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
LITERATURE
deoxynucleoside triphosphate + DNAn = diphosphate + DNAn+1
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
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
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
-
-
HIV-1 reverse transcriptase
Human immunodeficiency virus 1 M01
-
-
HIV-1 RT
Human immunodeficiency virus 1 BG05
-
-
HIV-1 RT
Human immunodeficiency virus 1 M01
-
-
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
-
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
-
telomerase reverse transcriptase
-
catalytic subunit of telomerase
telomerase reverse transcriptase
-
-
telomerase reverse transcriptase
-
-
telomerase reverse transcriptase
-
-
TERT
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
-
XMRV RT
Xenotropic MLV-related virus
-
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
UNIPROT
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
Clostridium stercorarium
-
-
-
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
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
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
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
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'-deoxycytidine 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-beta-D-ribofuranosyl 5'-triphosphate + DNAn
diphosphate + ?
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-beta-D-ribofuranosyl 5'-triphosphate + DNAn
diphosphate + ?
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-beta-D-ribofuranosyl 5'-triphosphate + DNAn
diphosphate + ?
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-beta-D-ribofuranosyl 5'-triphosphate + DNAn
diphosphate + ?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
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
-
-
?
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
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 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
poly(rA)noligo(dT)12-18
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
show the reaction diagram
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
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
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
-
-
?
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
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
-
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
-
-
?
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
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
-
-
?
dTTP + DNAn
diphosphate + DNAn+1
show the reaction diagram
Human immunodeficiency virus 1 BG05
-
-
?
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
-
-
-
-
-
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
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
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
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
-
-
-
?
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
-
-
-
?
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
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
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
COMMENTARY
LITERATURE
IMAGE
((1s,3s)-3-(7-amino-2H-2,3,5,6-tetraazabenzo[cd]azulen-2-yl)cyclobutyl)methyl tetrahydrogen triphosphate
-
-
(+)-Calanolide A
-
-
(-)-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
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'-dideoxy-CTP
-
-
2',3'-dideoxycytidine
-
-
2',3'-dideoxyguanosine triphosphate
-
-
2',3'-dideoxyinosine
-
-
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-3'-azido-2',3'-dideoxy-N,N-dimethyladenosine 5'-triphosphate
-
-
2-amino-4-(3-benzoylphenyl)thiazole-5-carboxamide
-
2-amino-4-(3-bromo-4-chlorophenyl)thiazole-5-carboxamide
-
2-amino-4-(3-chlorophenyl)thiazole-5-carboxamide
-
2-amino-4-(3-iodophenyl)thiazole-5-carboxamide
-
2-amino-4-(3-phenylphenyl)thiazole-5-carboxamide
-
2-amino-4-phenylthiazole-5-carboxamide
-
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-beta-D-ribofuranosyl 5'-triphosphate
-
-
3'-azido-2',3'-dideoxy-2-amino-6-chloropurine-beta-D-ribofuranosyl 5'-triphosphate
-
-
3'-azido-2',3'-dideoxy-2-amino-6-methoxypurine-beta-D-ribofuranosyl 5'-triphosphate
-
-
3'-azido-2',3'-dideoxy-2-amino-6-N-allylaminopurine-beta-D-ribofuranosyl 5'-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-2',3'-dideoxythymidine-5'-triphosphate
-
-
3'-azido-3'-deoxythymidine
-
-
3'-azido-3'-deoxythymidine
-
-
3'-azido-3'-deoxythymidine
Xenotropic MLV-related virus
-
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
-
3-(3-chlorophenyl)-3-oxopropanenitrile
-
3-(3-iodophenyl)-3-oxopropanamide
-
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
-
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
-
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
-
-
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
-
-
4-(3-benzoylphenyl)thiazole-5-carboxamide
-
4-(3-bromo-4-chlorophenyl)-1H-imidazole-5-carboxamide
-
4-(3-bromo-4-chlorophenyl)thiazole-5-carboxamide
-
4-(3-chlorophenyl)-1H-imidazole-5-carboxamide
-
4-(3-iodophenyl)-3-oxobutanenitrile
-
4-amino-5-fluoro-1-[(2R,5S)-2-(hydroxymethyl)-1,3-oxathiolan-5-yl]pyrimidin-2-one
-
-
4-phenyl-1H-imidazole-5-carboxamide
-
4-phenylthiazole-5-carboxamide
-
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
9-aminonevirapine
-
-
adefovir diphosphate
-
-
adefovir diphosphate
Xenotropic MLV-related virus
-
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
d4T-Monophosphate
-
-
dATP
-
replacement of dATP by ATP completely prevents synthesis
ddATP
-
competitive with respect to dATP, noncompetitive with respect to dCTP, dGTP and dTTP
ddATP
-
0.28 mM
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
-
Dioxolan Thymidine
-
-
early growth response-1
-
overexpressio nof early growth response-1 decreases TERT protein production as well TERT mRNA transcription
-
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
KCl
-
IC50: 40-50 mM
lamivudine
-
-
lamivudine triphosphate
-
-
-
lamivudine triphosphate
-
-
-
lamivudine triphosphate
Xenotropic MLV-related virus
-
-
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
NF 345
-
IC50: 7 mg/ml
NF 346
-
IC50: 5 mg/ml
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
suramin
-
IC50: 4 mg/ml
Tenofovir
-
9-[(2-phosphonomethoxy)propyl]adenine
Tenofovir
Xenotropic MLV-related virus
-
tenofovir diphosphate
-
-
tenofovir diphosphate
Xenotropic MLV-related virus
-
tenofovir diphosphate
-
-
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
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
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]
SUBSTRATE
ORGANISM
UNIPROT
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
0.028
2'-deoxyguanosine 5'-triphosphate
-
at 37C
0.0046
2'-deoxythymidine 5'-triphosphate
-
at 37C
0.00029
3'-azido-2',3'-dideoxy-2,6-diaminopurine-beta-D-ribofuranosyl 5'-triphosphate
-
pH 7.5, 37C, wild-type enzyme
0.034
3'-azido-2',3'-dideoxy-2,6-diaminopurine-beta-D-ribofuranosyl 5'-triphosphate
-
pH 7.5, 37C, wild-type enzyme
0.00092
3'-azido-2',3'-dideoxy-2-amino-6-chloropurine-beta-D-ribofuranosyl 5'-triphosphate
-
pH 7.5, 37C, wild-type enzyme
0.0018
3'-azido-2',3'-dideoxy-2-amino-6-chloropurine-beta-D-ribofuranosyl 5'-triphosphate
-
pH 7.5, 37C, wild-type enzyme
0.012
3'-azido-2',3'-dideoxy-2-amino-6-methoxypurine-beta-D-ribofuranosyl 5'-triphosphate
-
pH 7.5, 37C, wild-type enzyme
0.0163
3'-azido-2',3'-dideoxy-2-amino-6-methoxypurine-beta-D-ribofuranosyl 5'-triphosphate
-
pH 7.5, 37C, wild-type enzyme
0.0048
3'-azido-2',3'-dideoxy-2-amino-6-N-allylaminopurine-beta-D-ribofuranosyl 5'-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
0.00148
dCTP
-
-
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
0.00035
deoxy-5'-CTP
-
at 37C
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
0.00255
dTTP
-
-
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
mutant enzyme Q84A
0.01137
dTTP
mutant enzyme Q84A
0.01294
dTTP
mutant enzyme F155H
0.01304
dTTP
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
mutant enzyme Q84A
-
0.01171
poly(rA)/(dT)18
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
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.042
(-)-beta-2',3'-dideoxy-3'-thiacytidine triphosphate
Human immunodeficiency virus 1
-
mutant enzyme Y1152-naphthyl-Tyr
0.15
(-)-beta-2',3'-dideoxy-3'-thiacytidine triphosphate
Human immunodeficiency virus 1
-
wild-type enzyme
0.16
(-)-beta-2',3'-dideoxy-3'-thiacytidine triphosphate
Human immunodeficiency virus 1
-
mutant enzyme Y115aminomethyl-Phe
0.077
2',3'-dideoxy-CTP
Human immunodeficiency virus 1
-
mutant enzyme Y1152-naphthyl-Tyr
0.49
2',3'-dideoxy-CTP
Human immunodeficiency virus 1
-
mutant enzyme Y115aminomethyl-Phe
0.67
2',3'-dideoxy-CTP
Human immunodeficiency virus 1
-
wild-type enzyme
0.0265
2'-deoxyadenosine 5'-triphosphate
Streptococcus agalactiae
-
at 37C
1.33
2'-deoxyguanosine 5'-triphosphate
Streptococcus agalactiae
-
at 37C
0.034
2'-deoxythymidine 5'-triphosphate
Streptococcus agalactiae
-
at 37C
0.16
3'-azido-2',3'-dideoxy-2,6-diaminopurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
14
3'-azido-2',3'-dideoxy-2,6-diaminopurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
0.37
3'-azido-2',3'-dideoxy-2-amino-6-chloropurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
2.7
3'-azido-2',3'-dideoxy-2-amino-6-chloropurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
0.22
3'-azido-2',3'-dideoxy-2-amino-6-methoxypurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
2.8
3'-azido-2',3'-dideoxy-2-amino-6-methoxypurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
2.1
3'-azido-2',3'-dideoxy-2-amino-6-N-allylaminopurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
14
3'-azido-2',3'-dideoxyadenosine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
0.042
borano-3TCTP
Human immunodeficiency virus 1
-
mutant enzyme Y1152-naphthyl-Tyr
0.15
borano-3TCTP
Human immunodeficiency virus 1
-
wild-type enzyme
0.16
borano-3TCTP
Human immunodeficiency virus 1
-
mutant enzyme Y115aminomethyl-Phe
0.00075
dATP
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.18
dATP
feline leukemia virus
-
-
0.21
dATP
feline immunodeficiency virus
-
-
0.25
dATP
Thermus aquaticus
-
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
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication, wild-type enzyme
17
dATP
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
0.000083
dCTP
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.15
dCTP
feline leukemia virus
-
-
0.22
dCTP
feline immunodeficiency virus
-
-
0.76
dCTP
Human immunodeficiency virus 1
-
mutant enzyme Y115aminomethyl-Phe
0.83
dCTP
Thermus aquaticus
-
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
Human immunodeficiency virus 1
-
wild-type enzyme
1.64
dCTP
Human immunodeficiency virus 1
-
wild-type enzyme
0.0117
deoxy-5'-CTP
Streptococcus agalactiae
-
at 37C
3
deoxynucleoside triphosphate
Simian 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
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
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.51
dGTP
feline immunodeficiency virus
-
-
0.56
dGTP
feline leukemia virus
-
-
17.3
dGTP
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
0.35
DNAn
Human immunodeficiency virus 1
-
pH 8.3, 25C, recombinant enzyme, HIV-1 M RT
1.1
DNAn
Human immunodeficiency virus 1
-
pH 8.3, 25C, recombinant enzyme, HIV-1 O RT
29
DNAn
Moloney murine leukemia virus
-
pH 8.3, 25C, recombinant enzyme
29
DNAn
Moloney murine leukemia virus
-
pH 8.2, 37C, recombinant enzyme, substrate is poly(rA)-p(dT)45
0.17
dTTP
feline leukemia virus
-
-
0.28
dTTP
feline immunodeficiency virus
-
-
0.29
dTTP
Human immunodeficiency virus 1
-
pH 8.0, 37C, reaction with poly(rA)*oligo(dT)20, enzyme from group O
0.35
dTTP
Human immunodeficiency virus 1
-
pH 8.3, 25C, recombinant enzyme, HIV-1 M RT
0.47
dTTP
Human immunodeficiency virus 1
-
pH 8.0, 37C, reaction with poly(rA)*oligo(dT)20, enzyme from group M
0.67
dTTP
Thermus aquaticus
-
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
Human immunodeficiency virus 1
-
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
Simian 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
29
dTTP
Moloney murine leukemia virus
-
pH 8.3, 25C, recombinant enzyme
0.07
N-cyclobutyladenosine-phosphonyl diphosphate
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication, wild-type enzyme
-
0.15
tenofovir diphosphate
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication, wild-type enzyme
35
dTTP
Moloney murine leukemia virus
-
pH 8.2, 37C, recombinant enzyme
additional information
additional information
Human immunodeficiency virus 1
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000005
3'-azido-2',3'-dideoxy-2,6-diaminopurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
7061
0.048
3'-azido-2',3'-dideoxy-2,6-diaminopurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
7061
0.000402
3'-azido-2',3'-dideoxy-2-amino-6-chloropurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
7062
0.0015
3'-azido-2',3'-dideoxy-2-amino-6-chloropurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
7062
0.000013
3'-azido-2',3'-dideoxy-2-amino-6-methoxypurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
7063
0.00023
3'-azido-2',3'-dideoxy-2-amino-6-methoxypurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
7063
0.00044
3'-azido-2',3'-dideoxy-2-amino-6-N-allylaminopurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
8956
0.044
3'-azido-2',3'-dideoxyadenosine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
8955
0.052
dATP
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
140
2.5
dATP
Thermus aquaticus
-
pH 9.0, 37C, recombinant mutant enzyme N483Q/S486Q/T539N/Y545Q/D547T/P548Q/A570Q/D578Q/A597T/W604R/S612N/V730L/R736Q/S739N/M747R
140
5.15
dATP
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication, wild-type enzyme
140
4.9
dCTP
Thermus aquaticus
-
pH 9.0, 37C, recombinant mutant enzyme N483Q/S486Q/T539N/Y545Q/D547T/P548Q/A570Q/D578Q/A597T/W604R/S612N/V730L/R736Q/S739N/M747R
179
0.00102
dGTP
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
219
1.8
dTTP
Thermus aquaticus
-
pH 9.0, 37C, recombinant mutant enzyme N483Q/S486Q/T539N/Y545Q/D547T/P548Q/A570Q/D578Q/A597T/W604R/S612N/V730L/R736Q/S739N/M747R
145
14.89
N-cyclobutyladenosine-phosphonyl diphosphate
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication, wild-type enzyme
28914
7.16
p-tRNAHis
Saccharomyces cerevisiae
-
pH 7.5, 22C
8913
4.36
ppp-tRNAHis
Saccharomyces cerevisiae
-
pH 7.5, 22C, mutant enzyme D68A
19390
5.58
ppp-tRNAHis
Saccharomyces cerevisiae
-
pH 7.5, 22C, wild-type enzyme
19390
0.039
ppp-tRNALeu
Saccharomyces cerevisiae
-
pH 7.5, 22C, mutant enzyme D68A
41329
0.0048
ppp-tRNAPhe
Saccharomyces cerevisiae
-
pH 7.5, 22C, wild-type enzyme
19389
0.42
ppp-tRNAPhe
Saccharomyces cerevisiae
-
pH 7.5, 22C, mutant enzyme D68A
19389
60.6
tenofovir diphosphate
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication, wild-type enzyme
5424
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
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
0.0000029
3'-Azido-2',3'-dideoxythymidine 5'-triphosphate
-
pH 8.0, 37C, reaction with poly(rA)*oligo(dT)20, group O enzyme
0.0000063
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
-
-
0.0000059
ddTTP
-
pH 8.0, 37C, reaction with poly(rA)*oligo(dT)20, group O enzyme
0.000014
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]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00003
1,10-di-2',3'-dideoxy-3'-thiacytidine-decanoate
Human immunodeficiency virus 1
-
enzyme from HIV-1 III B, pH and temperature not specified in the publication
-
0.00006
1,10-di-2',3'-dideoxy-3'-thiacytidine-decanoate
Human immunodeficiency virus 1
-
enzyme from HIV-1 US/92/727, pH and temperature not specified in the publication
-
0.000004
1,10-di-3'-azido-2',3'-dideoxythymidine-decanoate
Human immunodeficiency virus 1
-
enzyme from HIV-1 US/92/727, pH and temperature not specified in the publication
-
0.000005
1,10-di-3'-azido-2',3'-dideoxythymidine-decanoate
Human immunodeficiency virus 1
-
enzyme from HIV-1 III B, pH and temperature not specified in the publication
-
0.000001
1,10-di-3'-fluoro-2',3'-dideoxythymidine-decanoate
Human immunodeficiency virus 1
-
enzyme from HIV-1 US/92/727, pH and temperature not specified in the publication
-
0.000004
1,10-di-3'-fluoro-2',3'-dideoxythymidine-decanoate
Human immunodeficiency virus 1
-
enzyme from HIV-1 III B, pH and temperature not specified in the publication
-
0.000009
1,12-di-2',3'-dideoxy-3'-thiacytidine-dodecanoate
Human immunodeficiency virus 1
-
enzyme from HIV-1 III B, pH and temperature not specified in the publication
-
0.00002
1,12-di-2',3'-dideoxy-3'-thiacytidine-dodecanoate
Human immunodeficiency virus 1
-
enzyme from HIV-1 US/92/727, pH and temperature not specified in the publication
-
0.000002
1,12-di-3'-azido-2',3'-dideoxythymidine-dodecanoate
Human immunodeficiency virus 1
-
enzyme from HIV-1 US/92/727, pH and temperature not specified in the publication
-
0.000004
1,12-di-3'-azido-2',3'-dideoxythymidine-dodecanoate
Human immunodeficiency virus 1
-
enzyme from HIV-1 III B, pH and temperature not specified in the publication
-
0.00000097
1,12-di-3'-fluoro-2',3'-dideoxythymidine-dodecanoate
Human immunodeficiency virus 1
-
enzyme from HIV-1 US/92/727, pH and temperature not specified in the publication
-
0.000004
1,12-di-3'-fluoro-2',3'-dideoxythymidine-dodecanoate
Human immunodeficiency virus 1
-
enzyme from HIV-1 III B, pH and temperature not specified in the publication
-
0.000003
1,14-di-2',3'-dideoxy-3'-thiacytidine-tetradecanoate
Human immunodeficiency virus 1
-
enzyme from HIV-1 III B, pH and temperature not specified in the publication
-
0.00003
1,14-di-2',3'-dideoxy-3'-thiacytidine-tetradecanoate
Human immunodeficiency virus 1
-
enzyme from HIV-1 US/92/727, pH and temperature not specified in the publication
-
0.000003
1,14-di-3'-azido-2',3'-dideoxythymidine-tetradecanoate
Human immunodeficiency virus 1
-
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
-
0.00000076
1,14-di-3'-fluoro-2',3'-dideoxythymidine-tetradecanoate
Human immunodeficiency virus 1
-
enzyme from HIV-1 US/92/727, pH and temperature not specified in the publication
-
0.000003
1,14-di-3'-fluoro-2',3'-dideoxythymidine-tetradecanoate
Human immunodeficiency virus 1
-
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
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.1
1,2-bis[(3-oxobutan-2-yl)oxy]anthracene-9,10-dione
Human immunodeficiency virus 1
-
above, pH and temperature not specified in the publication
0.00013
1,4-di-2',3'-dideoxy-3'-thiacytidine-succinate
Human immunodeficiency virus 1
-
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
Human immunodeficiency virus 1
-
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
Moloney murine leukemia virus
-
pH 7.8, 37C
-
0.00009
2',3'-dideoxy-3'-thiacytidine
Human immunodeficiency virus 1
-
enzyme from HIV-1 US/92/727, pH and temperature not specified in the publication
-
0.0002
2',3'-dideoxy-3'-thiacytidine
Human immunodeficiency virus 1
-
enzyme from HIV-1 III B, pH and temperature not specified in the publication
-
0.00224
2',3'-dideoxy-CTP
Human immunodeficiency virus 1
-
-
0.0234
2-amino-3'-azido-2',3'-dideoxy-N,N-dimethyladenosine 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
0.05
2-amino-3'-azido-2',3'-dideoxy-N,N-dimethyladenosine 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant K65R; pH 7.5, 37C, mutant L74V; pH 7.5, 37C, mutant Q151M
0.0441
2-amino-4-(3-benzoylphenyl)thiazole-5-carboxamide
Human immunodeficiency virus 1
P04585
-
0.118
2-amino-4-(3-bromo-4-chlorophenyl)thiazole-5-carboxamide
Human immunodeficiency virus 1
P04585
-
0.0544
2-amino-4-(3-chlorophenyl)thiazole-5-carboxamide
Human immunodeficiency virus 1
P04585
-
0.1254
2-amino-4-(3-iodophenyl)thiazole-5-carboxamide
Human immunodeficiency virus 1
P04585
-
0.0592
2-amino-4-(3-phenylphenyl)thiazole-5-carboxamide
Human immunodeficiency virus 1
P04585
-
0.0807
2-amino-4-phenylthiazole-5-carboxamide
Human immunodeficiency virus 1
P04585
-
0.005
2-[2-(4-bromophenyl)-2-oxoethoxy]-9,10-dioxo-9,10-dihydroanthracen-1-yl acetate
Human immunodeficiency virus 1
-
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
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.00034
3'-azido-2',3'-dideoxy-2,6-diaminopurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant M184V
0.0008
3'-azido-2',3'-dideoxy-2,6-diaminopurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
0.0013
3'-azido-2',3'-dideoxy-2,6-diaminopurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant L74V
0.0025
3'-azido-2',3'-dideoxy-2,6-diaminopurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant K65R
0.0042
3'-azido-2',3'-dideoxy-2,6-diaminopurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant Q151M
0.0025
3'-azido-2',3'-dideoxy-2-amino-6-chloropurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant M184V
0.0032
3'-azido-2',3'-dideoxy-2-amino-6-chloropurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
0.0091
3'-azido-2',3'-dideoxy-2-amino-6-chloropurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant K65R
0.0118
3'-azido-2',3'-dideoxy-2-amino-6-chloropurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant L74V
0.0308
3'-azido-2',3'-dideoxy-2-amino-6-chloropurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant Q151M
0.0244
3'-azido-2',3'-dideoxy-2-amino-6-methoxypurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
0.0329
3'-azido-2',3'-dideoxy-2-amino-6-methoxypurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant M184V
0.078
3'-azido-2',3'-dideoxy-2-amino-6-methoxypurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant Q151M
0.08
3'-azido-2',3'-dideoxy-2-amino-6-methoxypurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant K65R
0.1
3'-azido-2',3'-dideoxy-2-amino-6-methoxypurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant L74V
0.0041
3'-azido-2',3'-dideoxy-2-amino-6-N-allylaminopurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
0.0048
3'-azido-2',3'-dideoxy-2-amino-6-N-allylaminopurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant M184V
0.0088
3'-azido-2',3'-dideoxy-2-amino-6-N-allylaminopurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant K65R
0.0103
3'-azido-2',3'-dideoxy-2-amino-6-N-allylaminopurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant L74V
0.0218
3'-azido-2',3'-dideoxy-2-amino-6-N-allylaminopurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant Q151M
0.00016
3'-azido-2',3'-dideoxyadenosine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
0.00019
3'-azido-2',3'-dideoxyadenosine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant M184V
0.00042
3'-azido-2',3'-dideoxyadenosine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant L74V
0.0007
3'-azido-2',3'-dideoxyadenosine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant K65R
0.0014
3'-azido-2',3'-dideoxyadenosine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant Q151M
0.00006
3'-azido-2',3'-dideoxyguanosine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant M184V
0.00015
3'-azido-2',3'-dideoxyguanosine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
0.00025
3'-azido-2',3'-dideoxyguanosine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant L74V
0.0003
3'-azido-2',3'-dideoxyguanosine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant Q151M
0.00036
3'-azido-2',3'-dideoxyguanosine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant K65R
0.000002
3'-azido-2',3'-dideoxythymidine
Human immunodeficiency virus 1
-
enzyme from HIV-1 III B, pH and temperature not specified in the publication
0.000008
3'-azido-2',3'-dideoxythymidine
Human immunodeficiency virus 1
-
enzyme from HIV-1 US/92/727, pH and temperature not specified in the publication
0.00002
3'-azido-2',3'-dideoxythymidine-5'-triphosphate
Human immunodeficiency virus 1
-
mutant enzyme I132A
0.00003
3'-azido-2',3'-dideoxythymidine-5'-triphosphate
Human immunodeficiency virus 1
-
mutant enzyme E138A; mutant enzyme I132M
0.00004
3'-azido-2',3'-dideoxythymidine-5'-triphosphate
Human immunodeficiency virus 1
-
mutant enzyme I135A
0.00006
3'-azido-2',3'-dideoxythymidine-5'-triphosphate
Human immunodeficiency virus 1
-
mutant enzyme I135M; mutant enzyme N137A; mutant enzyme T139V; wild-type enzyme
0.00007
3'-azido-2',3'-dideoxythymidine-5'-triphosphate
Human immunodeficiency virus 1
-
mutant enzyme E138K
0.042
3'-azido-3'deoxythymidine 5'-triphosphate
feline immunodeficiency virus
-
IC50: 0.042 mM
0.06
3'-azido-3'deoxythymidine 5'-triphosphate
feline leukemia virus
-
IC50: 0.06 mM
0.00006
3'-dideoxythymidine triphosphate
Human immunodeficiency virus 1
-
mutant enzyme I132M
-
0.00007
3'-dideoxythymidine triphosphate
Human immunodeficiency virus 1
-
mutant enzyme I132A
-
0.00008
3'-dideoxythymidine triphosphate
Human immunodeficiency virus 1
-
mutant enzyme I135A
-
0.00009
3'-dideoxythymidine triphosphate
Human immunodeficiency virus 1
-
mutant enzyme E138A; mutant enzyme I135M
-
0.0001
3'-dideoxythymidine triphosphate
Human immunodeficiency virus 1
-
mutant enzyme E138K; mutant enzyme N137A; mutant enzyme T139V; wild-type enzyme
-
0.000002
3'-fluoro-2',3'-dideoxythymidine
Human immunodeficiency virus 1
-
enzyme from HIV-1 US/92/727, pH and temperature not specified in the publication
0.00002
3'-fluoro-2',3'-dideoxythymidine
Human immunodeficiency virus 1
-
enzyme from HIV-1 III B, pH and temperature not specified in the publication
0.0643
3-(2-cyanoacetyl)phenyl diethyl phosphate
Human immunodeficiency virus 1
P04585
-
0.0041
3-(3-chlorophenyl)-3-oxopropanenitrile
Human immunodeficiency virus 1
P04585
-
0.0296
3-(3-iodophenyl)-3-oxopropanamide
Human immunodeficiency virus 1
P04585
-
0.000008
3-([3-bromo-2-oxo-5-[(pyridin-3-yloxy)methyl]-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
Human immunodeficiency virus 1
-
mutant Y181C, pH and temperature not specified in the publication
0.000011
3-([3-bromo-2-oxo-5-[(pyridin-3-yloxy)methyl]-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
Human immunodeficiency virus 1
-
wild-type enzyme, pH and temperature not specified in the publication
0.000016
3-([3-bromo-2-oxo-5-[(pyridin-3-yloxy)methyl]-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
Human immunodeficiency virus 1
-
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
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000008
3-([3-bromo-2-oxo-5-[(pyridin-4-yloxy)methyl]-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
Human immunodeficiency virus 1
-
mutant Y181C, pH and temperature not specified in the publication
0.00001
3-([3-bromo-2-oxo-5-[(pyridin-4-yloxy)methyl]-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
Human immunodeficiency virus 1
-
wild-type enzyme, pH and temperature not specified in the publication
0.000014
3-([3-bromo-2-oxo-5-[(pyridin-4-yloxy)methyl]-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
Human immunodeficiency virus 1
-
mutant K103N, pH and temperature not specified in the publication
0.000001
3-([3-bromo-5-fluoro-2-oxo-6-[2-(pyridin-4-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
Human immunodeficiency virus 1
-
mutant K103N, pH and temperature not specified in the publication; mutant Y181C, pH and temperature not specified in the publication
0.000002
3-([3-bromo-5-fluoro-2-oxo-6-[2-(pyridin-4-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
Human immunodeficiency virus 1
-
wild-type enzyme, pH and temperature not specified in the publication
0.000008
3-([3-bromo-6-[2-(3-chlorophenyl)ethyl]-5-fluoro-2-oxo-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
Human immunodeficiency virus 1
-
mutant K103N, pH and temperature not specified in the publication; mutant Y181C, pH and temperature not specified in the publication
0.000017
3-([3-bromo-6-[2-(3-chlorophenyl)ethyl]-5-fluoro-2-oxo-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
Human immunodeficiency virus 1
-
wild-type enzyme, pH and temperature not specified in the publication
0.000004
3-([6-[2-(1,3-benzoxazol-2-yl)ethyl]-3-chloro-2-oxo-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
Human immunodeficiency virus 1
-
mutant Y181C, pH and temperature not specified in the publication
0.000006
3-([6-[2-(1,3-benzoxazol-2-yl)ethyl]-3-chloro-2-oxo-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
Human immunodeficiency virus 1
-
wild-type enzyme, pH and temperature not specified in the publication
0.000016
3-([6-[2-(1,3-benzoxazol-2-yl)ethyl]-3-chloro-2-oxo-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
Human immunodeficiency virus 1
-
mutant K103N, pH and temperature not specified in the publication
0.0098
3-benzoyl-3-oxopropanenitrile
Human immunodeficiency virus 1
P04585
-
0.000021
3-chloro-5-([3-chloro-2-oxo-6-[2-(pyridin-2-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
Human immunodeficiency virus 1
-
wild-type enzyme, pH and temperature not specified in the publication
0.000033
3-chloro-5-([3-chloro-2-oxo-6-[2-(pyridin-2-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
Human immunodeficiency virus 1
-
mutant Y181C, pH and temperature not specified in the publication
0.000078
3-chloro-5-([3-chloro-2-oxo-6-[2-(pyridin-2-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
Human immunodeficiency virus 1
-
mutant K103N, pH and temperature not specified in the publication
0.000016
3-chloro-5-([3-chloro-2-oxo-6-[2-(pyridin-3-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
Human immunodeficiency virus 1
-
mutant K103N, pH and temperature not specified in the publication
0.000022
3-chloro-5-([3-chloro-2-oxo-6-[2-(pyridin-3-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
Human immunodeficiency virus 1
-
mutant Y181C, pH and temperature not specified in the publication; wild-type enzyme, pH and temperature not specified in the publication
0.000014
3-chloro-5-([3-chloro-2-oxo-6-[2-(pyridin-4-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
Human immunodeficiency virus 1
-
mutant K103N, pH and temperature not specified in the publication
0.000019
3-chloro-5-([3-chloro-2-oxo-6-[2-(pyridin-4-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
Human immunodeficiency virus 1
-
wild-type enzyme, pH and temperature not specified in the publication
0.000021
3-chloro-5-([3-chloro-2-oxo-6-[2-(pyridin-4-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
Human immunodeficiency virus 1
-
mutant Y181C, pH and temperature not specified in the publication
0.000002
3-chloro-5-([3-chloro-6-methyl-2-oxo-5-[2-(pyridin-3-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
Human immunodeficiency virus 1
-
mutant K103N, pH and temperature not specified in the publication
0.000003
3-chloro-5-([3-chloro-6-methyl-2-oxo-5-[2-(pyridin-3-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
Human immunodeficiency virus 1
-
mutant Y181C, pH and temperature not specified in the publication
0.000004
3-chloro-5-([3-chloro-6-methyl-2-oxo-5-[2-(pyridin-3-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
Human immunodeficiency virus 1
-
wild-type enzyme, pH and temperature not specified in the publication
0.00003
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
Human immunodeficiency virus 1
-
wild-type enzyme, pH and temperature not specified in the publication
0.000006
3-chloro-5-([3-chloro-6-[2-(3-chlorophenyl)ethyl]-2-oxo-1,2-dihydropyridin-4-yl]oxy)benzonitrile
Human immunodeficiency virus 1
-
mutant K103N, pH and temperature not specified in the publication
0.000007
3-chloro-5-([3-chloro-6-[2-(3-chlorophenyl)ethyl]-2-oxo-1,2-dihydropyridin-4-yl]oxy)benzonitrile
Human immunodeficiency virus 1
-
mutant Y181C, pH and temperature not specified in the publication
0.000012
3-chloro-5-([3-chloro-6-[2-(3-chlorophenyl)ethyl]-2-oxo-1,2-dihydropyridin-4-yl]oxy)benzonitrile
Human immunodeficiency virus 1
-
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
Human immunodeficiency virus 1
-
wild-type enzyme, pH and temperature not specified in the publication
0.000008
3-chloro-5-[[3-chloro-2-oxo-6-(2-phenylethyl)-1,2-dihydropyridin-4-yl]oxy]benzonitrile
Human immunodeficiency virus 1
-
wild-type enzyme, pH and temperature not specified in the publication
0.000007
3-chloro-5-[[3-chloro-5-fluoro-2-oxo-6-(2-phenylethyl)-1,2-dihydropyridin-4-yl]oxy]benzonitrile
Human immunodeficiency virus 1
-
wild-type enzyme, pH and temperature not specified in the publication
0.000005
3-chloro-5-[[3-chloro-6-methyl-2-oxo-5-(phenoxymethyl)-1,2-dihydropyridin-4-yl]oxy]benzonitrile
Human immunodeficiency virus 1
-
mutant K103N, pH and temperature not specified in the publication
0.000006
3-chloro-5-[[3-chloro-6-methyl-2-oxo-5-(phenoxymethyl)-1,2-dihydropyridin-4-yl]oxy]benzonitrile
Human immunodeficiency virus 1
-
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
Human immunodeficiency virus 1
P04585
-
0.000034
3-[(5-benzyl-3-bromo-2-oxo-1,2-dihydropyridin-4-yl)oxy]-5-chlorobenzonitrile
Human immunodeficiency virus 1
-
wild-type enzyme, pH and temperature not specified in the publication
0.000041
3-[(5-benzyl-3-bromo-2-oxo-1,2-dihydropyridin-4-yl)oxy]-5-chlorobenzonitrile
Human immunodeficiency virus 1
-
mutant Y181C, pH and temperature not specified in the publication
0.000071
3-[(5-benzyl-3-bromo-2-oxo-1,2-dihydropyridin-4-yl)oxy]-5-chlorobenzonitrile
Human immunodeficiency virus 1
-
mutant K103N, pH and temperature not specified in the publication
0.000007
3-[(5-benzyl-3-bromo-6-methyl-2-oxo-1,2-dihydropyridin-4-yl)oxy]-5-chlorobenzonitrile
Human immunodeficiency virus 1
-
mutant K103N, pH and temperature not specified in the publication
0.000008
3-[(5-benzyl-3-bromo-6-methyl-2-oxo-1,2-dihydropyridin-4-yl)oxy]-5-chlorobenzonitrile
Human immunodeficiency virus 1
-
mutant Y181C, pH and temperature not specified in the publication
0.00001
3-[(5-benzyl-3-bromo-6-methyl-2-oxo-1,2-dihydropyridin-4-yl)oxy]-5-chlorobenzonitrile
Human immunodeficiency virus 1
-
wild-type enzyme, pH and temperature not specified in the publication
0.000012
3-[6-bromo-3-[2-(3,4-dihydroisoquinolin-2(1H)-yl)-2-oxoethyl]-2-fluorophenoxy]-5-chlorobenzonitrile
Human immunodeficiency virus 1
-
wild-type enzyme, pH and temperature not specified in the publication
0.000011
3-[[3-bromo-2-oxo-5-(pyridin-4-ylmethoxy)-1,2-dihydropyridin-4-yl]oxy]-5-chlorobenzonitrile
Human immunodeficiency virus 1
-
mutant Y181C, pH and temperature not specified in the publication
0.000013
3-[[3-bromo-2-oxo-5-(pyridin-4-ylmethoxy)-1,2-dihydropyridin-4-yl]oxy]-5-chlorobenzonitrile
Human immunodeficiency virus 1
-
mutant K103N, pH and temperature not specified in the publication
0.000021
3-[[3-bromo-2-oxo-5-(pyridin-4-ylmethoxy)-1,2-dihydropyridin-4-yl]oxy]-5-chlorobenzonitrile
Human immunodeficiency virus 1
-
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
Moloney murine leukemia virus
-
pH 7.8, 37C
-
0.00029
4'-ethynyl-2-fluoro-2'-deoxyadenosine triphosphate
Moloney murine leukemia virus
-
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
Human immunodeficiency virus 1
P04585
-
0.0099
4-(3-bromo-4-chlorophenyl)-1H-imidazole-5-carboxamide
Human immunodeficiency virus 1
P04585
-
0.0875
4-(3-bromo-4-chlorophenyl)thiazole-5-carboxamide
Human immunodeficiency virus 1
P04585
-
0.0798
4-(3-chlorophenyl)-1H-imidazole-5-carboxamide
Human immunodeficiency virus 1
P04585
-
0.0035
4-(3-iodophenyl)-3-oxobutanenitrile
Human immunodeficiency virus 1
P04585
-
0.3
4-phenyl-1H-imidazole-5-carboxamide
Human immunodeficiency virus 1
P04585
-
0.283
4-phenylthiazole-5-carboxamide
Human immunodeficiency virus 1
P04585
-
0.018
4-[(3,5-dimethylphenyl)sulfanyl]quinolin-2(1H)-one
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.1
6-chloro-4-(2-fluorophenyl)quinolin-2(1H)-one
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.00015
6-chloro-4-(3,5-dimethylphenoxy)quinolin-2(1H)-one
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0056
6-chloro-4-(phenylsulfanyl)quinolin-2(1H)-one
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0089
6-chloro-4-(phenylsulfinyl)quinolin-2(1H)-one
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.049
6-chloro-4-(phenylsulfonyl)quinolin-2(1H)-one
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.003
6-chloro-4-phenoxyquinolin-2(1H)-one
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.1
6-chloro-4-phenylquinolin-2(1H)-one
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.00021
6-chloro-4-[(3,5-dimethylphenyl)sulfanyl]quinolin-2(1H)-one
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0026
6-chloro-4-[(3,5-dimethylphenyl)sulfinyl]quinolin-2(1H)-one
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.01
6-chloro-4-[(3,5-dimethylphenyl)sulfonyl]quinolin-2(1H)-one
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.06
9,10-dioxo-2-(2-oxo-2-phenylethoxy)-9,10-dihydroanthracen-1-yl acetate
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.1
9,10-dioxo-2-(2-oxopropoxy)-9,10-dihydroanthracen-1-yl acetate
Human immunodeficiency virus 1
-
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
Human immunodeficiency virus 1
-
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
Human immunodeficiency virus 1
-
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
Human immunodeficiency virus 1
-
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
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.1
9,10-dioxo-9,10-dihydroanthracene-1,2-diyl diacetate
Human immunodeficiency virus 1
-
above, pH and temperature not specified in the publication
0.012
9,10-dioxo-9,10-dihydroanthracene-1,2-diyl dibenzoate
Human immunodeficiency virus 1
-
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
Moloney murine leukemia virus
-
pH 7.8, 37C
0.079
alizarin
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.00134
azidothymidine triphosphate
Human immunodeficiency virus 1
-
-
0.0000054
capravirine
Human immunodeficiency virus 1
-
mutant enzyme K103N
0.0000086
capravirine
Human immunodeficiency virus 1
-
wild-type enzyme
0.0000112
capravirine
Human immunodeficiency virus 1
-
mutant enzyme K103N/Y181C
0.0000183
capravirine
Human immunodeficiency virus 1
-
mutant enzyme Y181C
0.000411
capravirine
Human immunodeficiency virus 1
-
mutant enzyme Y188L
0.00012
d4T-TP
Human immunodeficiency virus 1
-
mutant enzyme I132M
0.00013
d4T-TP
Human immunodeficiency virus 1
-
mutant enzyme I132A
0.00014
d4T-TP
Human immunodeficiency virus 1
-
mutant enzyme T139V
0.00016
d4T-TP
Human immunodeficiency virus 1
-
mutant enzyme E138A; mutant enzyme E138K; mutant enzyme I135A
0.00017
d4T-TP
Human immunodeficiency virus 1
-
mutant enzyme I135M
0.00018
d4T-TP
Human immunodeficiency virus 1
-
mutant enzyme N137A
0.0002
d4T-TP
Human immunodeficiency virus 1
-
wild-type enzyme
0.00152
Delavirdine
Human immunodeficiency virus 1
-
mutant enzyme N137A
0.00218
Delavirdine
Human immunodeficiency virus 1
-
wild-type enzyme
0.00261
Delavirdine
Human immunodeficiency virus 1
-
mutant enzyme T139V
0.00392
Delavirdine
Human immunodeficiency virus 1
-
mutant enzyme I135M
0.00762
Delavirdine
Human immunodeficiency virus 1
-
mutant enzyme E138A
0.0087
Delavirdine
Human immunodeficiency virus 1
-
mutant enzyme I132A
0.013
Delavirdine
Human immunodeficiency virus 1
-
mutant enzyme E138K
0.0302
Delavirdine
Human immunodeficiency virus 1
-
mutant enzyme I132M
0.0346
Delavirdine
Human immunodeficiency virus 1
-
mutant enzyme I135A
0.000002
efavirenz
Human immunodeficiency virus 1
-
wild-type enzyme, pH and temperature not specified in the publication
0.000003
efavirenz
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000003
efavirenz
Human immunodeficiency virus 1
-
mutant Y181C, pH and temperature not specified in the publication
0.0000037
efavirenz
Human immunodeficiency virus 1
-
mutant enzyme Y181C
0.0000039
efavirenz
Human immunodeficiency virus 1
-
wild-type enzyme
0.00006
efavirenz
Human immunodeficiency virus 1
-
-
0.000065
efavirenz
Human immunodeficiency virus 1
-
mutant K103N, pH and temperature not specified in the publication
0.0000734
efavirenz
Human immunodeficiency virus 1
-
mutant enzyme K103N
0.0000849
efavirenz
Human immunodeficiency virus 1
-
mutant enzyme K103N/Y181C
0.000087
efavirenz
Human immunodeficiency virus 1
-
mutant enzyme N137A
0.00009
efavirenz
Human immunodeficiency virus 1
-
mutant enzyme I132A
0.0000942
efavirenz
Human immunodeficiency virus 1
-
wild-type enzyme
0.000113
efavirenz
Human immunodeficiency virus 1
-
mutant enzyme T139V
0.000188
efavirenz
Human immunodeficiency virus 1
-
mutant enzyme E138A; mutant enzyme I135A
0.000197
efavirenz
Human immunodeficiency virus 1
-
mutant enzyme I135M
0.000216
efavirenz
Human immunodeficiency virus 1
-
mutant enzyme E138K
0.000228
efavirenz
Human immunodeficiency virus 1
-
mutant enzyme Y188L
0.000432
efavirenz
Human immunodeficiency virus 1
-
mutant enzyme I132M
0.0000046
GW8248
Human immunodeficiency virus 1
-
mutant enzyme K103N
0.0000051
GW8248
Human immunodeficiency virus 1
-
mutant enzyme K103N/Y181C
0.0000059
GW8248
Human immunodeficiency virus 1
-
mutant enzyme Y181C
0.0000082
GW8248
Human immunodeficiency virus 1
-
wild-type enzyme
0.0000679
GW8248
Human immunodeficiency virus 1
-
mutant enzyme Y188L
40 - 50
KCl
mouse mammary tumor virus
-
IC50: 40-50 mM
0.01
lamivudine triphosphate
Moloney murine leukemia virus
-
pH 7.8, 37C
-
0.021
lamivudine triphosphate
Xenotropic MLV-related virus
A1Z651
pH 7.8, 37C
-
40 - 50
NaCl
mouse mammary tumor virus
-
IC50: 40-50 mM
0.00028
nevirapine
Human immunodeficiency virus 1
-
-
0.00129
nevirapine
Human immunodeficiency virus 1
-
-
0.0017
nevirapine
Human immunodeficiency virus 1
P04585
-
0.002217
nevirapine
Human immunodeficiency virus 1
-
wild-type enzyme
0.0065
nevirapine
Human immunodeficiency virus 1
-
mutant enzyme N137A
0.0072
nevirapine
Human immunodeficiency virus 1
-
wild-type enzyme
0.0123
nevirapine
Human immunodeficiency virus 1
-
mutant enzyme T139V
0.0137
nevirapine
Human immunodeficiency virus 1
-
mutant enzyme E138A
0.0159
nevirapine
Human immunodeficiency virus 1
-
mutant enzyme E138K
0.018
nevirapine
Human immunodeficiency virus 1
-
mutant enzyme I132A
0.0389
nevirapine
Human immunodeficiency virus 1
-
mutant enzyme I135M
0.062
nevirapine
Human immunodeficiency virus 1
-
mutant enzyme I132M
0.087
nevirapine
Human immunodeficiency virus 1
-
mutant enzyme I135A
0.2
nevirapine
Human immunodeficiency virus 1
-
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
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
-
0.00151
tenofovir diphosphate
Moloney murine leukemia virus
-
pH 7.8, 37C
0.0064
tenofovir diphosphate
Xenotropic MLV-related virus
A1Z651
pH 7.8, 37C
0.0000126
TMC-125
Human immunodeficiency virus 1
-
mutant enzyme K103N
0.0000209
TMC-125
Human immunodeficiency virus 1
-
mutant enzyme Y181C
0.0000245
TMC-125
Human immunodeficiency virus 1
-
wild-type enzyme
0.0000324
TMC-125
Human immunodeficiency virus 1
-
mutant enzyme K103N/Y181C
0.0000647
TMC-125
Human immunodeficiency virus 1
-
mutant enzyme Y188L
0.00012
zidovudine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant M184V
0.00013
zidovudine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, wild-type enzyme
0.00018
zidovudine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant L74V
0.00066
zidovudine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant K65R
0.0027
zidovudine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37C, mutant Q151M
0.2
loviride
Human immunodeficiency virus 1
-
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
Human immunodeficiency virus 1
-
IC50-values of aptamers
-
additional information
additional information
Human immunodeficiency virus 1
-
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]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
-
assay at
7.5
-
reaction with RSV RNA, poly(rA)*poly(dT) and DNA
7.8
Xenotropic MLV-related virus
assay at
7.8
AF324493, Q8Q2U5, Q8Q2V9
assay at; assay at; assay at
7.8 - 8.5
Lymphadenopathy associated virus
-
-
8
-
reaction with poly(rA)*oligo(dT)
8
-
maximal incorporation of dTTP into poly(rA) template primed with oligo(dT)12
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)
8.2
-
reaction with AMV RNA
9
-
assay at
pH RANGE
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
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
-
assay at
37
-
assay at
37
Xenotropic MLV-related virus
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
ORGANISM
UNIPROT
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
ORGANISM
UNIPROT
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
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
UNIPROT
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B