beta-2',3'-dideoxy-3'-thiacytidine triphosphate
-
mutant enzyme Y1152-naphthyl-Tyr
0.15
-
(-)-beta-2',3'-dideoxy-3'-thiacytidine triphosphate
-
wild-type enzyme
0.16
-
(-)-beta-2',3'-dideoxy-3'-thiacytidine triphosphate
-
mutant enzyme Y115aminomethyl-Phe
0.077
-
2',3'-dideoxy-CTP
-
mutant enzyme Y1152-naphthyl-Tyr
0.49
-
2',3'-dideoxy-CTP
-
mutant enzyme Y115aminomethyl-Phe
0.67
-
2',3'-dideoxy-CTP
-
wild-type enzyme
0.0265
-
2'-Deoxyadenosine 5'-triphosphate
-
at 37C
0.0117
-
2'-deoxycytosine 5'-triphosphate
-
at 37C
1.33
-
2'-deoxyguanosine 5'-triphosphate
-
at 37C
0.034
-
2'-deoxythymidine 5'-triphosphate
-
at 37C
0.16
-
3'-azido-2',3'-dideoxy-2,6-diaminopurine triphosphate
-
pH 7.5, 37C, wild-type enzyme
-
14
-
3'-azido-2',3'-dideoxy-2,6-diaminopurine triphosphate
-
pH 7.5, 37C, wild-type enzyme
-
0.37
-
3'-azido-2',3'-dideoxy-2-amino-6-chloropurine triphosphate
-
pH 7.5, 37C, wild-type enzyme
-
2.7
-
3'-azido-2',3'-dideoxy-2-amino-6-chloropurine triphosphate
-
pH 7.5, 37C, wild-type enzyme
-
0.22
-
3'-azido-2',3'-dideoxy-2-amino-6-methoxypurine triphosphate
-
pH 7.5, 37C, wild-type enzyme
-
2.8
-
3'-azido-2',3'-dideoxy-2-amino-6-methoxypurine triphosphate
-
pH 7.5, 37C, wild-type enzyme
-
2.1
-
3'-azido-2',3'-dideoxy-2-amino-6-N-allylaminopurine triphosphate
-
pH 7.5, 37C, wild-type enzyme
-
14
-
3'-azido-2',3'-dideoxyadenosine triphosphate
-
pH 7.5, 37C, wild-type enzyme
-
0.042
-
borano-3TCTP
-
mutant enzyme Y1152-naphthyl-Tyr
0.15
-
borano-3TCTP
-
wild-type enzyme
0.16
-
borano-3TCTP
-
mutant enzyme Y115aminomethyl-Phe
0.00075
-
dATP
-
pH and temperature not specified in the publication
0.25
-
dATP
-
pH 9.0, 37C, recombinant mutant enzyme, N483Q/S486Q/T539N/Y545Q/D547T/P548Q/A570Q/D578Q/A597T/W604R/S612N/V730L/R736Q/S739N/M747R
0.4
-
dATP
-
pH and temperature not specified in the publication, wild-type enzyme
17
-
dATP
-
pH 7.5, 37C, wild-type enzyme
8.3e-05
-
dCTP
-
pH and temperature not specified in the publication
0.76
-
dCTP
-
mutant enzyme Y115aminomethyl-Phe
0.83
-
dCTP
-
pH 9.0, 37C, recombinant mutant enzyme, N483Q/S486Q/T539N/Y545Q/D547T/P548Q/A570Q/D578Q/A597T/W604R/S612N/V730L/R736Q/S739N/M747R
1.25
-
dCTP
-
wild-type enzyme
1.64
-
dCTP
-
wild-type enzyme
3
-
Deoxynucleoside triphosphate
-
determined for dNTPs on a heteropolymeric single stranded M13 substrate, pH and temperature not specified in the publication, recombinant His-tagged protease domain
4
-
Deoxynucleoside triphosphate
prototype foamy virus
-
determined for dNTPs on a heteropolymeric single stranded M13 substrate, pH and temperature not specified in the publication, recombinant His-tagged protease domain
0.00088
-
dGTP
-
pH and temperature not specified in the publication
17.3
-
dGTP
-
pH 7.5, 37C, wild-type enzyme
0.35
-
DNAn
-
pH 8.3, 25C, recombinant enzyme, HIV-1 M RT
1.1
-
DNAn
-
pH 8.3, 25C, recombinant enzyme, HIV-1 O RT
29
-
DNAn
-
pH 8.3, 25C, recombinant enzyme
29
-
DNAn
-
pH 8.2, 37C, recombinant enzyme, substrate is poly(rA)-p(dT)45
0.29
-
dTTP
-
pH 8.0, 37C, reaction with poly(rA)*oligo(dT)20, enzyme from group O
0.35
-
dTTP
-
pH 8.3, 25C, recombinant enzyme, HIV-1 M RT
0.47
-
dTTP
-
pH 8.0, 37C, reaction with poly(rA)*oligo(dT)20, enzyme from group M
0.67
-
dTTP
-
pH 9.0, 37C, recombinant mutant enzyme, N483Q/S486Q/T539N/Y545Q/D547T/P548Q/A570Q/D578Q/A597T/W604R/S612N/V730L/R736Q/S739N/M747R
1.1
-
dTTP
-
pH 8.3, 25C, recombinant enzyme, HIV-1 O RT
5.5
-
dTTP
prototype foamy virus
-
determined for TTP on the homopolymeric substrate poly(rA)/oligo(dT), pH and temperature not specified in the publication, recombinant His-tagged protease domain
7.1
-
dTTP
-
determined for TTP on the homopolymeric substrate poly(rA)/oligo(dT), pH and temperature not specified in the publication, recombinant His-tagged protease domain
29
-
dTTP
-
pH 8.3, 25C, recombinant enzyme
0.07
-
N-cyclobutyladenosine-phosphonyl diphosphate
-
pH and temperature not specified in the publication, wild-type enzyme
-
0.15
-
tenofovir diphosphate
-
pH and temperature not specified in the publication, wild-type enzyme
35
-
dTTP
-
pH 8.2, 37C, recombinant enzyme
additional information
-
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5e-06
-
3'-azido-2',3'-dideoxy-2,6-diaminopurine triphosphate
-
pH 7.5, 37C, wild-type enzyme
0
0.048
-
3'-azido-2',3'-dideoxy-2,6-diaminopurine triphosphate
-
pH 7.5, 37C, wild-type enzyme
0
0.000402
-
3'-azido-2',3'-dideoxy-2-amino-6-chloropurine triphosphate
-
pH 7.5, 37C, wild-type enzyme
0
0.0015
-
3'-azido-2',3'-dideoxy-2-amino-6-chloropurine triphosphate
-
pH 7.5, 37C, wild-type enzyme
0
1.3e-05
-
3'-azido-2',3'-dideoxy-2-amino-6-methoxypurine triphosphate
-
pH 7.5, 37C, wild-type enzyme
0
0.00023
-
3'-azido-2',3'-dideoxy-2-amino-6-methoxypurine triphosphate
-
pH 7.5, 37C, wild-type enzyme
0
0.00044
-
3'-azido-2',3'-dideoxy-2-amino-6-N-allylaminopurine triphosphate
-
pH 7.5, 37C, wild-type enzyme
0
0.044
-
3'-azido-2',3'-dideoxyadenosine triphosphate
-
pH 7.5, 37C, wild-type enzyme
0
0.052
-
dATP
-
pH 7.5, 37C, wild-type enzyme
9499
2.5
-
dATP
-
pH 9.0, 37C, recombinant mutant enzyme N483Q/S486Q/T539N/Y545Q/D547T/P548Q/A570Q/D578Q/A597T/W604R/S612N/V730L/R736Q/S739N/M747R
9499
5.15
-
dATP
-
pH and temperature not specified in the publication, wild-type enzyme
9499
4.9
-
dCTP
-
pH 9.0, 37C, recombinant mutant enzyme N483Q/S486Q/T539N/Y545Q/D547T/P548Q/A570Q/D578Q/A597T/W604R/S612N/V730L/R736Q/S739N/M747R
9510
0.00102
-
dGTP
-
pH 7.5, 37C, wild-type enzyme
9669
1.8
-
dTTP
-
pH 9.0, 37C, recombinant mutant enzyme N483Q/S486Q/T539N/Y545Q/D547T/P548Q/A570Q/D578Q/A597T/W604R/S612N/V730L/R736Q/S739N/M747R
10218
14.89
-
N-cyclobutyladenosine-phosphonyl diphosphate
-
pH and temperature not specified in the publication, wild-type enzyme
0
7.16
-
p-tRNAHis
-
pH 7.5, 22C
0
4.36
-
ppp-tRNAHis
-
pH 7.5, 22C, mutant enzyme D68A
0
5.58
-
ppp-tRNAHis
-
pH 7.5, 22C, wild-type enzyme
0
0.039
-
ppp-tRNALeu
-
pH 7.5, 22C, mutant enzyme D68A
0
0.0048
-
ppp-tRNAPhe
-
pH 7.5, 22C, wild-type enzyme
0
0.42
-
ppp-tRNAPhe
-
pH 7.5, 22C, mutant enzyme D68A
0
60.6
-
tenofovir diphosphate
-
pH and temperature not specified in the publication, wild-type enzyme
269800
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.054
-
2',3'-dideoxyguanosine 5'-triphosphate
-
pH 7.5, 37C
0.0093
-
2',3'-dideoxythymidine 5'-triphosphate
-
pH 8.5, 37C
0.034
-
2',3'-dideoxythymidine 5'-triphosphate
-
pH 7.5, 37C
0.0163
-
2'-deoxyxylofuranosylthymidine 5'-triphosphate
-
pH 8.5, 37C
2.9e-06
-
3'-Azido-2',3'-dideoxythymidine 5'-triphosphate
-
pH 8.0, 37C, reaction with poly(rA)*oligo(dT)20, group O enzyme
6.3e-06
-
3'-Azido-2',3'-dideoxythymidine 5'-triphosphate
-
pH 8.0, 37C, reaction with poly(rA)*oligo(dT)20, group M enzyme
0.0018
-
3'-Azido-2',3'-dideoxythymidine 5'-triphosphate
-
pH 8.5, 37C
0.0085
-
3'-Azido-2',3'-dideoxythymidine 5'-triphosphate
-
pH 7.5, 37C
0.042
-
3'-Azido-2',3'-dideoxythymidine 5'-triphosphate
-
-
5.9e-06
-
ddTTP
-
pH 8.0, 37C, reaction with poly(rA)*oligo(dT)20, group O enzyme
1.4e-05
-
ddTTP
-
pH 8.0, 37C, reaction with poly(rA)*oligo(dT)20, group M enzyme
additional information
-
additional information
-
inhibition kinetic analysis of 2-deoxyadenosine 5-triphosphate compounds with wild-type and mutant K65R enzymes, overview
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3e-05
-
1,10-di-2',3'-dideoxy-3'-thiacytidine-decanoate
-
enzyme from HIV-1 III B, pH and temperature not specified in the publication
-
6e-05
-
1,10-di-2',3'-dideoxy-3'-thiacytidine-decanoate
-
enzyme from HIV-1 US/92/727, pH and temperature not specified in the publication
-
4e-06
-
1,10-di-3'-azido-2',3'-dideoxythymidine-decanoate
-
enzyme from HIV-1 US/92/727, pH and temperature not specified in the publication
-
5e-06
-
1,10-di-3'-azido-2',3'-dideoxythymidine-decanoate
-
enzyme from HIV-1 III B, pH and temperature not specified in the publication
-
1e-06
-
1,10-di-3'-fluoro-2',3'-dideoxythymidine-decanoate
-
enzyme from HIV-1 US/92/727, pH and temperature not specified in the publication
-
4e-06
-
1,10-di-3'-fluoro-2',3'-dideoxythymidine-decanoate
-
enzyme from HIV-1 III B, pH and temperature not specified in the publication
-
9e-06
-
1,12-di-2',3'-dideoxy-3'-thiacytidine-dodecanoate
-
enzyme from HIV-1 III B, pH and temperature not specified in the publication
-
2e-05
-
1,12-di-2',3'-dideoxy-3'-thiacytidine-dodecanoate
-
enzyme from HIV-1 US/92/727, pH and temperature not specified in the publication
-
2e-06
-
1,12-di-3'-azido-2',3'-dideoxythymidine-dodecanoate
-
enzyme from HIV-1 US/92/727, pH and temperature not specified in the publication
-
4e-06
-
1,12-di-3'-azido-2',3'-dideoxythymidine-dodecanoate
-
enzyme from HIV-1 III B, pH and temperature not specified in the publication
-
9.7e-07
-
1,12-di-3'-fluoro-2',3'-dideoxythymidine-dodecanoate
-
enzyme from HIV-1 US/92/727, pH and temperature not specified in the publication
-
4e-06
-
1,12-di-3'-fluoro-2',3'-dideoxythymidine-dodecanoate
-
enzyme from HIV-1 III B, pH and temperature not specified in the publication
-
3e-06
-
1,14-di-2',3'-dideoxy-3'-thiacytidine-tetradecanoate
-
enzyme from HIV-1 III B, pH and temperature not specified in the publication
-
3e-05
-
1,14-di-2',3'-dideoxy-3'-thiacytidine-tetradecanoate
-
enzyme from HIV-1 US/92/727, pH and temperature not specified in the publication
-
3e-06
-
1,14-di-3'-azido-2',3'-dideoxythymidine-tetradecanoate
-
enzyme from HIV-1 III B, pH and temperature not specified in the publication; enzyme from HIV-1 US/92/727, pH and temperature not specified in the publication
-
7.6e-07
-
1,14-di-3'-fluoro-2',3'-dideoxythymidine-tetradecanoate
-
enzyme from HIV-1 US/92/727, pH and temperature not specified in the publication
-
3e-06
-
1,14-di-3'-fluoro-2',3'-dideoxythymidine-tetradecanoate
-
enzyme from HIV-1 III B, pH and temperature not specified in the publication
-
0.014
-
1,2-bis(2-oxopropoxy)anthracene-9,10-dione
-
pH and temperature not specified in the publication
0.1
-
1,2-bis[(3-oxobutan-2-yl)oxy]anthracene-9,10-dione
-
above, pH and temperature not specified in the publication
0.00013
-
1,4-di-2',3'-dideoxy-3'-thiacytidine-succinate
-
enzyme from HIV-1 III B, pH and temperature not specified in the publication
-
0.00015
-
1,4-di-2',3'-dideoxy-3'-thiacytidine-succinate
-
enzyme from HIV-1 US/92/727, pH and temperature not specified in the publication
-
0.00077
-
2',3'-dehydro-2',3'-deoxythymidine triphosphate
Xenotropic MLV-related virus
A1Z651
pH 7.8, 37C
-
0.00237
-
2',3'-dehydro-2',3'-deoxythymidine triphosphate
-
pH 7.8, 37C
-
9e-05
-
2',3'-dideoxy-3'-thiacytidine
-
enzyme from HIV-1 US/92/727, pH and temperature not specified in the publication
-
0.0002
-
2',3'-dideoxy-3'-thiacytidine
-
enzyme from HIV-1 III B, pH and temperature not specified in the publication
-
0.00224
-
2',3'-dideoxy-CTP
-
-
0.0441
-
2-amino-4-(3-benzoylphenyl)thiazole-5-carboxamide
P04585
-
0.118
-
2-amino-4-(3-bromo-4-chlorophenyl)thiazole-5-carboxamide
P04585
-
0.0544
-
2-amino-4-(3-chlorophenyl)thiazole-5-carboxamide
P04585
-
0.1254
-
2-amino-4-(3-iodophenyl)thiazole-5-carboxamide
P04585
-
0.0592
-
2-amino-4-(3-phenylphenyl)thiazole-5-carboxamide
P04585
-
0.0807
-
2-amino-4-phenylthiazole-5-carboxamide
P04585
-
0.005
-
2-[2-(4-bromophenyl)-2-oxoethoxy]-9,10-dioxo-9,10-dihydroanthracen-1-yl acetate
-
pH and temperature not specified in the publication
0.006
-
2-[2-(biphenyl-4-yl)-2-oxoethoxy]-9,10-dioxo-9,10-dihydroanthracen-1-yl acetate
-
pH and temperature not specified in the publication
0.00034
-
3'-azido-2',3'-dideoxy-2,6-diaminopurine triphosphate
-
pH 7.5, 37C, mutant M184V
-
0.0008
-
3'-azido-2',3'-dideoxy-2,6-diaminopurine triphosphate
-
pH 7.5, 37C, wild-type enzyme
-
0.0013
-
3'-azido-2',3'-dideoxy-2,6-diaminopurine triphosphate
-
pH 7.5, 37C, mutant L74V
-
0.0025
-
3'-azido-2',3'-dideoxy-2,6-diaminopurine triphosphate
-
pH 7.5, 37C, mutant K65R
-
0.0042
-
3'-azido-2',3'-dideoxy-2,6-diaminopurine triphosphate
-
pH 7.5, 37C, mutant Q151M
-
0.0025
-
3'-azido-2',3'-dideoxy-2-amino-6-chloropurine triphosphate
-
pH 7.5, 37C, mutant M184V
-
0.0032
-
3'-azido-2',3'-dideoxy-2-amino-6-chloropurine triphosphate
-
pH 7.5, 37C, wild-type enzyme
-
0.0091
-
3'-azido-2',3'-dideoxy-2-amino-6-chloropurine triphosphate
-
pH 7.5, 37C, mutant K65R
-
0.0118
-
3'-azido-2',3'-dideoxy-2-amino-6-chloropurine triphosphate
-
pH 7.5, 37C, mutant L74V
-
0.0308
-
3'-azido-2',3'-dideoxy-2-amino-6-chloropurine triphosphate
-
pH 7.5, 37C, mutant Q151M
-
0.0244
-
3'-azido-2',3'-dideoxy-2-amino-6-methoxypurine triphosphate
-
pH 7.5, 37C, wild-type enzyme
-
0.0329
-
3'-azido-2',3'-dideoxy-2-amino-6-methoxypurine triphosphate
-
pH 7.5, 37C, mutant M184V
-
0.078
-
3'-azido-2',3'-dideoxy-2-amino-6-methoxypurine triphosphate
-
pH 7.5, 37C, mutant Q151M
-
0.08
-
3'-azido-2',3'-dideoxy-2-amino-6-methoxypurine triphosphate
-
pH 7.5, 37C, mutant K65R
-
0.1
-
3'-azido-2',3'-dideoxy-2-amino-6-methoxypurine triphosphate
-
pH 7.5, 37C, mutant L74V
-
0.0234
-
3'-azido-2',3'-dideoxy-2-amino-6-N,N-dimethylaminopurine triphosphate
-
pH 7.5, 37C, wild-type enzyme
-
0.05
-
3'-azido-2',3'-dideoxy-2-amino-6-N,N-dimethylaminopurine triphosphate
-
pH 7.5, 37C, mutant K65R; pH 7.5, 37C, mutant L74V; pH 7.5, 37C, mutant Q151M
-
0.0041
-
3'-azido-2',3'-dideoxy-2-amino-6-N-allylaminopurine triphosphate
-
pH 7.5, 37C, wild-type enzyme
-
0.0048
-
3'-azido-2',3'-dideoxy-2-amino-6-N-allylaminopurine triphosphate
-
pH 7.5, 37C, mutant M184V
-
0.0088
-
3'-azido-2',3'-dideoxy-2-amino-6-N-allylaminopurine triphosphate
-
pH 7.5, 37C, mutant K65R
-
0.0103
-
3'-azido-2',3'-dideoxy-2-amino-6-N-allylaminopurine triphosphate
-
pH 7.5, 37C, mutant L74V
-
0.0218
-
3'-azido-2',3'-dideoxy-2-amino-6-N-allylaminopurine triphosphate
-
pH 7.5, 37C, mutant Q151M
-
0.00016
-
3'-azido-2',3'-dideoxyadenosine triphosphate
-
pH 7.5, 37C, wild-type enzyme
-
0.00019
-
3'-azido-2',3'-dideoxyadenosine triphosphate
-
pH 7.5, 37C, mutant M184V
-
0.00042
-
3'-azido-2',3'-dideoxyadenosine triphosphate
-
pH 7.5, 37C, mutant L74V
-
0.0007
-
3'-azido-2',3'-dideoxyadenosine triphosphate
-
pH 7.5, 37C, mutant K65R
-
0.0014
-
3'-azido-2',3'-dideoxyadenosine triphosphate
-
pH 7.5, 37C, mutant Q151M
-
6e-05
-
3'-azido-2',3'-dideoxyguanosine triphosphate
-
pH 7.5, 37C, mutant M184V
-
0.00015
-
3'-azido-2',3'-dideoxyguanosine triphosphate
-
pH 7.5, 37C, wild-type enzyme
-
0.00025
-
3'-azido-2',3'-dideoxyguanosine triphosphate
-
pH 7.5, 37C, mutant L74V
-
0.0003
-
3'-azido-2',3'-dideoxyguanosine triphosphate
-
pH 7.5, 37C, mutant Q151M
-
0.00036
-
3'-azido-2',3'-dideoxyguanosine triphosphate
-
pH 7.5, 37C, mutant K65R
-
2e-06
-
3'-azido-2',3'-dideoxythymidine
-
enzyme from HIV-1 III B, pH and temperature not specified in the publication
8e-06
-
3'-azido-2',3'-dideoxythymidine
-
enzyme from HIV-1 US/92/727, pH and temperature not specified in the publication
2e-05
-
3'-azido-3'-dideoxythymidine triphosphate
-
mutant enzyme I132A
-
3e-05
-
3'-azido-3'-dideoxythymidine triphosphate
-
mutant enzyme E138A; mutant enzyme I132M
-
4e-05
-
3'-azido-3'-dideoxythymidine triphosphate
-
mutant enzyme I135A
-
6e-05
-
3'-azido-3'-dideoxythymidine triphosphate
-
mutant enzyme I135M; mutant enzyme N137A; mutant enzyme T139V; wild-type enzyme
-
7e-05
-
3'-azido-3'-dideoxythymidine triphosphate
-
mutant enzyme E138K
-
0.042
-
3'-azido-3'deoxythymidine 5'-triphosphate
-
IC50: 0.042 mM
-
0.06
-
3'-azido-3'deoxythymidine 5'-triphosphate
-
IC50: 0.06 mM
-
6e-05
-
3'-dideoxythymidine triphosphate
-
mutant enzyme I132M
-
7e-05
-
3'-dideoxythymidine triphosphate
-
mutant enzyme I132A
-
8e-05
-
3'-dideoxythymidine triphosphate
-
mutant enzyme I135A
-
9e-05
-
3'-dideoxythymidine triphosphate
-
mutant enzyme E138A; mutant enzyme I135M
-
0.0001
-
3'-dideoxythymidine triphosphate
-
mutant enzyme E138K; mutant enzyme N137A; mutant enzyme T139V; wild-type enzyme
-
2e-06
-
3'-fluoro-2',3'-dideoxythymidine
-
enzyme from HIV-1 US/92/727, pH and temperature not specified in the publication
2e-05
-
3'-fluoro-2',3'-dideoxythymidine
-
enzyme from HIV-1 III B, pH and temperature not specified in the publication
0.0643
-
3-(2-cyanoacetyl)phenyl diethyl phosphate
P04585
-
0.0041
-
3-(3-chlorophenyl)-3-oxopropanenitrile
P04585
-
0.0296
-
3-(3-iodophenyl)-3-oxopropanamide
P04585
-
8e-06
-
3-([3-bromo-2-oxo-5-[(pyridin-3-yloxy)methyl]-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
-
mutant Y181C, pH and temperature not specified in the publication
1.1e-05
-
3-([3-bromo-2-oxo-5-[(pyridin-3-yloxy)methyl]-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
-
wild-type enzyme, pH and temperature not specified in the publication
1.6e-05
-
3-([3-bromo-2-oxo-5-[(pyridin-3-yloxy)methyl]-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
-
mutant K103N, pH and temperature not specified in the publication
0.1
-
3-([3-bromo-2-oxo-5-[(pyridin-3-yloxy)methyl]-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
-
pH and temperature not specified in the publication
8e-06
-
3-([3-bromo-2-oxo-5-[(pyridin-4-yloxy)methyl]-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
-
mutant Y181C, pH and temperature not specified in the publication
1e-05
-
3-([3-bromo-2-oxo-5-[(pyridin-4-yloxy)methyl]-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
-
wild-type enzyme, pH and temperature not specified in the publication
1.4e-05
-
3-([3-bromo-2-oxo-5-[(pyridin-4-yloxy)methyl]-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
-
mutant K103N, pH and temperature not specified in the publication
1e-06
-
3-([3-bromo-5-fluoro-2-oxo-6-[2-(pyridin-4-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
-
mutant K103N, pH and temperature not specified in the publication; mutant Y181C, pH and temperature not specified in the publication
2e-06
-
3-([3-bromo-5-fluoro-2-oxo-6-[2-(pyridin-4-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
-
wild-type enzyme, pH and temperature not specified in the publication
8e-06
-
3-([3-bromo-6-[2-(3-chlorophenyl)ethyl]-5-fluoro-2-oxo-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
-
mutant K103N, pH and temperature not specified in the publication; mutant Y181C, pH and temperature not specified in the publication
1.7e-05
-
3-([3-bromo-6-[2-(3-chlorophenyl)ethyl]-5-fluoro-2-oxo-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
-
wild-type enzyme, pH and temperature not specified in the publication
4e-06
-
3-([6-[2-(1,3-benzoxazol-2-yl)ethyl]-3-chloro-2-oxo-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
-
mutant Y181C, pH and temperature not specified in the publication
6e-06
-
3-([6-[2-(1,3-benzoxazol-2-yl)ethyl]-3-chloro-2-oxo-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
-
wild-type enzyme, pH and temperature not specified in the publication
1.6e-05
-
3-([6-[2-(1,3-benzoxazol-2-yl)ethyl]-3-chloro-2-oxo-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
-
mutant K103N, pH and temperature not specified in the publication
0.0098
-
3-benzoyl-3-oxopropanenitrile
P04585
-
2.1e-05
-
3-chloro-5-([3-chloro-2-oxo-6-[2-(pyridin-2-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
-
wild-type enzyme, pH and temperature not specified in the publication
3.3e-05
-
3-chloro-5-([3-chloro-2-oxo-6-[2-(pyridin-2-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
-
mutant Y181C, pH and temperature not specified in the publication
7.8e-05
-
3-chloro-5-([3-chloro-2-oxo-6-[2-(pyridin-2-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
-
mutant K103N, pH and temperature not specified in the publication
1.6e-05
-
3-chloro-5-([3-chloro-2-oxo-6-[2-(pyridin-3-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
-
mutant K103N, pH and temperature not specified in the publication
2.2e-05
-
3-chloro-5-([3-chloro-2-oxo-6-[2-(pyridin-3-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
-
mutant Y181C, pH and temperature not specified in the publication; wild-type enzyme, pH and temperature not specified in the publication
1.4e-05
-
3-chloro-5-([3-chloro-2-oxo-6-[2-(pyridin-4-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
-
mutant K103N, pH and temperature not specified in the publication
1.9e-05
-
3-chloro-5-([3-chloro-2-oxo-6-[2-(pyridin-4-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
-
wild-type enzyme, pH and temperature not specified in the publication
2.1e-05
-
3-chloro-5-([3-chloro-2-oxo-6-[2-(pyridin-4-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
-
mutant Y181C, pH and temperature not specified in the publication
2e-06
-
3-chloro-5-([3-chloro-6-methyl-2-oxo-5-[2-(pyridin-3-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
-
mutant K103N, pH and temperature not specified in the publication
3e-06
-
3-chloro-5-([3-chloro-6-methyl-2-oxo-5-[2-(pyridin-3-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
-
mutant Y181C, pH and temperature not specified in the publication
4e-06
-
3-chloro-5-([3-chloro-6-methyl-2-oxo-5-[2-(pyridin-3-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
-
wild-type enzyme, pH and temperature not specified in the publication
3e-05
-
3-chloro-5-([3-chloro-6-[2-(3,4-dihydroisoquinolin-2(1H)-yl)-2-oxoethyl]-5-fluoro-2-oxo-1,2-dihydropyridin-4-yl]oxy)benzonitrile
-
wild-type enzyme, pH and temperature not specified in the publication
6e-06
-
3-chloro-5-([3-chloro-6-[2-(3-chlorophenyl)ethyl]-2-oxo-1,2-dihydropyridin-4-yl]oxy)benzonitrile
-
mutant K103N, pH and temperature not specified in the publication
7e-06
-
3-chloro-5-([3-chloro-6-[2-(3-chlorophenyl)ethyl]-2-oxo-1,2-dihydropyridin-4-yl]oxy)benzonitrile
-
mutant Y181C, pH and temperature not specified in the publication
1.2e-05
-
3-chloro-5-([3-chloro-6-[2-(3-chlorophenyl)ethyl]-2-oxo-1,2-dihydropyridin-4-yl]oxy)benzonitrile
-
wild-type enzyme, pH and temperature not specified in the publication
0.00022
-
3-chloro-5-([6-[2-(3,4-dihydroisoquinolin-2(1H)-yl)-2-oxoethyl]-3-(dimethylamino)-5-fluoro-2-oxo-1,2-dihydropyridin-4-yl]oxy)benzonitrile
-
wild-type enzyme, pH and temperature not specified in the publication
8e-06
-
3-chloro-5-[[3-chloro-2-oxo-6-(2-phenylethyl)-1,2-dihydropyridin-4-yl]oxy]benzonitrile
-
wild-type enzyme, pH and temperature not specified in the publication
7e-06
-
3-chloro-5-[[3-chloro-5-fluoro-2-oxo-6-(2-phenylethyl)-1,2-dihydropyridin-4-yl]oxy]benzonitrile
-
wild-type enzyme, pH and temperature not specified in the publication
5e-06
-
3-chloro-5-[[3-chloro-6-methyl-2-oxo-5-(phenoxymethyl)-1,2-dihydropyridin-4-yl]oxy]benzonitrile
-
mutant K103N, pH and temperature not specified in the publication
6e-06
-
3-chloro-5-[[3-chloro-6-methyl-2-oxo-5-(phenoxymethyl)-1,2-dihydropyridin-4-yl]oxy]benzonitrile
-
mutant Y181C, pH and temperature not specified in the publication; wild-type enzyme, pH and temperature not specified in the publication
0.0334
-
3-phenyl-3-oxopropanenitrile
P04585
-
3.4e-05
-
3-[(5-benzyl-3-bromo-2-oxo-1,2-dihydropyridin-4-yl)oxy]-5-chlorobenzonitrile
-
wild-type enzyme, pH and temperature not specified in the publication
4.1e-05
-
3-[(5-benzyl-3-bromo-2-oxo-1,2-dihydropyridin-4-yl)oxy]-5-chlorobenzonitrile
-
mutant Y181C, pH and temperature not specified in the publication
7.1e-05
-
3-[(5-benzyl-3-bromo-2-oxo-1,2-dihydropyridin-4-yl)oxy]-5-chlorobenzonitrile
-
mutant K103N, pH and temperature not specified in the publication
7e-06
-
3-[(5-benzyl-3-bromo-6-methyl-2-oxo-1,2-dihydropyridin-4-yl)oxy]-5-chlorobenzonitrile
-
mutant K103N, pH and temperature not specified in the publication
8e-06
-
3-[(5-benzyl-3-bromo-6-methyl-2-oxo-1,2-dihydropyridin-4-yl)oxy]-5-chlorobenzonitrile
-
mutant Y181C, pH and temperature not specified in the publication
1e-05
-
3-[(5-benzyl-3-bromo-6-methyl-2-oxo-1,2-dihydropyridin-4-yl)oxy]-5-chlorobenzonitrile
-
wild-type enzyme, pH and temperature not specified in the publication
1.2e-05
-
3-[6-bromo-3-[2-(3,4-dihydroisoquinolin-2(1H)-yl)-2-oxoethyl]-2-fluorophenoxy]-5-chlorobenzonitrile
-
wild-type enzyme, pH and temperature not specified in the publication
1.1e-05
-
3-[[3-bromo-2-oxo-5-(pyridin-4-ylmethoxy)-1,2-dihydropyridin-4-yl]oxy]-5-chlorobenzonitrile
-
mutant Y181C, pH and temperature not specified in the publication
1.3e-05
-
3-[[3-bromo-2-oxo-5-(pyridin-4-ylmethoxy)-1,2-dihydropyridin-4-yl]oxy]-5-chlorobenzonitrile
-
mutant K103N, pH and temperature not specified in the publication
2.1e-05
-
3-[[3-bromo-2-oxo-5-(pyridin-4-ylmethoxy)-1,2-dihydropyridin-4-yl]oxy]-5-chlorobenzonitrile
-
wild-type enzyme, pH and temperature not specified in the publication
0.00014
-
4'-ethynyl-2-amino-2'-deoxyadenosine triphosphate
Xenotropic MLV-related virus
A1Z651
pH 7.8, 37C
-
0.00018
-
4'-ethynyl-2-amino-2'-deoxyadenosine triphosphate
-
pH 7.8, 37C
-
0.00029
-
4'-ethynyl-2-fluoro-2'-deoxyadenosine triphosphate
-
pH 7.8, 37C
-
0.00043
-
4'-ethynyl-2-fluoro-2'-deoxyadenosine triphosphate
Xenotropic MLV-related virus
A1Z651
pH 7.8, 37C
-
0.0163
-
4-(3-benzoylphenyl)thiazole-5-carboxamide
P04585
-
0.0099
-
4-(3-bromo-4-chlorophenyl)-1H-imidazole-5-carboxamide
P04585
-
0.0875
-
4-(3-bromo-4-chlorophenyl)thiazole-5-carboxamide
P04585
-
0.0798
-
4-(3-chlorophenyl)-1H-imidazole-5-carboxamide
P04585
-
0.0035
-
4-(3-iodophenyl)-3-oxobutanenitrile
P04585
-
0.3
-
4-phenyl-1H-imidazole-5-carboxamide
P04585
-
0.283
-
4-phenylthiazole-5-carboxamide
P04585
-
0.018
-
4-[(3,5-dimethylphenyl)sulfanyl]quinolin-2(1H)-one
-
pH and temperature not specified in the publication
0.1
-
6-chloro-4-(2-fluorophenyl)quinolin-2(1H)-one
-
pH and temperature not specified in the publication
0.00015
-
6-chloro-4-(3,5-dimethylphenoxy)quinolin-2(1H)-one
-
pH and temperature not specified in the publication
0.0056
-
6-chloro-4-(phenylsulfanyl)quinolin-2(1H)-one
-
pH and temperature not specified in the publication
0.0089
-
6-chloro-4-(phenylsulfinyl)quinolin-2(1H)-one
-
pH and temperature not specified in the publication
0.049
-
6-chloro-4-(phenylsulfonyl)quinolin-2(1H)-one
-
pH and temperature not specified in the publication
0.003
-
6-chloro-4-phenoxyquinolin-2(1H)-one
-
pH and temperature not specified in the publication
0.1
-
6-chloro-4-phenylquinolin-2(1H)-one
-
pH and temperature not specified in the publication
0.00021
-
6-chloro-4-[(3,5-dimethylphenyl)sulfanyl]quinolin-2(1H)-one
-
pH and temperature not specified in the publication
0.0026
-
6-chloro-4-[(3,5-dimethylphenyl)sulfinyl]quinolin-2(1H)-one
-
pH and temperature not specified in the publication
0.01
-
6-chloro-4-[(3,5-dimethylphenyl)sulfonyl]quinolin-2(1H)-one
-
pH and temperature not specified in the publication
0.06
-
9,10-dioxo-2-(2-oxo-2-phenylethoxy)-9,10-dihydroanthracen-1-yl acetate
-
pH and temperature not specified in the publication
0.1
-
9,10-dioxo-2-(2-oxopropoxy)-9,10-dihydroanthracen-1-yl acetate
-
above, pH and temperature not specified in the publication
0.082
-
9,10-dioxo-2-(prop-2-en-1-yloxy)-9,10-dihydroanthracen-1-yl acetate
-
pH and temperature not specified in the publication
0.1
-
9,10-dioxo-2-(prop-2-yn-1-yloxy)-9,10-dihydroanthracen-1-yl acetate
-
above, pH and temperature not specified in the publication
0.1
-
9,10-dioxo-2-[(2-oxopentan-3-yl)oxy]-9,10-dihydroanthracen-1-yl acetate
-
above, pH and temperature not specified in the publication
0.061
-
9,10-dioxo-2-[(3-oxobutan-2-yl)oxy]-9,10-dihydroanthracen-1-yl acetate
-
pH and temperature not specified in the publication
0.1
-
9,10-dioxo-9,10-dihydroanthracene-1,2-diyl diacetate
-
above, pH and temperature not specified in the publication
0.012
-
9,10-dioxo-9,10-dihydroanthracene-1,2-diyl dibenzoate
-
pH and temperature not specified in the publication
0.00092
-
adefovir diphosphate
Xenotropic MLV-related virus
A1Z651
pH 7.8, 37C
0.00102
-
adefovir diphosphate
-
pH 7.8, 37C
0.079
-
alizarin
-
pH and temperature not specified in the publication
0.00134
-
azidothymidine triphosphate
-
-
5.4e-06
-
capravirine
-
mutant enzyme K103N
8.6e-06
-
capravirine
-
wild-type enzyme
1.12e-05
-
capravirine
-
mutant enzyme K103N/Y181C
1.83e-05
-
capravirine
-
mutant enzyme Y181C
0.000411
-
capravirine
-
mutant enzyme Y188L
0.00012
-
d4T-TP
-
mutant enzyme I132M
0.00013
-
d4T-TP
-
mutant enzyme I132A
0.00014
-
d4T-TP
-
mutant enzyme T139V
0.00016
-
d4T-TP
-
mutant enzyme E138A; mutant enzyme E138K; mutant enzyme I135A
0.00017
-
d4T-TP
-
mutant enzyme I135M
0.00018
-
d4T-TP
-
mutant enzyme N137A
0.0002
-
d4T-TP
-
wild-type enzyme
0.00152
-
Delavirdine
-
mutant enzyme N137A
0.00218
-
Delavirdine
-
wild-type enzyme
0.00261
-
Delavirdine
-
mutant enzyme T139V
0.00392
-
Delavirdine
-
mutant enzyme I135M
0.00762
-
Delavirdine
-
mutant enzyme E138A
0.0087
-
Delavirdine
-
mutant enzyme I132A
0.013
-
Delavirdine
-
mutant enzyme E138K
0.0302
-
Delavirdine
-
mutant enzyme I132M
0.0346
-
Delavirdine
-
mutant enzyme I135A
2e-06
-
efavirenz
-
wild-type enzyme, pH and temperature not specified in the publication
3e-06
-
efavirenz
-
pH and temperature not specified in the publication
3e-06
-
efavirenz
-
mutant Y181C, pH and temperature not specified in the publication
3.7e-06
-
efavirenz
-
mutant enzyme Y181C
3.9e-06
-
efavirenz
-
wild-type enzyme
6.5e-05
-
efavirenz
-
mutant K103N, pH and temperature not specified in the publication
7.34e-05
-
efavirenz
-
mutant enzyme K103N
8.49e-05
-
efavirenz
-
mutant enzyme K103N/Y181C
8.7e-05
-
efavirenz
-
mutant enzyme N137A
9e-05
-
efavirenz
-
mutant enzyme I132A
9.42e-05
-
efavirenz
-
wild-type enzyme
0.000113
-
efavirenz
-
mutant enzyme T139V
0.000188
-
efavirenz
-
mutant enzyme E138A; mutant enzyme I135A
0.000197
-
efavirenz
-
mutant enzyme I135M
0.000216
-
efavirenz
-
mutant enzyme E138K
0.000228
-
efavirenz
-
mutant enzyme Y188L
0.000432
-
efavirenz
-
mutant enzyme I132M
4.6e-06
-
GW8248
-
mutant enzyme K103N
5.1e-06
-
GW8248
-
mutant enzyme K103N/Y181C
5.9e-06
-
GW8248
-
mutant enzyme Y181C
8.2e-06
-
GW8248
-
wild-type enzyme
6.79e-05
-
GW8248
-
mutant enzyme Y188L
40
50
KCl
-
IC50: 40-50 mM
0.01
-
lamivudine triphosphate
-
pH 7.8, 37C
-
0.021
-
lamivudine triphosphate
Xenotropic MLV-related virus
A1Z651
pH 7.8, 37C
-
40
50
NaCl
-
IC50: 40-50 mM
0.0017
-
nevirapine
P04585
-
0.002217
-
nevirapine
-
wild-type enzyme
0.0065
-
nevirapine
-
mutant enzyme N137A
0.0072
-
nevirapine
-
wild-type enzyme
0.0123
-
nevirapine
-
mutant enzyme T139V
0.0137
-
nevirapine
-
mutant enzyme E138A
0.0159
-
nevirapine
-
mutant enzyme E138K
0.018
-
nevirapine
-
mutant enzyme I132A
0.0389
-
nevirapine
-
mutant enzyme I135M
0.062
-
nevirapine
-
mutant enzyme I132M
0.087
-
nevirapine
-
mutant enzyme I135A
0.2
-
nevirapine
-
the enzyme from the group M strain BH10 isolate is sensitive, the enzyme from the Spanish HIV-1 group O isolate shows high-level resistance with IC50 above 0.2 mM
0.00126
-
PHP protein
-
pH and temperature not specified in the publication
-
0.00151
-
tenofovir diphosphate
-
pH 7.8, 37C
0.0064
-
tenofovir diphosphate
Xenotropic MLV-related virus
A1Z651
pH 7.8, 37C
1.26e-05
-
TMC-125
-
mutant enzyme K103N
2.09e-05
-
TMC-125
-
mutant enzyme Y181C
2.45e-05
-
TMC-125
-
wild-type enzyme
3.24e-05
-
TMC-125
-
mutant enzyme K103N/Y181C
6.47e-05
-
TMC-125
-
mutant enzyme Y188L
0.00012
-
zidovudine triphosphate
-
pH 7.5, 37C, mutant M184V
0.00013
-
zidovudine triphosphate
-
pH 7.5, 37C, wild-type enzyme
0.00018
-
zidovudine triphosphate
-
pH 7.5, 37C, mutant L74V
0.00066
-
zidovudine triphosphate
-
pH 7.5, 37C, mutant K65R
0.0027
-
zidovudine triphosphate
-
pH 7.5, 37C, mutant Q151M
0.2
-
loviride
-
IC50: 0.0082-0.16 mM, depending on the substrate used.The enzyme from the group M strain BH10 isolate is sensitive. The enzyme from the Spanish HIV-1 group O isolate shows high-level resistance with IC50 above 0.2 mM
additional information
-
additional information
-
IC50-values of aptamers
-
additional information
-
additional information
-
the IC50 values for 3-[(8Z)-pentadec-8-en-1-yl]phenol, 3-[(10Z)-heptadec-10-en-1-yl]phenol, 3-tridecylphenol, 3-pentadecylphenol, 5-[(8Z)-pentadec-8-en-1-yl]benzene-1,3-diol, 5-tridecylbenzene-1,3-diol, 2-hydroxy-6-[(8Z)-pentadec-8-en-1-yl]benzoic acid, 2-[(10Z)-heptadec-10-en-1-yl]-6-hydroxybenzoic acid, and 2-hydroxy-6-pentadecylbenzoic acid are above 100 microM
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.000104
-
-
above
0.135
-
-
incorporation of dTMP with poly(RA)*oligo(dT) as template-primer
additional information
-
-
-
additional information
-
-
-
additional information
-
-
quantitative analysis of DNA- and RNA-dependent DNA polymerase activity of enzyme mutants, overview
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.4
-
-
assay at
7.5
-
-
reaction with RSV RNA, poly(rA)*poly(dT) and DNA
7.8
8.5
Lymphadenopathy associated virus
-
-
7.8
-
Xenotropic MLV-related virus
A1Z651
assay at
7.8
-
AF324493, Q8Q2U5, Q8Q2V9
assay at; assay at; assay at
8
8.2
-
assay at
8
8.5
-
optimal activity with the 1.6 kb in vitro transcript corresponding to the 3' end of the plasmid RNA (pVXN15/NsiI, CCA transcript) and with poly(rC)-oligo(dG)12-18
8
9.5
-
reaction with poly(rC)*oligo(dG)
8
-
-
reaction with poly(rA)*oligo(dT)
8
-
-
maximal incorporation of dTTP into poly(rA) template primed with oligo(dT)12
8.2
-
-
reaction with AMV RNA
9
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
10
-
pH 7.0: about 90% of maximal activity, pH 10.0: about 50% of maximal activity
7
8.8
-
pH 7.0: about 40% of maximal activity, pH 8.8: about 75% of maximal activity
7.2
9.8
-
about 50% of maximal activity at pH 7.2 and pH 9.8
7.5
8.5
-
activity falls off rapidly below pH 7.5 and much less rapidly above pH 8.5
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
30
-
optimal activity with poly(rC)-oligo(dG)12-18
30
37
-
optimal activity with the 1.6 kb in vitro transcript corresponding to the 3' end of the plasmid RNA (pVXN15/NsiI, CCA transcript)
37
-
-
-
37
-
-
assay at
37
-
-
assay at
37
-
Xenotropic MLV-related virus
A1Z651
assay at
37
-
AF324493, Q8Q2U5, Q8Q2V9
assay at; assay at; assay at
65
-
-
activity increases from 37C, reaching its highest activity at 65C
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
23
47
-
23C: about 30% of maximal activity, 47C: about 15% of maximal activity
37
65
-
activity increases from 37C, reaching its highest activity at 65C, significant decrease in activity at 75C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.75
-
HTLV-III
-
the enzyme is heterogenous with two isoelectric points, 5.75 and 6.25
6.25
-
HTLV-III
-
the enzyme is heterogenous with two isoelectric points, 5.75 and 6.25
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
gastrointestinal stromal tumors overexpress the catalytic subunit of the human telomerase reverse transcriptase
Manually annotated by BRENDA team
additional information
-
TERT is overexpressed in more than 85% of human cancers
Manually annotated by BRENDA team
additional information
-
telomerase is upregulated in some preneoplastic lesions and overexpressed in the majority of malignant tumors, but absent in most nonneoplastic somatic tissues
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Equine infectious anemia virus (isolate 1369)
Equine infectious anemia virus (isolate 1369)
Human immunodeficiency virus type 1 group M subtype B (isolate ARV2/SF2)
Human immunodeficiency virus type 1 group M subtype B (isolate ARV2/SF2)
Human immunodeficiency virus type 1 group M subtype B (isolate ARV2/SF2)
Human immunodeficiency virus type 1 group M subtype B (isolate ARV2/SF2)
Human immunodeficiency virus type 1 group M subtype B (isolate ARV2/SF2)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
Human immunodeficiency virus type 1 group M subtype B (isolate BH5)
Human immunodeficiency virus type 1 group M subtype B (isolate BH5)
Human immunodeficiency virus type 1 group M subtype B (isolate BH5)
Human immunodeficiency virus type 1 group M subtype B (isolate BH5)
Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
Human immunodeficiency virus type 1 group M subtype B (isolate LW123)
Human immunodeficiency virus type 1 group M subtype B (isolate NY5)
Human immunodeficiency virus type 1 group M subtype B (isolate NY5)
Human immunodeficiency virus type 1 group M subtype B (isolate NY5)
Human immunodeficiency virus type 1 group M subtype B (isolate NY5)
Human immunodeficiency virus type 1 group M subtype B (isolate NY5)
Human immunodeficiency virus type 1 group M subtype B (isolate NY5)
Human immunodeficiency virus type 1 group M subtype B (isolate NY5)
Human immunodeficiency virus type 1 group M subtype B (isolate NY5)
Human immunodeficiency virus type 1 group M subtype B (isolate NY5)
Human immunodeficiency virus type 1 group M subtype B (isolate NY5)
Human immunodeficiency virus type 2 subtype A (isolate ROD)
Moloney murine leukemia virus (isolate Shinnick)
Moloney murine leukemia virus (isolate Shinnick)
Moloney murine leukemia virus (isolate Shinnick)
Moloney murine leukemia virus (isolate Shinnick)
Moloney murine leukemia virus (isolate Shinnick)
Moloney murine leukemia virus (isolate Shinnick)
Moloney murine leukemia virus (isolate Shinnick)
Moloney murine leukemia virus (isolate Shinnick)
Moloney murine leukemia virus (isolate Shinnick)
Moloney murine leukemia virus (isolate Shinnick)
Moloney murine leukemia virus (isolate Shinnick)
Moloney murine leukemia virus (isolate Shinnick)
Moloney murine leukemia virus (isolate Shinnick)
Moloney murine leukemia virus (isolate Shinnick)
Moloney murine leukemia virus (isolate Shinnick)
Moloney murine leukemia virus (isolate Shinnick)
Moloney murine leukemia virus (isolate Shinnick)
Moloney murine leukemia virus (isolate Shinnick)
Moloney murine leukemia virus (isolate Shinnick)
Moloney murine leukemia virus (isolate Shinnick)
Moloney murine leukemia virus (isolate Shinnick)
Moloney murine leukemia virus (isolate Shinnick)
Moloney murine leukemia virus (isolate Shinnick)
Moloney murine leukemia virus (isolate Shinnick)
Moloney murine leukemia virus (isolate Shinnick)
Moloney murine leukemia virus (isolate Shinnick)
Rous sarcoma virus (strain Prague C)
Rous sarcoma virus (strain Prague C)
Rous sarcoma virus (strain Prague C)
Rous sarcoma virus (strain Prague C)
Rous sarcoma virus (strain Schmidt-Ruppin B)
Rous sarcoma virus (strain Schmidt-Ruppin B)
Rous sarcoma virus (strain Schmidt-Ruppin B)
Rous sarcoma virus (strain Schmidt-Ruppin B)
Rous sarcoma virus (strain Schmidt-Ruppin B)
Rous sarcoma virus (strain Schmidt-Ruppin B)
Rous sarcoma virus (strain Schmidt-Ruppin B)
Rous sarcoma virus (strain Schmidt-Ruppin B)
Rous sarcoma virus (strain Schmidt-Ruppin B)
Rous sarcoma virus (strain Schmidt-Ruppin B)
Rous sarcoma virus (strain Schmidt-Ruppin B)
Rous sarcoma virus (strain Schmidt-Ruppin B)
Rous sarcoma virus (strain Schmidt-Ruppin B)
Rous sarcoma virus (strain Schmidt-Ruppin B)
Rous sarcoma virus (strain Schmidt-Ruppin B)
Rous sarcoma virus (strain Schmidt-Ruppin B)
Rous sarcoma virus (strain Schmidt-Ruppin B)
Rous sarcoma virus (strain Schmidt-Ruppin B)
Rous sarcoma virus (strain Schmidt-Ruppin B)
Rous sarcoma virus (strain Schmidt-Ruppin B)
Rous sarcoma virus (strain Schmidt-Ruppin B)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Simian foamy virus type 1
Xenotropic MuLV-related virus (isolate VP35)
Xenotropic MuLV-related virus (isolate VP35)
Xenotropic MuLV-related virus (isolate VP35)
Xenotropic MuLV-related virus (isolate VP62)
Xenotropic MuLV-related virus (isolate VP62)
Xenotropic MuLV-related virus (isolate VP62)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
66000
-
-
glycerol gradient ultracentrifugation
70000
-
-
gel filtration
71000
-
-
glycerol gradient centrifugation
90000
-
-
velocity centrifugation in a glycerol gradient containing 0.05 M KCl
95000
98000
HTLV-III
-
gel filtration
103000
-
-
gel filtration
120000
130000
-
glycerol gradient centrifugation
120000
-
Hamster leukemia virus
-
-
170000
-
-
gel filtration
additional information
-
-
the enzyme exists in two forms with different sizes: 65000 Da and 105000 Da
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 65000, SDS-PAGE; x * 67227, calculation from nucleotide sequence
?
-
x * 65000 + x * 95000, SDS-PAGE
?
-
two polypeptide chains are detected by SDS-PAGE: 69000 Da and 110000 Da
?
-
x * 62879, mutant DNA polymerase I, sequence calculation, x * 62865, mutant DNA polymerase I, mass spectrometry
?
Avian myeloblastosis virus BAI
-
two polypeptide chains are detected by SDS-PAGE: 69000 Da and 110000 Da
-
dimer
-
1 * 50000 + 1 * 64000, both subunits exhibit enzymatic activity, the 64000 Da subunit shows the predominant activity, SDS-PAGE
dimer
Hamster leukemia virus
-
1 * 53000 + 1 * 68000, SDS-PAGE
dimer
-
1 * 66000 + 1 * 51000 or 2 * 66000 or 2 * 51000
dimer
-
while the biologically relevant form of RT is the p66-p51 heterodimer, two recombinant homodimer forms of RT, p66-p66 and p51p51, are also catalytically active
dimer
prototype foamy virus, Simian foamy virus
-
hydrophobic interactions might promote dimerization
dimer
AF324493, Q8Q2U5, Q8Q2V9
1 * 66000 + 1 * 51000, SDS-PAGE; 1 * 66000 + 1 * 51000, SDS-PAGE; 1 * 66000 + 1 * 51000, SDS-PAGE
dimer
Hamster leukemia virus HaLV
-
1 * 53000 + 1 * 68000, SDS-PAGE
-
dimer
Human immunodeficiency virus 1 BG05, Human immunodeficiency virus 1 M01
-
1 * 66000 + 1 * 51000, SDS-PAGE
-
heterodimer
-
-
heterodimer
-
heterodimer consisting of a p51 and a p66 subunit, the latter of which contains catalytically active DNA polymerase and RNAseH domains
heterodimer
-
consists of p66 and p51 subunits
heterodimer
-
1 * 66000 + 1 * 51000, the p66 subunit is composed of a DNA polymerase domain and an RNase H domain, whereas the p51 subunit contains only the polymerase domain
monomer
-
x * 70000-84000
monomer
-
1 * 66000
monomer
-
1 * 71000, SDS-PAGE
monomer
-
-
monomer
mouse mammary tumor virus BR6
-
1 * 66000
-
monomer
Reticuloendotheliosis virus T
-
x * 70000-84000
-
additional information
-
-
additional information
-
three polypeptides of 60000 Da, 68000 Da and 82000 Da are detected by SDS-PAGE. It seems likely that the 68000 Da and the 60000 Da polypeptide are degradation products of the 82000 Da polypeptide
additional information
-
two polypeptides are detected by SDS-PAGE: 70000 Da and 110000 Da
additional information
Human T-cell lymphotropic virus/lymphadenopathy-associated virus
-
two polypeptides of 66000 Da and 41000 Da are detectable in polymerase-expressing bacterial lysates. The 51000 Da protein appears to originate from the 66000 Da molecule
additional information
-
the two subunits are cloned and functionally expressed in Escherichia coli. The recombinant proteins are enzymatically active as homodimers, p66 and p51, as well as a heterodimer p66/p51. The p66/p51 heterodimer can perform strand displacement DNA synthesis of appriximately 300 bases. The homodimer p66 alone can carry out limited strand displacement DNA synthesis, but this activity is stimulated by the p51 subunit at a molar ratio of one molecule of p55 to five molecules of p51. The homodimer p51 itself is unable to fill a small gap of 26 nucleotides in a double-stranded DNA substrate and is not active by itself in strand displacement DNA synthesis
additional information
-
HIV-1 RT exists as a heterodimer as well as a homodimer
additional information
-
structure modeling of K4 polymerase, overview
additional information
-
the FV reverse transcriptase harbors a protease, polymerase and RNase H domain
additional information
AF324493, Q8Q2U5, Q8Q2V9
p66/p51 heterodimer formation through protease cleavage. Although p51 provides RT with essential structural and conformational stability, p66 is the catalytically active subunit and includes the N-terminal polymerase domain (residues 1-321) and C-terminal RNase H domain (residues 441-560), linked by a connection domain; p66/p51 heterodimer formation through protease cleavage. Although p51 provides RT with essential structural and conformational stability, p66 is the catalytically active subunit and includes the N-terminal polymerase domain (residues 1-321) and C-terminal RNase H domain (residues 441-560), linked by a connection domain; p66/p51 heterodimer formation through protease cleavage. Although p51 provides RT with essential structural and conformational stability, p66 is the catalytically active subunit and includes the N-terminal polymerase domain (residues 1-321) and C-terminal RNase H domain (residues 441-560), linked by a connection domain
additional information
-
subunit p66 structure model with bound dNTP substrate and two catalytic Mg2+ ions, overview
additional information
Human immunodeficiency virus 1 BG05, Human immunodeficiency virus 1 M01
-
p66/p51 heterodimer formation through protease cleavage. Although p51 provides RT with essential structural and conformational stability, p66 is the catalytically active subunit and includes the N-terminal polymerase domain (residues 1-321) and C-terminal RNase H domain (residues 441-560), linked by a connection domain
-
additional information
Thermotoga petrophila K4
-
structure modeling of K4 polymerase, overview
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ribonucleoprotein
-
-
proteolytic modification
AF324493, Q8Q2U5, Q8Q2V9
p66/p51 heterodimer formation through protease cleavage; p66/p51 heterodimer formation through protease cleavage; p66/p51 heterodimer formation through protease cleavage
proteolytic modification
Human immunodeficiency virus 1 BG05, Human immunodeficiency virus 1 M01
-
p66/p51 heterodimer formation through protease cleavage
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
in complex with inhibitor TMC278, hanging drop vapour diffusion method, using 9% to 12% PEG 8000, 50 mM imidazole pH 6.0-6.8, 10 mM spermine, 15 mM MgSO4 and 100 mM ammonium sulfate
-
crystal structure of the full-length Moloney murine leukemia virus reverse transcriptase at 3.0 A resolution, hanging-drop vapour-diffusion method
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
activity with poly(rC)*oligo(dG) is stable for up to 20 min
37
-
-
10 min, activity with poly(rA)*oligo(dT) is stable
42
-
-
15 min, 50% loss of activity
45
-
-
25 min, poly(rA)*poligo(dT)-dependent activity is completely destroyed, 20% of the poly(rC)*oligo(dG)-dependent activity is preserved
48
-
-
at high glycerol concehntrations, 2.5 min, 50% loss of activity
50
-
-
thermal inactivation half-life of point mutants at 50C, overview
70
-
-
15 min, complete inactivation
additional information
-
-
heat stable enzyme
additional information
-
-
heat sensitive enzyme
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
presence of 0.2 M ammonium sulfate helps to stabilize the enzyme
-
rapid inactivation by repeated freezing and thawing
-
the enzyme can be recovered after pressure dialysis
-
stable against freezing, thawing, overnight dialysis and high dilutions
Human T-cell lymphotropic virus/lymphadenopathy-associated virus
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
DMSO
-
50% loss of activity at 15% v/v, inactivation at 25% v/v
DMSO
-
stable up to 15% v/v, 50% activation at 5-15% v/v, inactivation at 25% v/v
formamide
-
HIV-1 RT has low susceptibility to formamide, stable up to 15% v/v, inactivation at 25% v/v
formamide
-
50% loss of activity at 17.5% v/v, inactivation at 15% v/v
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 50% glycerol, 2 mM dithioerythritol, less than 20% loss of activity after 2 months
-
-20C, 50% v/v glycerol, purified enzyme retains activity for about 6 months, enzyme also retains activity when stored frozen at -70C
-
-20C, less than 10% loss of activity after 5 weeks
-
-70C, 50% glycerol, stable for more than 12 months
-
-85 to -75C, in frozen cells or tissues, at least one year, remains stable
-
-20C, 50% glycerol, stable
Human T-cell lymphotropic virus/lymphadenopathy-associated virus
-
-10C, 50-70% loss of activity after 1 month
-
-70C, stable for at least 6 months
-
4C, after 2 d the enzyme loses 20% of the poly(rA)*oligo(dT) activity, no activity loss is observed with poly(rC)*oligo(dG) activity
-
-20C, 50% glycerol, 0.2 mg/ml bovine serum albumin, no appreciable loss of activity after several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
improved purification of the 3 enzyme forms: alpha, alpha,beta and beta2
-
recombinant
A2TD24, -
it is important to purify RT-Ec67 from an Escherichia coli strain defective in DNA polymerase I, because this enzyme can utilize an RNA template to synthesize DNA
-
recombinant polyhistidine-tagged reverse transcriptase domain from Escherichia coli by nickel affinity chromatography
-
cloned from a new HIV-1 group O isolate from Spain and expressed in Escherichia coli
-
Mono Q column chromatography
-
purification method development, one-step purification 157fold using an affinity column prepared by conjugating an RNase H specific inhibitor with NHS-activated resin, washing with Mn2+, and elution with EDTA, or purification using a C-terminal intein and a biotin tag for avidin affinty chromatography, followed by reductive cleavage of the Mxe intein, overview. Purification of recombinant enzyme from Escherichia coli strain BL21 (DE3). RNase inhibitors have a greater affinity for the RNase H active site in the presence of Mn2+ than in the presence of Mg2+
-
recombinant His-tagged subtype B HIV-1 reverse transcriptase in heterodimeric form from Escherichia coli strain M15 by metal affinity chromatography and ion exchange chromatography to homogeneity; recombinant His-tagged subtype C HIV-1 reverse transcriptase in heterodimeric form from Escherichia coli strain M15 by metal affinity chromatography and ion exchange chromatography to homogeneity; recombinant His-tagged subtype C HIV-1 reverse transcriptase in heterodimeric form from Escherichia coli strain M15 by metal affinity chromatography and ion exchange chromatography to homogeneity
AF324493, Q8Q2U5, Q8Q2V9
recombinant N-terminal His6-tagged p66/p66 homodimer HIV-1 RT from Escherichia coli strain BL21 (DE3) by nickel affinity, anion exchange, and cation exchange chromatography
-
recombinant N-terminally His6-tagged HIV-1 group M and O RT subunits p51 and p66 from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation, dialysis, anion exchange and nickel affinity chromatography
-
variants of p66 subunit of reverse transcriptase containing meta-Tyr, nor-Tyr, aminomethyl-Phe, and 1-naphthyl-Tyr and 2-naphthyl-Tyr are produced in an Escherichia coli coupled transcription/translation system. Mutant p66 subunits are reconstituted with wild-type p51 subunit of reverse transcriptase and purified
-
wild-type and 3'-azido-3'-deoxythymidine resistant strain D67N/K70R/T215Y/K219Q, expression in Escherichia coli
-
-
Human T-cell lymphotropic virus/lymphadenopathy-associated virus
-
-
Lymphadenopathy associated virus
-
recombinant His-tagged enzyme from Escherichia coli strain BL21-pLysS by nickel affinity chromatography and gel filtration
-
recombinant His-tagged MMLV RT from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation, dialysis, anion exchange and nickel affinity chromatography
-
recombinant enzyme with a six-histidine tag
-
recombinant His-tagged protease domain from Escherichia coli strain BL21 (DE3) pREP4:GroESL by nickel affinity and hydrophobic interaction chromatography
-
HisTrap column chromatography
-
recombinant K4PolI from Escherichia coli
-
recombinant mutant DNA polymerase I from Escherichia coli strain BL21 AI cytoplasm by metal ion and heparin affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21-pLysS by nickel affinity chromatography and gel filtration
Xenotropic MLV-related virus
A1Z651
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli. The recombinant protein proves to be insoluble and is unable to be recovered from the insoluble fraction of lysates of Escherichia coli. The reverse transcriptase is successfully expressed in a baculovirus vector although yields remained low
A2TD24, -
diverse parts of the sequence coding for reverse-transcriptase are subcloned and expressed in Escherichia coli
-
the two subunits are cloned and functionally expressed in Escherichia coli. The recombinant proteins are enzymatically active as homodimers, p66 and p51, as well as a heterodimer p66/p51
-
expression in Escherichia coli
-
expression of active polyhistidine-tagged reverse transcriptase domain, comprising residues 304-693, in an Escherichia coli/rabbit reticulocyte lysate coupled transcriptase-translation system
-
ectopic expression in the heterohybridoma cell line K6H6/B5
-
human LINE-1 ORF2, which encodes reverse transcriptase, is inserted into a baculovirus shuttle vector and expressed in SF21 cells
-
cloned from a new HIV-1 group O isolate from Spain and expressed in Escherichia coli
-
expressed in Escherichia coli BL21 cells
-
expression of N-terminal His6-tagged p66/p66 homodimer HIV-1 RT in Escherichia coli strain BL21 (DE3)
-
expression of N-terminally His6-tagged HIV-1 group M and O RT subunits p51 and p66 in Escherichia coli strain BL21(DE3)
-
expression of untagged or C-terminally intein- and biotin-tagged enzyme in Escherichia coli strain BL21 (DE3)
-
expression of wild-type enzyme and mutant enzymes I132A, I132M, I135A, I135M, N136A, N137A, E138A, E138K, T139A, T139V or P140A in Escherichia coli
-
recombinant expression of His-tagged subtype B HIV-1 reverse transcriptase in Escherichia coli strain M15; recombinant expression of His-tagged subtype C HIV-1 reverse transcriptase in Escherichia coli strain M15; recombinant expression of His-tagged subtype C HIV-1 reverse transcriptase in Escherichia coli strain M15
AF324493, Q8Q2U5, Q8Q2V9
recombinant expression of HIV-1 RTp66/p51 heterodimers, expression of RTp66 subunit in Escherichia coli strain M15 in the absence of HIV-1 protease. The lack of protease allows for the expression of RTp66 without a subsequent cleavage to generate RTp51
-
variants of p66 subunit of reverse transcriptase containing meta-Tyr, nor-Tyr, aminomethyl-Phe, and 1-naphthyl-Tyr and 2-naphthyl-Tyr are produced in an Escherichia coli coupled transcription/translation system. Mutant p66 subunits are reconstituted with wild-type p51 subunit of reverse transcriptase
-
expression in Escherichia coli
Human T-cell lymphotropic virus/lymphadenopathy-associated virus
-
construction of a gene fusion expressing stable fusion protein, expression in Escherichia coli. The resulting gene fusion consists of an open reading frame encoding 698 amino acids. The first 18 amino acids at the N terminus are encoded by the trpE gene, followed by 7 amino acids which are encoded by the pol gene but are not part of the reverse transcriptase. The subsequent 664 amino acids are encoded by the pol gene and the terminal 9 amino acids by pBR322. Construction of deletions at the 3' terminus of the gene results in a 4fold increase in the level of the reverse transcriptase activity in the soluble fraction of crude lysates
-
expression of His-tagged MMLV RT in Escherichia coli strain BL21(DE3)
-
expression of the C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
-
His-tagged enzyme expression in Escherichia coli strain BL21-pLysS
-
recombinantly expressed in Escherichia coli
P03355
construction of a plasmid that induces in bacteria the synthesis of an enzymatically active reverse transcriptase, expression of a protein with a six-histidine tag in Escherichia coli
-
expression of His-tagged protease domain in Escherichia coli strain BL21 (DE3) pREP4:GroESL
-
expressed in Escherichia coli strain Bli5
-
chimeric DNA polymerase, termed CS5 pol, constructed from T. Z05 pol and Tma pol and containing the 5'-3' nuclease domain from Thermus sp. Z05 DNA polymerase (residues 1-291) and the 3'-5' exonuclease and polymerase domains from Thermotoga maritima DNA polymerase (residues 292-893). This chimera retains thermostable DNA polymerase activity, as well as proofreading activity. Using the CS5 chimera, a series of mutant proteins is constructed in which the amino acid side chains are mutated to modulate the 3'-5' exonuclease activity. The chimeric DNA polymerases are overexpressed under the control of the lambda PL promoter are expressed in Escherichia coli
-
phylogenetic tree, expression of K4PolI in Escherichia coli
-
expression of A608T/E520G/W827R, M747K/E742K, and M761T/D547G/I584V in Escherichia coli
-
expression of mutant DNA polymerase I in Escherichia coli strain BL21 AI cytoplasm
-
chimeric DNA polymerase, termed CS5 pol, constructed from T. Z05 pol and Tma pol and containing the 5'-3' nuclease domain from Thermus sp. Z05 DNA polymerase (residues 1-291) and the 3'-5' exonuclease and polymerase domains from Thermotoga maritima DNA polymerase (residues 292-893). This chimera retains thermostable DNA polymerase activity, as well as proofreading activity. Using the CS5 chimera, a series of mutant proteins is constructed in which the amino acid side chains are mutated to modulate the 3'-5' exonuclease activity. The chimeric DNA polymerases are overexpressed under the control of the lambda PL promoter are expressed in Escherichia coli
-
His-tagged enzyme expression in Escherichia coli strain BL21-pLysS
Xenotropic MLV-related virus
A1Z651
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
L180M
-
lamivudine-resistant mutant
M204V
-
lamivudine-resistant mutant
P306A
-
replication competency is reduced to 12.75% of the wild-type value
P306D
-
replication competency is increased to 121.57% of the wild-type value
P306E
-
replication competency is increased to 940.59% of the wild-type value
P306F
-
replication competency is reduced to 41.18% of the wild-type value
P306G
-
replication competency is reduced to 1.96% of the wild-type value
P306L
-
replication competency is increased to 128.04% of the wild-type value
P306R
-
replication competency is reduced to 20.26% of the wild-type value
P306S
-
replication competency is reduced to 47.25% of the wild-type value
P306T
-
replication competency is reduced to 4.5% of the wild-type value
P306V
-
replication competency is increased to 152.75% of the wild-type value
P306Y
-
replication competency is reduced to 10.98% of the wild-type value
A114G
-
mutant enzyme retains significant DNA polymerase activity. 5-6fold increase in the ability of the enzyme to discriminate against ddNTPs
A114S
-
mutant enzyme retains significant DNA polymerase activity, enzyme shows wild-type ddNTP/dNTP discrimination efficiency
A114T
-
mutant enzyme shows very low catalytic efficiency in nucleotide incorporation assays, due to the high KM-values for dNTP. Decreased susceptibility to AZTTP when poly(rA)/(dT)16 is used as substrate
A114V
-
mutant enzyme shows very low catalytic efficiency in nucleotide incorporation assays, due to the high KM-values for dNTP. Decreased susceptibility to AZTTP when poly(rA)/(dT)16 is used as substrate, enzyme shows wild-type ddNTP/dNTP discrimination efficiency
D67N/K70R/T215Y/K219Q
-
mutation results in a 1.5fold decrease in the rate constant for polymerization and a 2.5fold decrease in the equilibrium dissociation constant for 3'-azido-3'-deoxythymidine 5'-triphosphate compared to wild-type enzyme. These values translate into a 4fold decrease in selectivity for 3'-azido-3'-deoxythymidine 5'-monophosphate incorporation ba the mutant enzyme as compared to wild-type enzyme for RNA dependent DNA replication. No such decrease in selectivity is detected for DNA dependent replication
G190V
O12158
mutant with high level of resistance to efavirenz and nevirapine
I132A
-
mutation confers low-level resistance to nevirapine and delavirdine
I132M
-
mutation confers high-level resistance to nevirapine and delavirdine (more than 10fold) and low-level resistance (about 2fold) to efavirenz
I135A
-
mutation confers high level resistance to nevirapine and delavirdine, but not to efavirenz
I135M
-
mutation confers low-level resistance (about 2fold) to nevirapine, delavirdine and efavirenz
K101R
O12158
non-nucleoside reverse transcriptase inhibitor resistance mutation
K103N
-
mutation shows only moderate effects on either polymerase or RNAse H inhibitory potencies of GW8248 and TMC-125. IC50 for nevirapine is strongly enhanced. 1.6fold decrease in IC50-value for capravirine, 18.8fold increase in IC50-value for efavirenz
K103N
-
site-directed mutagenesis, the DNA polymerase function of the enzyme is sensitive to alizarine inhibitors like the wild-type enzyme
K103N
-
site-directed mutagenesis
K103N/Y181C
-
mutation shows only moderate effects on either polymerase or RNAse H inhibitory potencies of GW8248 and TMC-125. IC50 for nevirapine is strongly enhanced. 1.3fold increase in IC50-value for capravirine, 21.8fold increase in IC50-value for efavirenz
K103R
O12158
non-nucleoside reverse transcriptase inhibitor resistance mutation
K65R
-
exhibits an 8-fold resistance to ddATP. 22fold decrease of the catalytic rate constant
K65R
-
mutant maintains a susceptibility to GS-9148 that is similar to wild type enzyme
K65R
-
a HIV-1 O RT variant that shows increased fidelity and stability compared to the wild-type enzyme
K65R
-
site-directed mutagenesis
K65R/L74V
-
84fold decrease of the catalytic rate constant. Virus replication capacity is severely impaired relative to wild-type enzyme. Poor ability of K65R/L74V RT to use natural nucleotides relative to wild-type enzyme: 15% that of wild-type enzyme for dATP, 36% for dGTP, 50% for dTTP, and 25% for dCTP
K65R/V75I
-
a HIV-1 O RT variant that shows increased fidelity and stability compared to the wild-type enzyme
L74V
-
site-directed mutagenesis
M184V
-
mutant maintains a susceptibility to GS-9148 that is similar to wild type enzyme
M184V
-
site-directed mutagenesis
M184V
AF324493, Q8Q2U5, Q8Q2V9
the fidelity of DNA polymerization of the mutant HIV-1 RT is significantly higher than that of wild-type enzyme; the fidelity of DNA polymerization of the mutant HIV-1 RT is significantly higher than that of wild-type enzyme
M230D
O12158
non-nucleoside reverse transcriptase inhibitor resistance mutation
M230N
O12158
non-nucleoside reverse transcriptase inhibitor resistance mutation
N136A
-
mutant enzyme with very low reverse transcriptase activity
N137A
-
mutation confers no resistance to nevirapine, delavirdine and efavirenz
P140A
-
mutant enzyme with very low reverse transcriptase activity
Q151A
-
severe reduction in the polymerase activity withoput any significant effect on the affinity for dNTP substrate. The mutant is nearly devoid of diphosphorolytic activity on a RNA/primer-binding-site template-primer
Q151M
-
site-directed mutagenesis
Q151N
-
reduced dNTP binding affinity, mutant loses the interaction with the 3'-OH of the incoming dTTP, mutant enzyme binds to AZTTP 12 times more tightly than to dTTP
Q151N
-
mutant is catalytically active only at high dNTP concentrations because of its reduced dNTP binding affinity. The modified HIV-1 vector harboring the Q151N mutant reverse transcriptase preferentially transduces tumor cells containing higher cellular dNTP concentrations than primary cells (e.g. human lung fibroblasts and human keratinocytes). The wild type HIV-1 vector transduces both human lung fibroblasts and tumor cells. The Q151N vector fails to transduce human lung fibroblasts and keratinocytes but efficiently transduces tumor cells. Pretreatment of human lung fibroblasts with deoxynucleosides, which increase cellular dNTP pools, enables the mutant vector to transduce human lung fibroblasts, suggesting that the transduction failure of the RT mutant vector to primary cells is because of inefficient reverse transcription in low cellular dNTP environments
R78A
-
a HIV-1 O RT variant that shows increased fidelity and stability compared to the wild-type enzyme
T139A
-
mutant enzyme with very low reverse transcriptase activity
T139V
-
mutation confers no resistance to nevirapine, delavirdine and efavirenz
V148I
-
reduced dNTP binding affinity, mutation V148I disrupts positioning of Q151 for interaction with the 3'-OH of the incoming dTTP, mutant enzyme binds to AZTTP 18 times more tightly than to dTTP
V197I
O12158
non-nucleoside reverse transcriptase inhibitor resistance mutation
Y1152-naphthyl-Tyr
-
mutant of the p66 subunit of reverse transcriptase reconstituted with wild-type p51 subunit. Mutant enzyme inefficiently incorporates dCTP at low concentrations and is kinetically slower with all dCTP analogues tested. 5fold less efficient for dCTP incorporation and 15fold less efficient for 2',3'-dideoxy-CTP incorporation compared to the wild-type enzyme
Y115aminomethyl-Phe
-
mutant of the p66 subunit of reverse transcriptase reconstituted with wild-type p51 subunit. Mutant enzyme incorporates dCTP more efficiently than the wild-type and is resistant to the chain terminator (-)-beta-2',3'-dideoxy-3'-thiacytidine triphosphate when examined in a steady-state fidelity assay. Mutant enzyme incorporates very little 3TCMP, even when the concentration of the chain terminator was 100times that of the dCTP
Y181C
-
mutation shows only moderate effects on either polymerase or RNAse H inhibitory potencies of GW8248 and TMC-125. IC50 for nevirapine is strongly enhanced. 2.1fold increase in IC50-value for capravirine, IC50 for efavirenz is nearly identical to wild-type value
Y181C
-
site-directed mutagenesis, the DNA polymerase function of the enzyme is insensitive to alizarine inhibitors
Y181C
-
site-directed mutagenesis
Y188L
-
mutation shows only moderate effects on either polymerase or RNAse H inhibitory potencies of GW8248 and TMC-125. IC50 for nevirapine is strongly enhanced. 47.8fold increase in IC50-value for capravirine, 58fold increase in IC50-value for efavirenz
M184V
Human immunodeficiency virus 1 BG05, Human immunodeficiency virus 1 M01
-
the fidelity of DNA polymerization of the mutant HIV-1 RT is significantly higher than that of wild-type enzyme
-
Q294A
-
the mutation has no significant effect on the noticeable level of the DNA polymerase activity of the enzyme (12% increase of activity compared to the wild type enzyme)
Q294C
-
the mutation has no significant effect on the noticeable level of the DNA polymerase activity of the enzyme (34% increase of activity compared to the wild type enzyme)
Q294E
-
the mutation has no significant effect on the noticeable level of the DNA polymerase activity of the enzyme (11% increase of activity compared to the wild type enzyme)
Q294H
-
the mutation has no significant effect on the noticeable level of the DNA polymerase activity of the enzyme (16% increase of activity compared to the wild type enzyme)
Q294M
-
the mutation has no significant effect on the noticeable level of the DNA polymerase activity of the enzyme (4% increase of activity compared to the wild type enzyme)
Q294N
-
the mutation has no significant effect on the noticeable level of the DNA polymerase activity of the enzyme (36% increase of activity compared to the wild type enzyme)
Q294P
-
the mutation has no significant effect on the noticeable level of the DNA polymerase activity of the enzyme (13% increase of activity compared to the wild type enzyme)
Q294R
-
the mutation has no significant effect on the noticeable level of the DNA polymerase activity of the enzyme (35% increase of activity compared to the wild type enzyme)
Q294S
-
the mutation has no significant effect on the noticeable level of the DNA polymerase activity of the enzyme (19% increase of activity compared to the wild type enzyme)
Q294W
-
the mutation has no significant effect on the noticeable level of the DNA polymerase activity of the enzyme (13% increase of activity compared to the wild type enzyme)
Q294Y
-
the mutation has no significant effect on the noticeable level of the DNA polymerase activity of the enzyme (3% increase of activity compared to the wild type enzyme)
A502V
-
site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme
A644V
-
site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme
D200N
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
D200N/L603W/T330P/L139P/E607K
-
site-directed mutagenesis, highly processive and thermostable multiply-mutated M-MuLV RT variant with 65fold improvement in comparison to the wild-type enzyme, the maximum temperature of the full-length cDNA synthesis is raised to 62C, compared to 45C for the wild-type enzyme
E607K
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
F155V
P03355
the mutation increase the affinity of the enzyme for ribonucleotides, without affecting the Vmax for catalysis, and thereby conferrs to the enzyme significant RNA polymerase activity
F625S
-
site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme
H126R
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
K103R
-
site-directed mutagenesis, the mutant is resistant to inhibition by tenofovir and 3'-azido-3'-deoxythymidine
K658R
-
site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme
L139P
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
L333Q
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
L603W
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
L671P
-
site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme
N649S
-
site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme
P130S
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
P65S
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
Q190M
-
site-directed mutagenesis, the mutant is resistant to inhibition by tenofovir and 3'-azido-3'-deoxythymidine
Q84A
P03355
mutant enzyme displays higher DNA polymerase activities than wild-type enzyme. Vmax of Q84AH using dTTP as a substrate is about three times that of wild-type value, whereas the Km values are very similar
Q84A/F155V
P03355
Q84A mutation further improves RNA polymerase and DNA polymerase activity of mutant F155V
Q84N
P03355
mutant enzyme displays higher DNA polymerase activities than wild-type enzyme
T287A
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
T330P
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
W388R
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
Y344H
-
site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme
D211N
-
still capable of in vitro polymerization, although it is blocked for in vivo transposition. D211N mutation has minimal effect on nucleotide binding but reduces the kpol by about 230fold. The mutation reduces binding affinity for both Mn2+ and Mg2+
F292A
-
slight diminuation in DNA-dependent DNA synthesis (under conditions allowing multiple rounds of synthesis). Significant reduction in polymerase activity in presence of heparin
F292Y
-
severly impaired Rnase H activity
G294A
-
mutation results in enhanced pausing at multiple positions of the DNA template in DNA-dependent DNA synthesis (under conditions allowing multiple rounds of synthesis). Significant reduction in polymerase activity in presence of heparin
Y298A
-
slight diminuation in DNA-dependent DNA synthesis (under conditions allowing multiple rounds of synthesis). Significant reduction in polymerase activity in presence of heparin
Y298W
-
significant reduction in polymerase activity in presence of heparin
F227L
-
mutant shows 2 to 3fold increase in infectivity
G211S
-
mutant shows 2 to 3fold increase in infectivity
I148V
-
mutant shows 2 to 3fold increase in infectivity
I257M
-
mutant shows 2 to 3fold increase in infectivity
K412E
-
mutant demonstrates a 12fold increase in infectivity compared to the parental virus SIVmneCl8 indicating a role for mutations in the connection domain of reverse transcriptase in influencing viral infectivity and replication
R173K
-
mutant shows 2 to 3fold increase in infectivity
T288A
-
mutant shows 2 to 3fold increase in infectivity
V108I
-
mutant shows 2 to 3fold increase in infectivity
F227L
Simian immunodeficiency virus mneCl8
-
mutant shows 2 to 3fold increase in infectivity
-
I257M
Simian immunodeficiency virus mneCl8
-
mutant shows 2 to 3fold increase in infectivity
-
K412E
Simian immunodeficiency virus mneCl8
-
mutant demonstrates a 12fold increase in infectivity compared to the parental virus SIVmneCl8 indicating a role for mutations in the connection domain of reverse transcriptase in influencing viral infectivity and replication
-
R173K
Simian immunodeficiency virus mneCl8
-
mutant shows 2 to 3fold increase in infectivity
-
V108I
Simian immunodeficiency virus mneCl8
-
mutant shows 2 to 3fold increase in infectivity
-
F388A
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
L329A
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
L329A/Q384A
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
L329A/Y438A
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
M408A
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
Q384A
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
Q384A/Y438A
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
T326A
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
Y438A
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
F388A
Thermotoga petrophila K4
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
-
L329A
Thermotoga petrophila K4
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
-
Q384A
Thermotoga petrophila K4
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
-
T326A
Thermotoga petrophila K4
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
-
Y438A
Thermotoga petrophila K4
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
-
A608T/E520G/W827R
-
substitution rates per base for RNA-dependent DNA is similar or lower than that of avian myeloblastosis virus reverse transcriptase. Rate constants kcat of about two orders of magnitude larger than those of the Stoffel fragment
M747K/E742K
-
substitution rates per base for RNA-dependent DNA is similar to that of avian myeloblastosis virus reverse transcriptase
K103R
Xenotropic MLV-related virus
A1Z651
site-directed mutagenesis, the mutant is resistant to inhibition by tenofovir and 3'-azido-3'-deoxythymidine
Q190M
Xenotropic MLV-related virus
A1Z651
site-directed mutagenesis, the mutant is resistant to inhibition by tenofovir and 3'-azido-3'-deoxythymidine
M428L
-
site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme
additional information
-
construction of deletions at the 3' terminus of the gene results in a 4fold increase in the level of the reverse transcriptase activity in the soluble fraction of crude lysates
additional information
-
generation of enzyme mutants with increased thermostability using compartmentalized ribosome display evolution in vitro technique, overview. Identification of a large set of mutations that enable cDNA synthesis at elevated temperatures. Altered substrate-binding affinity and progressivity of mutant enzymes, overview
D215A
-
enzyme mutant devoid of 3'-5' exonuclease activity
additional information
-
Z derivatives have the fingers domain of Tgo-Pol replaced with that from Pol zeta, insertion of the Pol zeta finger domains into the Thermococcus gorgonarius Tgo-Pol resulting in the Z derivatives increase the enzyme activity. Z1 shows increased activity, which is further increased with Z2, created by fusion of Z1 with the processivity-increasing DNA binding protein Sso7d, overview
additional information
-
chimeric DNA polymerase, termed CS5 pol, constructed from T. Z05 pol and Tma pol and containing the 5'-3' nuclease domain from Thermus sp. Z05 DNA polymerase (residues 1-291) and the 3'-5' exonuclease and polymerase domains from Thermotoga maritima DNA polymerase (residues 292-893). This chimera retains thermostable DNA polymerase activity, as well as proofreading activity. Using the CS5 chimera, a series of mutant proteins is constructed in which the amino acid side chains are mutated to modulate the 3'-5'?exonuclease activity. A thermoactive and thermostable enzyme with reverse transcriptase and 3'-5'exonuclease activity is described
M761T/D547G/I584V
-
fidelity which is about 10-times higher than that of avian myeloblastosis virus reverse transcriptase. Almost tenfold improved catalytic efficiency as measured by the kcat/Km ratio when compared with the Stoffel fragment
additional information
-
directed polymerase-evolution experiment yields variants endowed with RNA-dependent DNA polymerization. To further estimate the fidelity during reverse transcription, the variants A608T/E520G/W827R, M747K/E742K, and M761T/D547G/I584V are used to copy a part of messenger RNA(mRNA) into complementary DNA (cDNA) prior to subcloning for sequencing of reverse transcription products. The sequences showsd that selected variants can polymerize more than 300 nucleotides and are not limited to the addition of single nucleotides at the 3 end of DNA primers. The substitution rates per base for RNA-dependent DNA polymerization of the most active variants, A608T/E520G/W827R and M747K/E742K are similar or lower than that of avian myeloblastosis virus reverse transcriptase, which is used as a standard. The most abundant variant and M761T/D547G/I584V has a fidelity which is about 10-times higher than that of avian myeloblastosis virus reverse transcriptase
N483Q/S486Q/T539N/Y545Q/D547T/P548Q/A570Q/D578Q/A597T/W604R/S612N/V730L/R736Q/S739N/M747R
-
selection of a polymerase with 15 mutations, mostly located at the template binding interface, by directed evolution of Thermus aquaticus DNA polymerase I, the mutant enzyme is a single variant of the Stoffel fragment of Taq DNA polymerase I, the enzyme shows broad template specificity and is a thermostable DNA-dependent and RNA-dependent DNA-polymerase, see also EC 2.7.7.7
additional information
-
chimeric DNA polymerase, termed CS5 pol, constructed from T. Z05 pol and Tma pol and containing the 5'-3' nuclease domain from Thermussp. Z05 DNA polymerase (residues 1-291) and the 3'-5' exonuclease and polymerase domains from Thermotoga maritima DNA polymerase (residues 292-893). This chimera retains thermostable DNA polymerase activity, as well as proofreading activity. Using the CS5 chimera, a series of mutant proteins is constructed in which the amino acid side chains are mutated to modulate the 3'-5' exonuclease activity. A thermoactive and thermostable enzyme with reverse transcriptase and 3'-5'?exonuclease activity is described
additional information
Thermus sp. Z05
-
chimeric DNA polymerase, termed CS5 pol, constructed from T. Z05 pol and Tma pol and containing the 5'-3' nuclease domain from Thermussp. Z05 DNA polymerase (residues 1-291) and the 3'-5' exonuclease and polymerase domains from Thermotoga maritima DNA polymerase (residues 292-893). This chimera retains thermostable DNA polymerase activity, as well as proofreading activity. Using the CS5 chimera, a series of mutant proteins is constructed in which the amino acid side chains are mutated to modulate the 3'-5' exonuclease activity. A thermoactive and thermostable enzyme with reverse transcriptase and 3'-5'?exonuclease activity is described
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
synthesis
-
reverse transcriptase is commonly used to synthesize DNA complementary to a variety of RNA templates, synthesis of cDNA. Reverse transcriptase can utilize single-stranded DNA or RNA-DNA hybrid as template to synthesize double-stranded DNA. The reverse transcriptase, unlike the bacterial DNA polymerase, lacks the 3'-5' and 5'-3' exonuclease and can thus be efficiently used for end labeling or gap filling
medicine
-
gene inhibition causing reduction of telomerase reverse transcriptase activity may provide a basis for cancer therapeutics
medicine
-
telomerase is a universal tumor antigen
medicine
-
target in HIV therapy
medicine
-
telomerase activity in exfoliated/disseminated epithelial cells can be used as a reliable marker for gastrointestinal cancers
drug development
-
the enzyme is a drug target
drug development
-
the enzyme is a primary target in the development of antiviral agents against HIV-1
drug development
AF324493, Q8Q2U5, Q8Q2V9
HIV-1 reverse transcriptase is a major target of antiviral therapy; HIV-1 reverse transcriptase is a major target of antiviral therapy; HIV-1 reverse transcriptase is a major target of antiviral therapy
medicine
-
the recombinant group O enzyme should be useful for studies aimed at discovering and designing drugs directed towards group O isolates of HIV-1
medicine
-
the modified vector system harboring the viral DNA polymerase mutant with reduced dNTP binding affinity can be a potential gene delivery system for the specific transduction of cells with high dNTP concentrations, such as tumor cells.The identification and use of unique cellular and virological factors essential for the specificity of viral based vectors can contribute to the development of safe and effective gene delivery tools
medicine
-
combination therapy consisting of nucleoside reverse-transcriptase together with non-nucleoside reverse-transcriptase inhibitors or protease inhibitors leads to a suppression of viral replication
medicine
AF324493, Q8Q2U5, Q8Q2V9
HIV-1 reverse transcriptase is a major target of antiviral therapy; HIV-1 reverse transcriptase is a major target of antiviral therapy; HIV-1 reverse transcriptase is a major target of antiviral therapy
drug development
Human immunodeficiency virus 1 BG05
-
HIV-1 reverse transcriptase is a major target of antiviral therapy
-
medicine
Human immunodeficiency virus 1 BG05
-
HIV-1 reverse transcriptase is a major target of antiviral therapy
-
drug development
Human immunodeficiency virus 1 M01
-
HIV-1 reverse transcriptase is a major target of antiviral therapy
-
medicine
Human immunodeficiency virus 1 M01
-
HIV-1 reverse transcriptase is a major target of antiviral therapy
-
synthesis
-
reverse transcriptase is commonly used to synthesize DNA complementary to a variety of RNA templates, synthesis of cDNA. Reverse transcriptase can utilize single-stranded DNA or RNA-DNA hybrid as template to synthesize double-stranded DNA. The reverse transcriptase, unlike the bacterial DNA polymerase, lacks the 3'-5' and 5'-3' exonuclease and can thus be efficiently used for end labeling or gap filling
analysis
-
the laser capture microdissection microscopycombined with multiplex quantitative real-time reverse transcriptase PCR, LCMM/qRTPCR, technique can be used to resolve and quantify GFP mRNA variability at high spatial resolution, the method is useful for quantification of any gene expressed by bacteria in their native environment, method development, overview
synthesis
-
reverse transcriptase is commonly used to synthesize DNA complementary to a variety of RNA templates, synthesis of cDNA. Reverse transcriptase can utilize single-stranded DNA or RNA-DNA hybrid as template to synthesize double-stranded DNA. The reverse transcriptase, unlike the bacterial DNA polymerase, lacks the 3'-5' and 5'-3' exonuclease and can thus be efficiently used for end labeling or gap filling