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((1s,3s)-3-(7-amino-2H-2,3,5,6-tetraazabenzo[cd]azulen-2-yl)cyclobutyl)methyl tetrahydrogen triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
((2R,3S,5R)-3-hydroxy-5-(6-(prop-2-yn-1-ylamino)-9H-purin-9-yl)tetrahydrofuran-2-yl)methyl tetrahydrogen triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
((2R,3S,5R)-5-(2-amino-6-(prop-2-yn-1-ylamino)-9H-purin-9-yl)-3-hydroxytetrahydrofuran-2-yl)methyl tetrahydrogen triphosphate
diphosphate + DNAn+1
-
-
-
-
?
((2R,3S,5R)-5-(2-amino-6-(prop-2-yn-1-yloxy)-9H-purin-9-yl)-3-hydroxytetrahydrofuran-2-yl)methyl tetrahydrogen triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
((2R,3S,5R)-5-(6-amino-8-(prop-2-yn-1-ylamino)-9H-purin-9-yl)-3-hydroxytetrahydrofuran-2-yl)methyl tetrahydrogen triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
(-)-beta-2',3'-dideoxy-3'-thiacytidine triphosphate + 2-naphthyl-Tyr115 of p66 reverse transcriptase
?
-
-
-
-
?
(-)-beta-2',3'-dideoxy-3'-thiacytidine triphosphate + aminomethyl-Phe115 of p66 reverse transcriptase
?
-
-
-
-
?
(-)-beta-2',3'-dideoxy-3'-thiacytidine triphosphate + DNAn
diphosphate + ?
-
-
-
-
?
(-)-beta-2',3'-dideoxy-3'-thiacytidine triphosphate + Tyr115 of p66 reverse transcriptase
?
-
-
-
-
?
2',3'-dideoxy-CTP + DNAn
diphosphate + DNAn+1
-
-
-
-
?
2'-deoxyadenosine 5'-triphosphate + DNAn
diphosphate + DNAn+1
2'-deoxycytidine 5'-triphosphate + DNAn
diphosphate + DNAn+1
2'-deoxyguanosine 5'-triphosphate + DNAn
diphosphate + DNAn+1
2'-deoxyribonucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
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
2'-fluoro-N-cyclobutyladenosine triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
3'-azido-2',3'-dideoxy-2,6-diaminopurine-beta-D-ribofuranosyl 5'-triphosphate + DNAn
diphosphate + ?
-
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 + ?
-
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 + ?
-
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 + ?
-
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
-
incorporation activity of the enzyme with the enzyme inhibitor as A analogue or G analogue
-
-
?
a 2'-deoxyribonucleoside 5'-triphosphate + DNAn
diphosphate + DNAn+1
dATP + DNAn
diphosphate + DNAn+1
dCTP + DNAn
diphosphate + DNAn+1
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
dGTP + DNAn
diphosphate + DNAn+1
dTTP + DNAn
diphosphate + DNAn+1
N-cyclobutyladenosine triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
N-cyclobutyladenosine-phosphonyl diphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
tenofovir diphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
thymidine-5'-O-1-thiotriphosphate + DNAn
diphosphate + DNAn+1
-
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
-
-
?
additional information
?
-
2'-deoxyadenosine 5'-triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
2'-deoxyadenosine 5'-triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
2'-deoxycytidine 5'-triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
2'-deoxycytidine 5'-triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
2'-deoxyguanosine 5'-triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
2'-deoxyguanosine 5'-triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
2'-deoxythymidine 5'-triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
2'-deoxythymidine 5'-triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
a 2'-deoxyribonucleoside 5'-triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
a 2'-deoxyribonucleoside 5'-triphosphate + DNAn
diphosphate + DNAn+1
the enzyme exhibits an innate ability to reverse transcribe RNA and other synthetic congeners (XNAs) into DNA. Analysis of the active site of the enzyme reveals the importance of structural plasticity as a possible mechanism for XNA-dependent DNA synthesis
-
-
?
a 2'-deoxyribonucleoside 5'-triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
a 2'-deoxyribonucleoside 5'-triphosphate + DNAn
diphosphate + DNAn+1
-
exploration of the reaction mechanism of HIV reverse transcriptase with a nucleotide substrate
-
-
?
a 2'-deoxyribonucleoside 5'-triphosphate + DNAn
diphosphate + DNAn+1
-
globally fitting transient kinetic data are collected over a range of substrate concentrations and temperatures to derive kinetic and thermodynamic parameters governing enzyme specificity. Nucleotide binding is exothermic but is marginally stable relative to the physiological substrate concentrations, but substrate binding triggers an enzyme conformational change, which is the major determinant of specificity
-
-
?
dATP + DNAn
diphosphate + DNAn+1
-
-
-
-
?
dATP + DNAn
diphosphate + DNAn+1
-
-
-
-
?
dATP + DNAn
diphosphate + DNAn+1
-
-
-
-
?
dATP + DNAn
diphosphate + DNAn+1
-
RNA-dependent DNA synthesis
-
-
?
dATP + DNAn
diphosphate + DNAn+1
-
-
-
-
?
dATP + DNAn
diphosphate + DNAn+1
-
-
-
-
?
dATP + DNAn
diphosphate + DNAn+1
-
enzyme mutant N483Q/S486Q/T539N/Y545Q/D547T/P548Q/A570Q/D578Q/A597T/W604R/S612N/V730L/R736Q/S739N/M747R
-
-
?
dCTP + DNAn
diphosphate + DNAn+1
-
-
-
-
?
dCTP + DNAn
diphosphate + DNAn+1
-
-
-
-
?
dCTP + DNAn
diphosphate + DNAn+1
-
-
-
-
?
dCTP + DNAn
diphosphate + DNAn+1
-
-
-
-
?
dCTP + DNAn
diphosphate + DNAn+1
-
enzyme mutant N483Q/S486Q/T539N/Y545Q/D547T/P548Q/A570Q/D578Q/A597T/W604R/S612N/V730L/R736Q/S739N/M747R
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
efficiency of natural and synthetic templates
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
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
-
the enzyme exhibits both synthetic and degradative activity, DNA polymerase and RNAse H
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
affinity of the enzyme for (U)n and a series of (U)n analogs
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
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
-
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
-
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
-
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
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
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
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
the enzyme appears to be required very early after infection to synthesize proviral DNA
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
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
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
Chicken syncytial virus
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
Chicken syncytial virus
-
the enzyme appears to be required very early after infection to synthesize proviral DNA
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
the enzyme appears to be required very early after infection to synthesize proviral DNA
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
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
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
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
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
the enzyme might play a role in normal differentiation
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
the enzyme exhibits both synthetic and degradative activity, DNA polymerase and RNAse H
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
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
Hamster leukemia virus
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
Hamster leukemia virus
-
the enzyme exhibits both synthetic and degradative activity, DNA polymerase and RNAse H
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
Hamster leukemia virus
-
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
Hamster leukemia virus HaLV
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
poly(dA)/oligo(dT)12-18 and poly(rA)/oligo(dT)12-18 as template-primers
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
691140, 691152, 691632, 691882, 692539, 692555, 692567, 692580, 692582, 692597, 693312, 693914, 694207, 694309, 694504, 695141, 695224 -
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
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
-
DNA polymerase Pol gamma also catalyzes reverse transcription with a slightly higher efficiency than HIV-1 reverse transcriptase
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
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
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
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
661221, 662208, 662652, 690316, 690317, 691234, 691261, 691778, 691942, 692252, 692800, 693371, 693584, 693910, 695260, 695261, 714972, 721311, 721815, 722241, 722692, 723089 -
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
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
-
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
-
mechenism
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
poly(rA)n¥oligo(dT)12-18
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
reverse transcriptase has RNA-dependent and DNA-dependent DNA polymerase activity
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
RNA-dependent DNA synthesis
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
Ext-T DNA 23-mer primer annealed to the RNA 40-mer template
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
Human T-cell lymphotropic virus/lymphadenopathy-associated virus
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
Lymphadenopathy associated virus
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
the enzyme exhibits both synthetic and degradative activity, DNA polymerase and RNAse H
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
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
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
681096, 691513, 692219, 693073, 693484, 693960, 694030, 695179, 721311, 721508, 723292 -
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
the enzyme appears to be required very early after infection to synthesize proviral DNA
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
wild-type Moloney murine leukemia virus reverse transcriptase selectively uses deoxyribonucleotides over ribonucleotides as substrates
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
Td26/50-Cy3-Pd18b
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
the enzyme exhibits both synthetic and degradative activity, DNA polymerase and RNAse H
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
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
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
the enzyme exhibits both synthetic and degradative activity, DNA polymerase and RNAse H
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
the enzyme appears to be required very early after infection to synthesize proviral DNA
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
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
-
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
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
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
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
prototype foamy virus
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
prototype foamy virus
-
heteropolymeric single stranded M13 substrate
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
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
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
the enzyme exhibits both synthetic and degradative activity, DNA polymerase and RNAse H
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
the enzyme appears to be required very early after infection to synthesize proviral DNA
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
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
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
the enzyme appears to be required very early after infection to synthesize proviral DNA
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
the enzyme exhibits both synthetic and degradative activity, DNA polymerase and RNAse H
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
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
-
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
-
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
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
the enzyme plays a central role in transposition of retroelements
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
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
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
heteropolymeric single stranded M13 substrate
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
the enzyme shows both RNA-dependent and DNA-dependent DNA synthesis activity and an associated RNAse H activity
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
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
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
the enzyme appears to be required very early after infection to synthesize proviral DNA
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
the enzyme exhibits both synthetic and degradative activity, DNA polymerase and RNAse H
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
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
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
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
-
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
-
DNA polymerase shows significant reverse-transcriptase activity in presence of Mg2+
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
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
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
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
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
the enzyme exhibits both synthetic and degradative activity, DNA polymerase and RNAse H
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
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
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
Td26/50-Cy3-Pd18b
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
DNA polymerase shows significant reverse-transcriptase activity in presence of Mg2+
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
poly(rC)*p(dG)(12-18)
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
DNA polymerase shows significant reverse-transcriptase activity in presence of Mg2+
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
poly(rC)*p(dG)(12-18)
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
DNA polymerase shows significant reverse-transcriptase activity in presence of Mg2+
-
-
?
deoxynucleoside triphosphate + DNAn
diphosphate + DNAn+1
-
DNA polymerase shows significant reverse-transcriptase activity in presence of Mg2+
-
-
?
dGTP + DNAn
diphosphate + DNAn+1
-
-
-
-
?
dGTP + DNAn
diphosphate + DNAn+1
-
-
-
-
?
dGTP + DNAn
diphosphate + DNAn+1
-
-
-
-
?
dGTP + DNAn
diphosphate + DNAn+1
-
RNA-dependent DNA synthesis
-
-
?
dGTP + DNAn
diphosphate + DNAn+1
-
-
-
-
?
dGTP + DNAn
diphosphate + DNAn+1
-
-
-
-
?
dGTP + DNAn
diphosphate + DNAn+1
-
-
-
-
?
dTTP + DNAn
diphosphate + DNAn+1
-
-
-
?
dTTP + DNAn
diphosphate + DNAn+1
-
incorporation of dTTP into poly(rA)-p(dT)15
-
-
?
dTTP + DNAn
diphosphate + DNAn+1
-
-
-
?
dTTP + DNAn
diphosphate + DNAn+1
-
-
-
?
dTTP + DNAn
diphosphate + DNAn+1
-
incorporation of dTTP into poly(rA)-p(dT)15
-
-
?
dTTP + DNAn
diphosphate + DNAn+1
-
incorporation of dTTP into poly(rA)-p(dT)45
-
-
?
dTTP + DNAn
diphosphate + DNAn+1
prototype foamy virus
-
homopolymeric substrate poly(rA)/oligo(dT)
-
-
?
dTTP + DNAn
diphosphate + DNAn+1
-
homopolymeric substrate poly(rA)/oligo(dT)
-
-
?
dTTP + DNAn
diphosphate + DNAn+1
-
enzyme mutant N483Q/S486Q/T539N/Y545Q/D547T/P548Q/A570Q/D578Q/A597T/W604R/S612N/V730L/R736Q/S739N/M747R
-
-
?
dTTP + poly(rA)/(dT)18
?
-
-
-
-
?
dTTP + poly(rA)/(dT)18
?
-
-
-
-
?
dTTP + poly(rA)/(dT)18
?
-
-
-
-
?
dTTP + poly(rA)/(dT)18
?
-
-
-
?
dTTP + poly(rA)/(dT)18
?
-
-
-
-
?
dTTP + poly(rA)/(dT)18
?
-
-
-
-
?
dTTP + poly(rA)/(dT)18
?
-
-
-
-
?
dTTP + poly(rA)/(dT)18
?
-
-
-
-
?
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
?
-
-
the reverse transcriptase activity of DNA polymerase gamma is not likely to contribute significantly to the biology of mitochondrial DNA replication
-
-
?
additional information
?
-
-
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
?
-
-
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
?
-
-
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
?
-
-
bis-(2'-deoxynucleoside)5,5'-tetraphosphates and bis-(2'-deoxynucleoside)5',5'-triphosphates are effective substrates for DNA elongation
-
-
?
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
?
-
-
uses the cellular tRNALys,3 molecule as primer
-
-
?
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, 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
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
?
-
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
?
-
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
?
-
-
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
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
?
-
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
?
-
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
?
-
-
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
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
?
-
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
?
-
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
?
-
-
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
?
-
-
binding affinity Kd of HIV-1 reverse transcriptase for non-canonical rNTPs is 1.4- to 43fold lower, and the rNTP rate of incorporation is 15- to 1551fold slower than for dNTP, suggesting that reverse transcriptase is more selective for incorporation of dNTPs rather than rNTPs. HIV-1 reverse transcriptase selectivity for dNTP versus rNTP is the lowest for ATP
-
-
?
additional information
?
-
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
?
-
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
?
-
-
HIV-1 RT has high substrate affinity and low susceptibility to formamide
-
-
?
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
?
-
-
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
?
-
-
elongates telomeres to tolerate mutations in the telomeric template
-
-
?
additional information
?
-
-
the N-terminal protease domain of the reverse transcriptase also shows polymerase activity
-
-
?
additional information
?
-
-
no saturation is observed for extension on DNA templates
-
-
?
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
?
-
-
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
?
-
-
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
-
-
?
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((1s,3s)-3-(7-amino-2H-2,3,5,6-tetraazabenzo[cd]azulen-2-yl)cyclobutyl)methyl tetrahydrogen triphosphate
-
-
(-)-epigallocatechin-3-gallate
-
exposure to (-)-epigallocatechin-3-gallate reduces cellular proliferation and induced apoptosis in both MCF-7 and HL60 cells in vitro, although TERT mRNA expression is decreased only in MCF-7 cells
(2-amino-5-chlorophenyl)(2-chlorophenyl)methanone
-
-
(2-amino-5-chlorophenyl)(2-fluorophenyl)methanone
-
-
(2-amino-5-chlorophenyl)(phenyl)methanone
-
-
(4S)-6-chloro-4-(cyclopropylethynyl)-4-(trifluoromethyl)-1,4-dihydro-2H-3,1-benzoxazin-2-one
-
(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
-
-
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
-
-
1,12-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-benzyl-4-(2,6-difluorophenyl)-7,7-dimethyl-5-oxo-5,6,7,8-tetrahydro-1H-pyrrolo[2,3-b]quinoline-3-carbonitrile
-
-
1-benzyl-4-(2,6-dimethylphenyl)-7,7-dimethyl-5-oxo-5,6,7,8-tetrahydro-1H-pyrrolo[2,3-b]quinoline-3-carbonitrile
-
-
1-benzyl-4-(3-chlorophenyl)-7,7-dimethyl-5-oxo-5,6,7,8-tetrahydro-1H-pyrrolo[2,3-b]quinoline-3-carbonitrile
-
-
1-benzyl-4-(4-fluorophenyl)-7,7-dimethyl-5-oxo-5,6,7,8-tetrahydro-1H-pyrrolo[2,3-b]quinoline-3-carbonitrile
-
-
1-benzyl-7,7-dimethyl-4-(4-nitrophenyl)-5-oxo-5,6,7,8-tetrahydro-1H-pyrrolo[2,3-b]quinoline-3-carbonitrile
-
-
1-benzyl-7,7-dimethyl-5-oxo-4-phenyl-5,6,7,8-tetrahydro-1H-pyrrolo[2,3-b]quinoline-3-carbonitrile
-
-
1-benzyl-7,7-dimethyl-5-oxo-5,6,7,8-tetrahydro-1H-pyrrolo[2,3-b]quinoline-3-carbonitrile
-
-
1-butyl-4-[2-fluoro-4-(trifluoromethyl)phenyl]-5-oxo-1,5-dihydroindeno[1,2-b]pyrrolo[3,2-e]pyridine-3-carbonitrile
-
-
1-tert-butyl-5-formyl-2,3-dihydro-1H-pyrrolo[2,3-b]pyridine-3-carbonitrile
-
-
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
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
2',3'-dideoxy-3'-thiacytidine
-
-
2',3'-dideoxy-5-fluoro-3'-thiacytidine
-
-
2',3'-dideoxycytidine
-
-
2',3'-dideoxyguanosine triphosphate
-
-
2',3'-dideoxythymidine 5'-triphosphate
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
-
-
2,7-dihydroxy-2,4,6-cyclo-heptatrien-1-one
-
beta-thujaplicinol analogue. Compound has no effect on polymerase-dependent RNase H cleavages but significantly affects the rates of polymerase-independent RNase H cleavages. In a model, the compoouind binds to the RNase H active site after the primary polymerase-dependent RNase H cleavage has occurred and stabilizes the 3'-end of the DNA primer in the polymerase active site thus blocking the enzyme's ability to carry out the polymerase-independent cleavages
2-acetyl-4-[4-(dimethylamino)phenyl]indeno[1,2-b]pyrrolo[3,2-e]pyridin-5(1H)-one
-
-
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
-
3'-azido-3'-deoxythymidine
3'-azido-3'deoxythymidine 5'-triphosphate
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
3,5-dimethyl-4-[[2-([(3R)-1-[(pyridin-4-yl)methyl]pyrrolidin-3-yl]amino)thieno[3,2-d]pyrimidin-4-yl]oxy]benzonitrile
-
exceptionally potent against a wide range of HIV-1 strains carrying single NNRTI-resistant mutations
3,5-dimethyl-4-[[2-([(3S)-1-[(pyridin-4-yl)methyl]pyrrolidin-3-yl]amino)thieno[3,2-d]pyrimidin-4-yl]oxy]benzonitrile
-
-
3,5-dimethyl-4-[[2-([1-[(4-nitrophenyl)methyl]-1,2,3,4-tetrahydropyridin-4-yl]amino)-5,7-dihydrothieno[3,4-d]pyrimidin-4-yl]oxy]benzonitrile
-
-
3,5-dimethyl-4-[[2-([1-[(4-nitrophenyl)methyl]piperidin-4-yl]amino)-5,7-dihydrofuro[3,4-d]pyrimidin-4-yl]oxy]benzonitrile
-
-
3,5-dimethyl-4-[[2-([1-[(4-nitrophenyl)methyl]piperidin-4-yl]amino)-6,7-dihydro-5H-cyclopenta[d]pyrimidin-4-yl]oxy]benzonitrile
-
-
3,5-dimethyl-4-[[2-([1-[(4-nitrophenyl)methyl]piperidin-4-yl]amino)-6,7-dihydrothieno[3,2-d]pyrimidin-4-yl]oxy]benzonitrile
-
-
3,5-dimethyl-4-[[2-([1-[(4-nitrophenyl)methyl]piperidin-4-yl]amino)-7,8-dihydro-6H-thiopyrano[3,2-d]pyrimidin-4-yl]oxy]benzonitrile
-
-
3,5-dimethyl-4-[[2-([1-[(pyridin-4-yl)methyl]azepan-4-yl]amino)thieno[3,2-d]pyrimidin-4-yl]oxy]benzonitrile
-
-
3,5-dimethyl-4-[[2-([1-[(pyridin-4-yl)methyl]azetidin-3-yl]amino)thieno[3,2-d]pyrimidin-4-yl]oxy]benzonitrile
-
-
3,5-dimethyl-4-[[2-([1-[(pyridin-4-yl)methyl]piperidin-4-yl]amino)-5,6,7,8-tetrahydroquinazolin-4-yl]oxy]benzonitrile
-
-
3,5-dimethyl-4-[[2-([1-[(pyridin-4-yl)methyl]piperidin-4-yl]amino)-5,7-dihydrofuro[3,4-d]pyrimidin-4-yl]oxy]benzonitrile
-
-
3,5-dimethyl-4-[[2-([1-[(pyridin-4-yl)methyl]piperidin-4-yl]amino)-6,7-dihydro-5H-cyclopenta[d]pyrimidin-4-yl]oxy]benzonitrile
-
-
3,5-dimethyl-4-[[2-([1-[(pyridin-4-yl)methyl]piperidin-4-yl]amino)-6,7-dihydrothieno[3,2-d]pyrimidin-4-yl]oxy]benzonitrile
-
-
3,5-dimethyl-4-[[2-([8-[(pyridin-4-yl)methyl]-8-azabicyclo[3.2.1]octan-3-yl]amino)thieno[3,2-d]pyrimidin-4-yl]oxy]benzonitrile
-
-
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-[(3-[[4-(4-cyano-2,6-dimethylphenoxy)thieno[3,2-d]pyrimidin-2-yl]amino]-8-azabicyclo[3.2.1]octan-8-yl)methyl]benzamide
-
-
3-[(3-[[4-(4-cyano-2,6-dimethylphenoxy)thieno[3,2-d]pyrimidin-2-yl]amino]azetidin-1-yl)methyl]benzamide
-
-
3-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-5,6,7,8-tetrahydroquinazolin-2-yl]amino]piperidin-1-yl)methyl]benzamide
-
-
3-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-5,7-dihydrofuro[3,4-d]pyrimidin-2-yl]amino]piperidin-1-yl)methyl]benzamide
-
-
3-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-6,7-dihydro-5H-cyclopenta[d]pyrimidin-2-yl]amino]piperidin-1-yl)methyl]benzamide
-
-
3-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-6,7-dihydrothieno[3,2-d]pyrimidin-2-yl]amino]piperidin-1-yl)methyl]benzamide
-
-
3-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-7,8-dihydro-6H-thiopyrano[3,2-d]pyrimidin-2-yl]amino]piperidin-1-yl)methyl]benzamide
-
-
3-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)thieno[3,2-d]pyrimidin-2-yl]amino]azepan-1-yl)methyl]benzamide
-
-
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-[11-(ethoxycarbonyl)-1,7,9,10,11,12-hexahydro-3,2-(metheno)-10-azaazuleno[1',8',7',6':3,4,5]cyclopenta[6,7]fluoreno[2,1,9,8-fghij]benzo[cd]cyclopenta[mno]acephenanthrylen-9-yl]-1-methylpyridinium
-
pyridinium fullerene derivative, 50% cytotoxicity above 0.05 mM
3-[6-bromo-3-[2-(3,4-dihydroisoquinolin-2(1H)-yl)-2-oxoethyl]-2-fluorophenoxy]-5-chlorobenzonitrile
-
-
3-[[(3R)-3-[[4-(4-cyano-2,6-dimethylphenoxy)thieno[3,2-d]pyrimidin-2-yl]amino]pyrrolidin-1-yl]methyl]benzamide
-
exceptionally potent against a wide range of HIV-1 strains carrying single NNRTI-resistant mutations. Favorable pharmacokinetic properties with an oral bioavailability of 30.96% and a half-life of 11.1 h.Ppromising anti-HIV-1 drug candidate with potent antiviral activities and desirable drug-like properties.
3-[[(3S)-3-[[4-(4-cyano-2,6-dimethylphenoxy)thieno[3,2-d]pyrimidin-2-yl]amino]pyrrolidin-1-yl]methyl]benzamide
-
-
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-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-((4-((4-(4-cyano-2,6-dimethylphenoxy)-5,7-dihydrofuro-[3,4-d]pyrimidin-2-yl)amino)piperidin-1-yl)methyl)benzamide
-
-
-
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-([2-[(1-[[4-(methanesulfonyl)phenyl]methyl]-1,2,3,4-tetrahydropyridin-4-yl)amino]-5,7-dihydrothieno[3,4-d]pyrimidin-4-yl]oxy)-3,5-dimethylbenzonitrile
-
-
4-([2-[(1-[[4-(methanesulfonyl)phenyl]methyl]azepan-4-yl)amino]thieno[3,2-d]pyrimidin-4-yl]oxy)-3,5-dimethylbenzonitrile
-
-
4-([2-[(1-[[4-(methanesulfonyl)phenyl]methyl]azetidin-3-yl)amino]thieno[3,2-d]pyrimidin-4-yl]oxy)-3,5-dimethylbenzonitrile
-
-
4-([2-[(1-[[4-(methanesulfonyl)phenyl]methyl]piperidin-4-yl)amino]-5,6,7,8-tetrahydroquinazolin-4-yl]oxy)-3,5-dimethylbenzonitrile
-
-
4-([2-[(1-[[4-(methanesulfonyl)phenyl]methyl]piperidin-4-yl)amino]-5,7-dihydrofuro[3,4-d]pyrimidin-4-yl]oxy)-3,5-dimethylbenzonitrile
-
-
4-([2-[(1-[[4-(methanesulfonyl)phenyl]methyl]piperidin-4-yl)amino]-6,7-dihydro-5H-cyclopenta[d]pyrimidin-4-yl]oxy)-3,5-dimethylbenzonitrile
-
-
4-([2-[(1-[[4-(methanesulfonyl)phenyl]methyl]piperidin-4-yl)amino]-6,7-dihydrothieno[3,2-d]pyrimidin-4-yl]oxy)-3,5-dimethylbenzonitrile
-
-
4-([2-[(1-[[4-(methanesulfonyl)phenyl]methyl]piperidin-4-yl)amino]-7,8-dihydro-6H-thiopyrano[3,2-d]pyrimidin-4-yl]oxy)-3,5-dimethylbenzonitrile
-
-
4-([2-[(8-[[4-(methanesulfonyl)phenyl]methyl]-8-azabicyclo[3.2.1]octan-3-yl)amino]thieno[3,2-d]pyrimidin-4-yl]oxy)-3,5-dimethylbenzonitrile
-
-
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-[(2-[[(3R)-1-[[4-(methanesulfonyl)phenyl]methyl]pyrrolidin-3-yl]amino]thieno[3,2-d]pyrimidin-4-yl)oxy]-3,5-dimethylbenzonitrile
-
-
4-[(2-[[(3S)-1-[[4-(methanesulfonyl)phenyl]methyl]pyrrolidin-3-yl]amino]thieno[3,2-d]pyrimidin-4-yl)oxy]-3,5-dimethylbenzonitrile
-
-
4-[(3,5-dimethylphenyl)sulfanyl]quinolin-2(1H)-one
-
-
4-[(3-[[4-(4-cyano-2,6-dimethylphenoxy)thieno[3,2-d]pyrimidin-2-yl]amino]-8-azabicyclo[3.2.1]octan-8-yl)methyl]benzamide
-
-
4-[(3-[[4-(4-cyano-2,6-dimethylphenoxy)thieno[3,2-d]pyrimidin-2-yl]amino]-8-azabicyclo[3.2.1]octan-8-yl)methyl]benzene-1-sulfonamide
-
-
4-[(3-[[4-(4-cyano-2,6-dimethylphenoxy)thieno[3,2-d]pyrimidin-2-yl]amino]azetidin-1-yl)methyl]benzamide
-
-
4-[(3-[[4-(4-cyano-2,6-dimethylphenoxy)thieno[3,2-d]pyrimidin-2-yl]amino]azetidin-1-yl)methyl]benzene-1-sulfonamide
-
-
4-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-5,6,7,8-tetrahydroquinazolin-2-yl]amino]piperidin-1-yl)methyl]benzamide
-
-
4-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-5,6,7,8-tetrahydroquinazolin-2-yl]amino]piperidin-1-yl)methyl]benzene-1-sulfonamide
-
-
4-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-5,7-dihydrofuro[3,4-d]pyrimidin-2-yl]amino]piperidin-1-yl)methyl]benzamide
-
-
4-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-5,7-dihydrofuro[3,4-d]pyrimidin-2-yl]amino]piperidin-1-yl)methyl]benzene-1-sulfonamide
-
-
4-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-5,7-dihydrothieno[3,4-d]pyrimidin-2-yl]amino]piperidin-1-yl)methyl]benzene-1-sulfonamide
-
-
4-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-6,7-dihydro-5H-cyclopenta[d]pyrimidin-2-yl]amino]piperidin-1-yl)methyl]benzamide
-
-
4-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-6,7-dihydro-5H-cyclopenta[d]pyrimidin-2-yl]amino]piperidin-1-yl)methyl]benzene-1-sulfonamide
-
-
4-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-6,7-dihydrothieno[3,2-d]pyrimidin-2-yl]amino]piperidin-1-yl)methyl]benzamide
-
-
4-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-6,7-dihydrothieno[3,2-d]pyrimidin-2-yl]amino]piperidin-1-yl)methyl]benzene-1-sulfonamide
-
-
4-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-7,8-dihydro-6H-thiopyrano[3,2-d]pyrimidin-2-yl]amino]piperidin-1-yl)methyl]benzamide
-
-
4-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-7,8-dihydro-6H-thiopyrano[3,2-d]pyrimidin-2-yl]amino]piperidin-1-yl)methyl]benzene-1-sulfonamide
-
-
4-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)thieno[3,2-d]pyrimidin-2-yl]amino]azepan-1-yl)methyl]benzamide
-
-
4-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)thieno[3,2-d]pyrimidin-2-yl]amino]azepan-1-yl)methyl]benzene-1-sulfonamide
-
-
4-[6-(4-methylpiperazin-1-yl)pyridin-3-yl]-1-(3-methoxypropyl)-8-(1-methyl-1H-pyrazol-4-yl)-2,5-dihydro-1H-indeno[1,2-d]pyrimidine
-
inhibits HIV-1 reverse transcriptase in a primer extension assay but has no measurable activity against human DNA polymerase gamma at 0.01 mM. It potently inhibits HIV-1 replication in vitro with 1.5 nM 50% effective concentration. The antiviral potency is unaffected by the presence of nonnucleotide RT inhibitor mutations L100I, K103N/Y181C, V106A, or Y188L. Viruses encoding K65R are hypersusceptible to inhibition by the compound, and it retains full activity against viruses encoding M184V. A recombinant virus encoding the RT W153L is highly resistant
4-[[(3R)-3-[[4-(4-cyano-2,6-dimethylphenoxy)thieno[3,2-d]pyrimidin-2-yl]amino]pyrrolidin-1-yl]methyl]benzamide
-
-
4-[[(3R)-3-[[4-(4-cyano-2,6-dimethylphenoxy)thieno[3,2-d]pyrimidin-2-yl]amino]pyrrolidin-1-yl]methyl]benzene-1-sulfonamide
-
-
4-[[(3S)-3-[[4-(4-cyano-2,6-dimethylphenoxy)thieno[3,2-d]pyrimidin-2-yl]amino]pyrrolidin-1-yl]methyl]benzamide
-
-
4-[[(3S)-3-[[4-(4-cyano-2,6-dimethylphenoxy)thieno[3,2-d]pyrimidin-2-yl]amino]pyrrolidin-1-yl]methyl]benzene-1-sulfonamide
-
-
4-[[2-([1-[(4-aminophenyl)methyl]piperidin-4-yl]amino)-5,7-dihydrothieno[3,4-d]pyrimidin-4-yl]oxy]-3,5-dimethylbenzonitrile
-
-
4-[[4-(4-chlorophenyl)piperazin-1-yl]methyl]-7,8-dihydroxy-2H-chromen-2-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-([2-[(4-cyanophenyl)amino]pyrimidin-4-yl]amino)-5,7-dimethylnaphthalene-2-carbonitrile
-
compound has potency below 10 nM towards wild-type HIV-1 and viral variants containing the clinically important Y181C and K103N/Y181C mutations, greater activity than efavirenz particularly towards the K103N-bearing variant, normal cytotoxicity, and solubility
6-([4-[(4-cyanophenyl)amino]-1,3,5-triazin-2-yl]amino)-5,7-dimethylnaphthalene-2-carbonitrile
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-(pyridin-3-yl)-1,7,9,10,11,12-hexahydro-3,2-(metheno)-10-azaazuleno[1',8',7',6':3,4,5]cyclopenta[6,7]fluoreno[2,1,9,8-fghij]benzo[cd]cyclopenta[mno]acephenanthrylene-11-carboxylic acid
-
pyridine fullerene derivative, 50% cytotoxicity above 0.05 mM
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 triphosphate
-
-
capravirine
-
HIV reverse transcriptase contains two distinct protein domains catalyzing DNA polymerase and RNase H activities. Inhibits 5'-RNA directed HIV RNase H activity of reverse transcriptase. Potency of RNase H inhibition correlats with the respective potencies of DNA polymerase inhibition
dATP
-
replacement of dATP by ATP completely prevents synthesis
ddTTP
-
inhibits the enzyme from the group M strain BH10 isolate and the enzyme from the Spanish HIV-1 group O isolate
Dextran sulfate
-
IC50: 0.0044 mg/ml
-
early growth response-1
-
overexpressio nof early growth response-1 decreases TERT protein production as well TERT mRNA transcription
-
emetine
-
plant alkaloid isolated from Psychotria ipecacuanha. Reverse transcriptase is blocked in the presence of emetine both both in in vitro reactions with isolated enzyme and intravirion, reaching 80% of reduction in HIV-1 infection, with low cytotoxic effect. Emetine also blocks HIV-1 infection of reverse transcriptase M184V mutants
flavanonol
-
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
Hygrophorus russula RNase
-
RNase isolated from fruiting bodies of the edible mushroom Hygrophorus russula inhibits reverse transcriptase by 91.6% at the concentration of 2.4 mg/ml
-
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 triphosphate
-
-
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
N-[4-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)thieno[3,2-d]pyrimidin-2-yl]amino]piperidin-1-yl)methyl]phenyl]methanesulfonamide
-
-
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
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
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
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
-
Streptonigrin
-
acts on the enzyme molecule in an enzyme-template primer complex by a series of reactions including oxidation-reduction
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
-
-
2',3'-dehydro-2',3'-deoxythymidine triphosphate
-
i.e. stavudine triphosphate
2',3'-dehydro-2',3'-deoxythymidine triphosphate
i.e. stavudine triphosphate
2',3'-dideoxy-2',3'-dehydrothymidine 5'-triphosphate
-
terminates synthesis of DNA
2',3'-dideoxy-2',3'-dehydrothymidine 5'-triphosphate
-
terminates synthesis of DNA
2',3'-dideoxythymidine 5'-triphosphate
-
-
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-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-3'-deoxythymidine
-
-
3'-azido-3'-deoxythymidine
-
-
3'-azido-3'-deoxythymidine
-
3'-azido-3'deoxythymidine 5'-triphosphate
-
IC50: 0.042 mM
3'-azido-3'deoxythymidine 5'-triphosphate
-
IC50: 0.06 mM
4'-ethynyl-2-amino-2'-deoxyadenosine triphosphate
-
-
4'-ethynyl-2-amino-2'-deoxyadenosine triphosphate
-
4'-ethynyl-2-fluoro-2'-deoxyadenosine triphosphate
-
-
4'-ethynyl-2-fluoro-2'-deoxyadenosine triphosphate
-
6-([4-[(4-cyanophenyl)amino]-1,3,5-triazin-2-yl]amino)-5,7-dimethylnaphthalene-2-carbonitrile
-
compound has potency below 10 nM towards wild-type HIV-1 and viral variants containing the clinically important Y181C and K103N/Y181C mutations, greater activity than efavirenz particularly towards the K103N-bearing variant, normal cytotoxicity, and solubility
6-([4-[(4-cyanophenyl)amino]-1,3,5-triazin-2-yl]amino)-5,7-dimethylnaphthalene-2-carbonitrile
i.e. F3284-8495, a specific inhibitor of reverse transcriptase RNase H, with low micromolar potency in vitro
adefovir diphosphate
-
-
azidothymidine
prototype foamy virus
-
inhibits foamy virus replication
azidothymidine
-
inhibits FV replication
ddATP
-
0.015 mM
ddATP
-
competitive with respect to dATP, noncompetitive with respect to dCTP, dGTP and dTTP
Delavirdine
-
-
didanosine
-
-
efavirenz
-
-
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
efavirenz
-
efavirenz actually stimulates wild type RNase H binding and catalytic functions, stimulating both 3' and 5'-directed RNase H activity. Efavirenz specifically promotes binding of the reverse transcriptase to RNase H substrates
efavirenz
-
Compound has no effect on polymerase-dependent RNase H cleavages but significantly affects the rates of polymerase-independent RNase H cleavages. Efavirenz destabilizes the 3'-end of the DNA primer in the DNA polymerase active site and promotes RT-mediated polymerase-independent cleavages
efavirenz
-
antiviral potency, EC50: 0.000001 mM
Etravirine
-
-
KCl
-
80 mM, 50% inhibition
KCl
-
80 mM, 60% inhibition
lamivudine
-
-
lamivudine triphosphate
-
-
lamivudine triphosphate
-
-
lamivudine triphosphate
-
Mn2+
-
above 1 mM MnCl2
NEM
-
-
NEM
-
2 mM, 82% loss of activity
nevirapine
-
-
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
nevirapine
-
antiviral potency, EC50: 0.00004 mM
Rilpivirine
-
-
stavudine
-
potent inhibitor
suramin
-
-
Tenofovir
-
-
Tenofovir
-
9-[(2-phosphonomethoxy)propyl]adenine
tenofovir diphosphate
-
-
tenofovir diphosphate
-
-
zidovudine
-
-
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
-
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
-
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
-
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
-
EC50 values, molecular modeling, overview
-
additional information
AF324493
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
-
additional information
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
-
additional information
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
-
additional information
-
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
-
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 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
-
targeted disruption of aromatase results in significant inhibition of telomerase activity
-
additional information
-
decreased telomerase activity and normal expression of telomere-binding proteins in the absence of Dicer
-
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
-
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
-
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0.00003 - 0.00006
1,10-di-2',3'-dideoxy-3'-thiacytidine-decanoate
0.000004 - 0.000005
1,10-di-3'-azido-2',3'-dideoxythymidine-decanoate
0.000001 - 0.000004
1,10-di-3'-fluoro-2',3'-dideoxythymidine-decanoate
0.000009 - 0.00002
1,12-di-2',3'-dideoxy-3'-thiacytidine-dodecanoate
0.000002 - 0.000004
1,12-di-3'-azido-2',3'-dideoxythymidine-dodecanoate
0.00000097 - 0.000004
1,12-di-3'-fluoro-2',3'-dideoxythymidine-dodecanoate
0.000003 - 0.00003
1,14-di-2',3'-dideoxy-3'-thiacytidine-tetradecanoate
0.000003
1,14-di-3'-azido-2',3'-dideoxythymidine-tetradecanoate
0.00000076 - 0.000003
1,14-di-3'-fluoro-2',3'-dideoxythymidine-tetradecanoate
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 - 0.00015
1,4-di-2',3'-dideoxy-3'-thiacytidine-succinate
0.00036
1-benzyl-4-(2,6-difluorophenyl)-7,7-dimethyl-5-oxo-5,6,7,8-tetrahydro-1H-pyrrolo[2,3-b]quinoline-3-carbonitrile
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.026
1-benzyl-4-(2,6-dimethylphenyl)-7,7-dimethyl-5-oxo-5,6,7,8-tetrahydro-1H-pyrrolo[2,3-b]quinoline-3-carbonitrile
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.058
1-benzyl-4-(3-chlorophenyl)-7,7-dimethyl-5-oxo-5,6,7,8-tetrahydro-1H-pyrrolo[2,3-b]quinoline-3-carbonitrile
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0029
1-benzyl-4-(4-fluorophenyl)-7,7-dimethyl-5-oxo-5,6,7,8-tetrahydro-1H-pyrrolo[2,3-b]quinoline-3-carbonitrile
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0014
1-benzyl-7,7-dimethyl-4-(4-nitrophenyl)-5-oxo-5,6,7,8-tetrahydro-1H-pyrrolo[2,3-b]quinoline-3-carbonitrile
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.00073
1-benzyl-7,7-dimethyl-5-oxo-4-phenyl-5,6,7,8-tetrahydro-1H-pyrrolo[2,3-b]quinoline-3-carbonitrile
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.012
1-benzyl-7,7-dimethyl-5-oxo-5,6,7,8-tetrahydro-1H-pyrrolo[2,3-b]quinoline-3-carbonitrile
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.00058 - 0.0063
1-butyl-4-[2-fluoro-4-(trifluoromethyl)phenyl]-5-oxo-1,5-dihydroindeno[1,2-b]pyrrolo[3,2-e]pyridine-3-carbonitrile
0.014
1-tert-butyl-5-formyl-2,3-dihydro-1H-pyrrolo[2,3-b]pyridine-3-carbonitrile
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.00077 - 0.00237
2',3'-dehydro-2',3'-deoxythymidine triphosphate
0.00009 - 0.0002
2',3'-dideoxy-3'-thiacytidine
0.00224
2',3'-dideoxy-CTP
Human immunodeficiency virus 1
-
-
0.015
2-acetyl-4-[4-(dimethylamino)phenyl]indeno[1,2-b]pyrrolo[3,2-e]pyridin-5(1H)-one
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0234 - 0.05
2-amino-3'-azido-2',3'-dideoxy-N,N-dimethyladenosine 5'-triphosphate
0.0441
2-amino-4-(3-benzoylphenyl)thiazole-5-carboxamide
Human immunodeficiency virus 1
-
0.118
2-amino-4-(3-bromo-4-chlorophenyl)thiazole-5-carboxamide
Human immunodeficiency virus 1
-
0.0544
2-amino-4-(3-chlorophenyl)thiazole-5-carboxamide
Human immunodeficiency virus 1
-
0.1254
2-amino-4-(3-iodophenyl)thiazole-5-carboxamide
Human immunodeficiency virus 1
-
0.0592
2-amino-4-(3-phenylphenyl)thiazole-5-carboxamide
Human immunodeficiency virus 1
-
0.0807
2-amino-4-phenylthiazole-5-carboxamide
Human immunodeficiency virus 1
-
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 - 0.0042
3'-azido-2',3'-dideoxy-2,6-diaminopurine-beta-D-ribofuranosyl 5'-triphosphate
0.0025 - 0.0308
3'-azido-2',3'-dideoxy-2-amino-6-chloropurine-beta-D-ribofuranosyl 5'-triphosphate
0.0244 - 0.1
3'-azido-2',3'-dideoxy-2-amino-6-methoxypurine-beta-D-ribofuranosyl 5'-triphosphate
0.0041 - 0.0218
3'-azido-2',3'-dideoxy-2-amino-6-N-allylaminopurine-beta-D-ribofuranosyl 5'-triphosphate
0.00016 - 0.0014
3'-azido-2',3'-dideoxyadenosine triphosphate
0.00006 - 0.00036
3'-azido-2',3'-dideoxyguanosine triphosphate
0.000002 - 0.000008
3'-azido-2',3'-dideoxythymidine
0.00002 - 0.00007
3'-azido-2',3'-dideoxythymidine-5'-triphosphate
0.042 - 0.06
3'-azido-3'deoxythymidine 5'-triphosphate
0.00006 - 0.0001
3'-dideoxythymidine triphosphate
0.000002 - 0.00002
3'-fluoro-2',3'-dideoxythymidine
0.000129
3,5-dimethyl-4-[[2-([1-[(4-nitrophenyl)methyl]-1,2,3,4-tetrahydropyridin-4-yl]amino)-5,7-dihydrothieno[3,4-d]pyrimidin-4-yl]oxy]benzonitrile
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.000092
3,5-dimethyl-4-[[2-([1-[(4-nitrophenyl)methyl]piperidin-4-yl]amino)-5,7-dihydrofuro[3,4-d]pyrimidin-4-yl]oxy]benzonitrile
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.000241
3,5-dimethyl-4-[[2-([1-[(4-nitrophenyl)methyl]piperidin-4-yl]amino)-6,7-dihydro-5H-cyclopenta[d]pyrimidin-4-yl]oxy]benzonitrile
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.000175
3,5-dimethyl-4-[[2-([1-[(4-nitrophenyl)methyl]piperidin-4-yl]amino)-6,7-dihydrothieno[3,2-d]pyrimidin-4-yl]oxy]benzonitrile
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.000094
3,5-dimethyl-4-[[2-([1-[(4-nitrophenyl)methyl]piperidin-4-yl]amino)-7,8-dihydro-6H-thiopyrano[3,2-d]pyrimidin-4-yl]oxy]benzonitrile
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.000072
3,5-dimethyl-4-[[2-([1-[(pyridin-4-yl)methyl]piperidin-4-yl]amino)-5,6,7,8-tetrahydroquinazolin-4-yl]oxy]benzonitrile
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.000056
3,5-dimethyl-4-[[2-([1-[(pyridin-4-yl)methyl]piperidin-4-yl]amino)-5,7-dihydrofuro[3,4-d]pyrimidin-4-yl]oxy]benzonitrile
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.000074
3,5-dimethyl-4-[[2-([1-[(pyridin-4-yl)methyl]piperidin-4-yl]amino)-6,7-dihydro-5H-cyclopenta[d]pyrimidin-4-yl]oxy]benzonitrile
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.000112
3,5-dimethyl-4-[[2-([1-[(pyridin-4-yl)methyl]piperidin-4-yl]amino)-6,7-dihydrothieno[3,2-d]pyrimidin-4-yl]oxy]benzonitrile
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.0643
3-(2-cyanoacetyl)phenyl diethyl phosphate
Human immunodeficiency virus 1
-
0.0041
3-(3-chlorophenyl)-3-oxopropanenitrile
Human immunodeficiency virus 1
-
0.0296
3-(3-iodophenyl)-3-oxopropanamide
Human immunodeficiency virus 1
-
0.000008 - 0.1
3-([3-bromo-2-oxo-5-[(pyridin-3-yloxy)methyl]-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
0.000008 - 0.000014
3-([3-bromo-2-oxo-5-[(pyridin-4-yloxy)methyl]-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
0.000001 - 0.000002
3-([3-bromo-5-fluoro-2-oxo-6-[2-(pyridin-4-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
0.000008 - 0.000017
3-([3-bromo-6-[2-(3-chlorophenyl)ethyl]-5-fluoro-2-oxo-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
0.000004 - 0.000016
3-([6-[2-(1,3-benzoxazol-2-yl)ethyl]-3-chloro-2-oxo-1,2-dihydropyridin-4-yl]oxy)-5-chlorobenzonitrile
0.0098
3-benzoyl-3-oxopropanenitrile
Human immunodeficiency virus 1
-
0.000021 - 0.000078
3-chloro-5-([3-chloro-2-oxo-6-[2-(pyridin-2-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
0.000016 - 0.000022
3-chloro-5-([3-chloro-2-oxo-6-[2-(pyridin-3-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
0.000014 - 0.000021
3-chloro-5-([3-chloro-2-oxo-6-[2-(pyridin-4-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
0.000002 - 0.000004
3-chloro-5-([3-chloro-6-methyl-2-oxo-5-[2-(pyridin-3-yl)ethyl]-1,2-dihydropyridin-4-yl]oxy)benzonitrile
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 - 0.000012
3-chloro-5-([3-chloro-6-[2-(3-chlorophenyl)ethyl]-2-oxo-1,2-dihydropyridin-4-yl]oxy)benzonitrile
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 - 0.000006
3-chloro-5-[[3-chloro-6-methyl-2-oxo-5-(phenoxymethyl)-1,2-dihydropyridin-4-yl]oxy]benzonitrile
0.0334
3-phenyl-3-oxopropanenitrile
Human immunodeficiency virus 1
-
0.000101
3-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-5,6,7,8-tetrahydroquinazolin-2-yl]amino]piperidin-1-yl)methyl]benzamide
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.000091
3-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-5,7-dihydrofuro[3,4-d]pyrimidin-2-yl]amino]piperidin-1-yl)methyl]benzamide
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.000241
3-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-6,7-dihydro-5H-cyclopenta[d]pyrimidin-2-yl]amino]piperidin-1-yl)methyl]benzamide
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.000094
3-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-6,7-dihydrothieno[3,2-d]pyrimidin-2-yl]amino]piperidin-1-yl)methyl]benzamide
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.000034 - 0.000071
3-[(5-benzyl-3-bromo-2-oxo-1,2-dihydropyridin-4-yl)oxy]-5-chlorobenzonitrile
0.000007 - 0.00001
3-[(5-benzyl-3-bromo-6-methyl-2-oxo-1,2-dihydropyridin-4-yl)oxy]-5-chlorobenzonitrile
0.00094
3-[11-(ethoxycarbonyl)-1,7,9,10,11,12-hexahydro-3,2-(metheno)-10-azaazuleno[1',8',7',6':3,4,5]cyclopenta[6,7]fluoreno[2,1,9,8-fghij]benzo[cd]cyclopenta[mno]acephenanthrylen-9-yl]-1-methylpyridinium
Human Immunodeficiency Virus
-
pH not specified in the publication, 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 - 0.000021
3-[[3-bromo-2-oxo-5-(pyridin-4-ylmethoxy)-1,2-dihydropyridin-4-yl]oxy]-5-chlorobenzonitrile
0.00014 - 0.00018
4'-ethynyl-2-amino-2'-deoxyadenosine triphosphate
0.00029 - 0.00043
4'-ethynyl-2-fluoro-2'-deoxyadenosine triphosphate
0.0163
4-(3-benzoylphenyl)thiazole-5-carboxamide
Human immunodeficiency virus 1
-
0.0099
4-(3-bromo-4-chlorophenyl)-1H-imidazole-5-carboxamide
Human immunodeficiency virus 1
-
0.0875
4-(3-bromo-4-chlorophenyl)thiazole-5-carboxamide
Human immunodeficiency virus 1
-
0.0798
4-(3-chlorophenyl)-1H-imidazole-5-carboxamide
Human immunodeficiency virus 1
-
0.0035
4-(3-iodophenyl)-3-oxobutanenitrile
Human immunodeficiency virus 1
-
0.000091
4-([2-[(1-[[4-(methanesulfonyl)phenyl]methyl]-1,2,3,4-tetrahydropyridin-4-yl)amino]-5,7-dihydrothieno[3,4-d]pyrimidin-4-yl]oxy)-3,5-dimethylbenzonitrile
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.0000989
4-([2-[(1-[[4-(methanesulfonyl)phenyl]methyl]piperidin-4-yl)amino]-5,6,7,8-tetrahydroquinazolin-4-yl]oxy)-3,5-dimethylbenzonitrile
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.000077
4-([2-[(1-[[4-(methanesulfonyl)phenyl]methyl]piperidin-4-yl)amino]-5,7-dihydrofuro[3,4-d]pyrimidin-4-yl]oxy)-3,5-dimethylbenzonitrile
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.000157
4-([2-[(1-[[4-(methanesulfonyl)phenyl]methyl]piperidin-4-yl)amino]-6,7-dihydro-5H-cyclopenta[d]pyrimidin-4-yl]oxy)-3,5-dimethylbenzonitrile
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.00013
4-([2-[(1-[[4-(methanesulfonyl)phenyl]methyl]piperidin-4-yl)amino]-6,7-dihydrothieno[3,2-d]pyrimidin-4-yl]oxy)-3,5-dimethylbenzonitrile
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.3
4-phenyl-1H-imidazole-5-carboxamide
Human immunodeficiency virus 1
-
0.283
4-phenylthiazole-5-carboxamide
Human immunodeficiency virus 1
-
0.018
4-[(3,5-dimethylphenyl)sulfanyl]quinolin-2(1H)-one
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000051
4-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-5,6,7,8-tetrahydroquinazolin-2-yl]amino]piperidin-1-yl)methyl]benzamide
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.000084
4-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-5,6,7,8-tetrahydroquinazolin-2-yl]amino]piperidin-1-yl)methyl]benzene-1-sulfonamide
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.000051
4-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-5,7-dihydrofuro[3,4-d]pyrimidin-2-yl]amino]piperidin-1-yl)methyl]benzamide
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.000109
4-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-5,7-dihydrofuro[3,4-d]pyrimidin-2-yl]amino]piperidin-1-yl)methyl]benzene-1-sulfonamide
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.00041
4-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-5,7-dihydrothieno[3,4-d]pyrimidin-2-yl]amino]piperidin-1-yl)methyl]benzene-1-sulfonamide
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.000073
4-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-6,7-dihydro-5H-cyclopenta[d]pyrimidin-2-yl]amino]piperidin-1-yl)methyl]benzamide
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.000091
4-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-6,7-dihydro-5H-cyclopenta[d]pyrimidin-2-yl]amino]piperidin-1-yl)methyl]benzene-1-sulfonamide
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.000066
4-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-6,7-dihydrothieno[3,2-d]pyrimidin-2-yl]amino]piperidin-1-yl)methyl]benzamide
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.000074
4-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)-6,7-dihydrothieno[3,2-d]pyrimidin-2-yl]amino]piperidin-1-yl)methyl]benzene-1-sulfonamide
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.0000026
4-[6-(4-methylpiperazin-1-yl)pyridin-3-yl]-1-(3-methoxypropyl)-8-(1-methyl-1H-pyrazol-4-yl)-2,5-dihydro-1H-indeno[1,2-d]pyrimidine
Human immunodeficiency virus 1
-
pH 7.8, 37°C
0.000115
4-[[2-([1-[(4-aminophenyl)methyl]piperidin-4-yl]amino)-5,7-dihydrothieno[3,4-d]pyrimidin-4-yl]oxy]-3,5-dimethylbenzonitrile
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
0.0004 - 0.0008
4-[[4-(4-chlorophenyl)piperazin-1-yl]methyl]-7,8-dihydroxy-2H-chromen-2-one
0.0011 - 0.0048
6-([4-[(4-cyanophenyl)amino]-1,3,5-triazin-2-yl]amino)-5,7-dimethylnaphthalene-2-carbonitrile
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
0.00008
9-(pyridin-3-yl)-1,7,9,10,11,12-hexahydro-3,2-(metheno)-10-azaazuleno[1',8',7',6':3,4,5]cyclopenta[6,7]fluoreno[2,1,9,8-fghij]benzo[cd]cyclopenta[mno]acephenanthrylene-11-carboxylic acid
Human Immunodeficiency Virus
-
pH not specified in the publication, temperature not specified in the publication
0.00092 - 0.00102
adefovir diphosphate
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 - 0.000411
capravirine
0.00152 - 0.0346
Delavirdine
0.000002 - 0.000432
efavirenz
0.0000046 - 0.0000679
GW8248
0.00464
Hygrophorus russula RNase
Human Immunodeficiency Virus
-
pH not specified in the publication, temperature not specified in the publication
-
40 - 50
KCl
mouse mammary tumor virus
-
IC50: 40-50 mM
0.01 - 0.021
lamivudine triphosphate
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
0.00014
N-[4-[(4-[[4-(4-cyano-2,6-dimethylphenoxy)thieno[3,2-d]pyrimidin-2-yl]amino]piperidin-1-yl)methyl]phenyl]methanesulfonamide
Human immunodeficiency virus 1
-
inhibition against wild-type enzyme, pH and temperature not specified in the publication
40 - 50
NaCl
mouse mammary tumor virus
-
IC50: 40-50 mM
0.00126
PHP protein
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
-
0.00151 - 0.0064
tenofovir diphosphate
0.0000126 - 0.0000647
TMC-125
0.00012 - 0.0027
zidovudine triphosphate
additional information
additional information
-
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
0.000003
1,14-di-3'-azido-2',3'-dideoxythymidine-tetradecanoate
Human immunodeficiency virus 1
-
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
0.00013
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
0.00058
1-butyl-4-[2-fluoro-4-(trifluoromethyl)phenyl]-5-oxo-1,5-dihydroindeno[1,2-b]pyrrolo[3,2-e]pyridine-3-carbonitrile
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0063
1-butyl-4-[2-fluoro-4-(trifluoromethyl)phenyl]-5-oxo-1,5-dihydroindeno[1,2-b]pyrrolo[3,2-e]pyridine-3-carbonitrile
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.00077
2',3'-dehydro-2',3'-deoxythymidine triphosphate
Xenotropic MuLV-related virus
pH 7.8, 37°C
0.00237
2',3'-dehydro-2',3'-deoxythymidine triphosphate
Moloney murine leukemia virus
-
pH 7.8, 37°C
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
0.0234
2-amino-3'-azido-2',3'-dideoxy-N,N-dimethyladenosine 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37°C, wild-type enzyme
0.05
2-amino-3'-azido-2',3'-dideoxy-N,N-dimethyladenosine 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37°C, mutant K65R
0.05
2-amino-3'-azido-2',3'-dideoxy-N,N-dimethyladenosine 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37°C, mutant L74V
0.05
2-amino-3'-azido-2',3'-dideoxy-N,N-dimethyladenosine 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37°C, mutant Q151M
0.00034
3'-azido-2',3'-dideoxy-2,6-diaminopurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37°C, mutant M184V
0.0008
3'-azido-2',3'-dideoxy-2,6-diaminopurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37°C, 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, 37°C, mutant L74V
0.0025
3'-azido-2',3'-dideoxy-2,6-diaminopurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37°C, mutant K65R
0.0042
3'-azido-2',3'-dideoxy-2,6-diaminopurine-beta-D-ribofuranosyl 5'-triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37°C, 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, 37°C, 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, 37°C, 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, 37°C, 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, 37°C, 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, 37°C, 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, 37°C, 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, 37°C, 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, 37°C, 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, 37°C, 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, 37°C, 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, 37°C, 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, 37°C, 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, 37°C, 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, 37°C, 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, 37°C, mutant Q151M
0.00016
3'-azido-2',3'-dideoxyadenosine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37°C, wild-type enzyme
0.00019
3'-azido-2',3'-dideoxyadenosine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37°C, mutant M184V
0.00042
3'-azido-2',3'-dideoxyadenosine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37°C, mutant L74V
0.0007
3'-azido-2',3'-dideoxyadenosine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37°C, mutant K65R
0.0014
3'-azido-2',3'-dideoxyadenosine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37°C, mutant Q151M
0.00006
3'-azido-2',3'-dideoxyguanosine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37°C, mutant M184V
0.00015
3'-azido-2',3'-dideoxyguanosine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37°C, wild-type enzyme
0.00025
3'-azido-2',3'-dideoxyguanosine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37°C, mutant L74V
0.0003
3'-azido-2',3'-dideoxyguanosine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37°C, mutant Q151M
0.00036
3'-azido-2',3'-dideoxyguanosine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37°C, 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
0.00003
3'-azido-2',3'-dideoxythymidine-5'-triphosphate
Human immunodeficiency virus 1
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
0.00006
3'-azido-2',3'-dideoxythymidine-5'-triphosphate
Human immunodeficiency virus 1
mutant enzyme N137A
0.00006
3'-azido-2',3'-dideoxythymidine-5'-triphosphate
Human immunodeficiency virus 1
mutant enzyme T139V
0.00006
3'-azido-2',3'-dideoxythymidine-5'-triphosphate
Human immunodeficiency virus 1
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
0.00009
3'-dideoxythymidine triphosphate
Human immunodeficiency virus 1
mutant enzyme I135M
0.0001
3'-dideoxythymidine triphosphate
Human immunodeficiency virus 1
mutant enzyme E138K
0.0001
3'-dideoxythymidine triphosphate
Human immunodeficiency virus 1
mutant enzyme N137A
0.0001
3'-dideoxythymidine triphosphate
Human immunodeficiency virus 1
mutant enzyme T139V
0.0001
3'-dideoxythymidine triphosphate
Human immunodeficiency virus 1
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
0.000008
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
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 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
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 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
0.000021
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
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
-
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
0.000006
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
0.000005
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
0.000006
3-chloro-5-[[3-chloro-6-methyl-2-oxo-5-(phenoxymethyl)-1,2-dihydropyridin-4-yl]oxy]benzonitrile
Human immunodeficiency virus 1
-
wild-type enzyme, pH and temperature not specified in the publication
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
0.000011
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 MuLV-related virus
pH 7.8, 37°C
0.00018
4'-ethynyl-2-amino-2'-deoxyadenosine triphosphate
Moloney murine leukemia virus
-
pH 7.8, 37°C
0.00029
4'-ethynyl-2-fluoro-2'-deoxyadenosine triphosphate
Moloney murine leukemia virus
-
pH 7.8, 37°C
0.00043
4'-ethynyl-2-fluoro-2'-deoxyadenosine triphosphate
Xenotropic MuLV-related virus
pH 7.8, 37°C
0.0004
4-[[4-(4-chlorophenyl)piperazin-1-yl]methyl]-7,8-dihydroxy-2H-chromen-2-one
Human immunodeficiency virus type 1 BH10
RNase H activity, presence of 10 mM Mg2+, pH 8.0, temperature not specified in the publication
0.0008
4-[[4-(4-chlorophenyl)piperazin-1-yl]methyl]-7,8-dihydroxy-2H-chromen-2-one
Human immunodeficiency virus type 1 BH10
RNase H activity, presence of 1 mM Mg2+, pH 7.4, temperature not specified in the publication
0.0011
6-([4-[(4-cyanophenyl)amino]-1,3,5-triazin-2-yl]amino)-5,7-dimethylnaphthalene-2-carbonitrile
Human immunodeficiency virus type 1 BH10
RNase H activity, presence of 10 mM Mg2+, pH 8.0, temperature not specified in the publication
0.0048
6-([4-[(4-cyanophenyl)amino]-1,3,5-triazin-2-yl]amino)-5,7-dimethylnaphthalene-2-carbonitrile
Human immunodeficiency virus type 1 BH10
RNase H activity, presence of 1 mM Mg2+, pH 7.4, temperature not specified in the publication
0.00092
adefovir diphosphate
Xenotropic MuLV-related virus
pH 7.8, 37°C
0.00102
adefovir diphosphate
Moloney murine leukemia virus
-
pH 7.8, 37°C
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
0.00016
d4T-TP
Human immunodeficiency virus 1
mutant enzyme E138K
0.00016
d4T-TP
Human immunodeficiency virus 1
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
0.00001
efavirenz
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
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
0.000188
efavirenz
Human immunodeficiency virus 1
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
0.01
lamivudine triphosphate
Moloney murine leukemia virus
-
pH 7.8, 37°C
0.021
lamivudine triphosphate
Xenotropic MuLV-related virus
pH 7.8, 37°C
0.00016
nevirapine
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.00028
nevirapine
Human immunodeficiency virus 1
-
-
0.00129
nevirapine
Human immunodeficiency virus 1
-
-
0.0017
nevirapine
Human immunodeficiency virus 1
-
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
0.00151
tenofovir diphosphate
Moloney murine leukemia virus
-
pH 7.8, 37°C
0.0064
tenofovir diphosphate
Xenotropic MuLV-related virus
pH 7.8, 37°C
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, 37°C, mutant M184V
0.00013
zidovudine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37°C, wild-type enzyme
0.00018
zidovudine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37°C, mutant L74V
0.00066
zidovudine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37°C, mutant K65R
0.0027
zidovudine triphosphate
Human immunodeficiency virus 1
-
pH 7.5, 37°C, mutant Q151M
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
-
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L180M
-
lamivudine-resistant mutant
M204V
-
lamivudine-resistant mutant
P306A
-
replication competency is reduced to 12.75% of the wild-type value
P306D
-
replication competency is increased to 121.57% of the wild-type value
P306E
-
replication competency is increased to 940.59% of the wild-type value
P306F
-
replication competency is reduced to 41.18% of the wild-type value
P306G
-
replication competency is reduced to 1.96% of the wild-type value
P306L
-
replication competency is increased to 128.04% of the wild-type value
P306R
-
replication competency is reduced to 20.26% of the wild-type value
P306S
-
replication competency is reduced to 47.25% of the wild-type value
P306T
-
replication competency is reduced to 4.5% of the wild-type value
P306V
-
replication competency is increased to 152.75% of the wild-type value
P306Y
-
replication competency is reduced to 10.98% of the wild-type value
A114G
-
mutant enzyme retains significant DNA polymerase activity. 5-6fold increase in the ability of the enzyme to discriminate against ddNTPs
A114S
-
mutant enzyme retains significant DNA polymerase activity, enzyme shows wild-type ddNTP/dNTP discrimination efficiency
A114T
-
mutant enzyme shows very low catalytic efficiency in nucleotide incorporation assays, due to the high KM-values for dNTP. Decreased susceptibility to AZTTP when poly(rA)/(dT)16 is used as substrate
A114V
-
mutant enzyme shows very low catalytic efficiency in nucleotide incorporation assays, due to the high KM-values for dNTP. Decreased susceptibility to AZTTP when poly(rA)/(dT)16 is used as substrate, enzyme shows wild-type ddNTP/dNTP discrimination efficiency
D67N/K70R/T215Y/K219Q
-
mutation results in a 1.5fold decrease in the rate constant for polymerization and a 2.5fold decrease in the equilibrium dissociation constant for 3'-azido-3'-deoxythymidine 5'-triphosphate compared to wild-type enzyme. These values translate into a 4fold decrease in selectivity for 3'-azido-3'-deoxythymidine 5'-monophosphate incorporation ba the mutant enzyme as compared to wild-type enzyme for RNA dependent DNA replication. No such decrease in selectivity is detected for DNA dependent replication
E478Q
-
polymerization activity of mutant E478Q that inactivates the RNase H catalytic site is much more sensitive to efavirenz than the wild type
G190V
mutant with high level of resistance to efavirenz and nevirapine
I132A
mutation confers low-level resistance to nevirapine and delavirdine
I132M
mutation confers high-level resistance to nevirapine and delavirdine (more than 10fold) and low-level resistance (about 2fold) to efavirenz
I135A
mutation confers high level resistance to nevirapine and delavirdine, but not to efavirenz
I135M
mutation confers low-level resistance (about 2fold) to nevirapine, delavirdine and efavirenz
K101E/G190S/M41lL/T215Y
-
patient isolate. Efavirenz stimulates the RNase H of an reverse transcriptase from a patient-derived virus that is highly resistant and grows more rapidly in the presence of low concentrations of efavirenz
K101R
non-nucleoside reverse transcriptase inhibitor resistance mutation
K103N/Y181C
-
mutation shows only moderate effects on either polymerase or RNAse H inhibitory potencies of GW8248 and TMC-125. IC50 for nevirapine is strongly enhanced. 1.3fold increase in IC50-value for capravirine, 21.8fold increase in IC50-value for efavirenz
K103R
non-nucleoside reverse transcriptase inhibitor resistance mutation
K65R/L74V
-
84fold decrease of the catalytic rate constant. Virus replication capacity is severely impaired relative to wild-type enzyme. Poor ability of K65R/L74V RT to use natural nucleotides relative to wild-type enzyme: 15% that of wild-type enzyme for dATP, 36% for dGTP, 50% for dTTP, and 25% for dCTP
K65R/V75I
-
a HIV-1 O RT variant that shows increased fidelity and stability compared to the wild-type enzyme
L74V
-
site-directed mutagenesis
M230D
non-nucleoside reverse transcriptase inhibitor resistance mutation
M230N
non-nucleoside reverse transcriptase inhibitor resistance mutation
N136A
mutant enzyme with very low reverse transcriptase activity
N137A
mutation confers no resistance to nevirapine, delavirdine and efavirenz
P140A
mutant enzyme with very low reverse transcriptase activity
Q151A
severe reduction in the polymerase activity withoput any significant effect on the affinity for dNTP substrate. The mutant is nearly devoid of diphosphorolytic activity on a RNA/primer-binding-site template-primer
Q151M
-
site-directed mutagenesis
Q258C/C280S
the engineered reverse transcriptase protein (Q258C and C280S mutations) cross-linked to the dsDNA primer/template (20-mer/27-mer) containing the N2-cystamine 2'-deoxyguanosine six bases upstream from the priming site (P site) was used for the crystallographic studies
R78A
-
a HIV-1 O RT variant that shows increased fidelity and stability compared to the wild-type enzyme
T139A
mutant enzyme with very low reverse transcriptase activity
T139V
mutation confers no resistance to nevirapine, delavirdine and efavirenz
V148I
-
reduced dNTP binding affinity, mutation V148I disrupts positioning of Q151 for interaction with the 3'-OH of the incoming dTTP, mutant enzyme binds to AZTTP 18 times more tightly than to dTTP
V197I
non-nucleoside reverse transcriptase inhibitor resistance mutation
Y1152-naphthyl-Tyr
-
mutant of the p66 subunit of reverse transcriptase reconstituted with wild-type p51 subunit. Mutant enzyme inefficiently incorporates dCTP at low concentrations and is kinetically slower with all dCTP analogues tested. 5fold less efficient for dCTP incorporation and 15fold less efficient for 2',3'-dideoxy-CTP incorporation compared to the wild-type enzyme
Y115aminomethyl-Phe
-
mutant of the p66 subunit of reverse transcriptase reconstituted with wild-type p51 subunit. Mutant enzyme incorporates dCTP more efficiently than the wild-type and is resistant to the chain terminator (-)-beta-2',3'-dideoxy-3'-thiacytidine triphosphate when examined in a steady-state fidelity assay. Mutant enzyme incorporates very little 3TCMP, even when the concentration of the chain terminator was 100times that of the dCTP
Y188L
-
mutation shows only moderate effects on either polymerase or RNAse H inhibitory potencies of GW8248 and TMC-125. IC50 for nevirapine is strongly enhanced. 47.8fold increase in IC50-value for capravirine, 58fold increase in IC50-value for efavirenz
Q294A
-
the mutation has no significant effect on the noticeable level of the DNA polymerase activity of the enzyme (12% increase of activity compared to the wild type enzyme)
Q294C
-
the mutation has no significant effect on the noticeable level of the DNA polymerase activity of the enzyme (34% increase of activity compared to the wild type enzyme)
Q294E
-
the mutation has no significant effect on the noticeable level of the DNA polymerase activity of the enzyme (11% increase of activity compared to the wild type enzyme)
Q294H
-
the mutation has no significant effect on the noticeable level of the DNA polymerase activity of the enzyme (16% increase of activity compared to the wild type enzyme)
Q294M
-
the mutation has no significant effect on the noticeable level of the DNA polymerase activity of the enzyme (4% increase of activity compared to the wild type enzyme)
Q294N
-
the mutation has no significant effect on the noticeable level of the DNA polymerase activity of the enzyme (36% increase of activity compared to the wild type enzyme)
Q294P
-
the mutation has no significant effect on the noticeable level of the DNA polymerase activity of the enzyme (13% increase of activity compared to the wild type enzyme)
Q294R
-
the mutation has no significant effect on the noticeable level of the DNA polymerase activity of the enzyme (35% increase of activity compared to the wild type enzyme)
Q294S
-
the mutation has no significant effect on the noticeable level of the DNA polymerase activity of the enzyme (19% increase of activity compared to the wild type enzyme)
Q294W
-
the mutation has no significant effect on the noticeable level of the DNA polymerase activity of the enzyme (13% increase of activity compared to the wild type enzyme)
Q294Y
-
the mutation has no significant effect on the noticeable level of the DNA polymerase activity of the enzyme (3% increase of activity compared to the wild type enzyme)
A502V
-
site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme
A644V
-
site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme
D200N
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
D200N/L603W/T330P/L139P/E607K
-
site-directed mutagenesis, highly processive and thermostable multiply-mutated M-MuLV RT variant with 65fold improvement in comparison to the wild-type enzyme, the maximum temperature of the full-length cDNA synthesis is raised to 62°C, compared to 45°C for the wild-type enzyme
D524A
-
mutant exhibits similar dissociation constants for heteropolymeric DNA/DNA (2.9-6.5 nM) and RNA/DNA complexes (1.2-2.9 nM) like wild-type. Unlike the WT, the mutant enzymes is devoid of RNase H activity, and not able to degrade RNA in RNA/DNA complexes
E286R
-
mutant exhibits similar dissociation constants for heteropolymeric DNA/DNA (2.9-6.5 nM) and RNA/DNA complexes (1.2-2.9 nM) like wild-type. Unlike the WT, the mutant enzymes is devoid of RNase H activity, and not able to degrade RNA in RNA/DNA complexes
E286R/E302K/L435R/D524A
-
mutant exhibits similar dissociation constants for heteropolymeric DNA/DNA (2.9-6.5 nM) and RNA/DNA complexes (1.2-2.9 nM) like wild-type. Unlike the WT, the mutant enzymes is devoid of RNase H activity, and not able to degrade RNA in RNA/DNA complexes
E302K
-
mutant exhibits similar dissociation constants for heteropolymeric DNA/DNA (2.9-6.5 nM) and RNA/DNA complexes (1.2-2.9 nM) like wild-type. Unlike the WT, the mutant enzymes is devoid of RNase H activity, and not able to degrade RNA in RNA/DNA complexes
E607K
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
F155V
the mutation increase the affinity of the enzyme for ribonucleotides, without affecting the Vmax for catalysis, and thereby conferrs to the enzyme significant RNA polymerase activity
F625S
-
site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme
H126R
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
K103R
-
site-directed mutagenesis, the mutant is resistant to inhibition by tenofovir and 3'-azido-3'-deoxythymidine
K658R
-
site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme
L139P
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
L333Q
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
L435R
-
mutant exhibits similar dissociation constants for heteropolymeric DNA/DNA (2.9-6.5 nM) and RNA/DNA complexes (1.2-2.9 nM) like wild-type. Unlike the WT, the mutant enzymes is devoid of RNase H activity, and not able to degrade RNA in RNA/DNA complexes
L603W
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
L671P
-
site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme
M428L
-
site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme
N649S
-
site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme
P130S
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
P65S
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
Q190M
-
site-directed mutagenesis, the mutant is resistant to inhibition by tenofovir and 3'-azido-3'-deoxythymidine
Q84A
mutant enzyme displays higher DNA polymerase activities than wild-type enzyme. Vmax of Q84AH using dTTP as a substrate is about three times that of wild-type value, whereas the Km values are very similar
Q84A/F155V
Q84A mutation further improves RNA polymerase and DNA polymerase activity of mutant F155V
Q84N
mutant enzyme displays higher DNA polymerase activities than wild-type enzyme
T287A
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
T330P
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
W388R
-
site-directed mutagenesis, the mutant shows increased thermostability and -performance compared to the wild-type enzyme
Y344H
-
site-directed mutagenesis, the mutant shows decreased thermostability and -performance compared to the wild-type enzyme
D211N
-
still capable of in vitro polymerization, although it is blocked for in vivo transposition. D211N mutation has minimal effect on nucleotide binding but reduces the kpol by about 230fold. The mutation reduces binding affinity for both Mn2+ and Mg2+
F292A
-
slight diminuation in DNA-dependent DNA synthesis (under conditions allowing multiple rounds of synthesis). Significant reduction in polymerase activity in presence of heparin
F292Y
-
severly impaired Rnase H activity
G294A
-
mutation results in enhanced pausing at multiple positions of the DNA template in DNA-dependent DNA synthesis (under conditions allowing multiple rounds of synthesis). Significant reduction in polymerase activity in presence of heparin
Y298A
-
slight diminuation in DNA-dependent DNA synthesis (under conditions allowing multiple rounds of synthesis). Significant reduction in polymerase activity in presence of heparin
Y298W
-
significant reduction in polymerase activity in presence of heparin
F227L
-
mutant shows 2 to 3fold increase in infectivity
G211S
-
mutant shows 2 to 3fold increase in infectivity
I148V
-
mutant shows 2 to 3fold increase in infectivity
I257M
-
mutant shows 2 to 3fold increase in infectivity
K412E
-
mutant demonstrates a 12fold increase in infectivity compared to the parental virus SIVmneCl8 indicating a role for mutations in the connection domain of reverse transcriptase in influencing viral infectivity and replication
R173K
-
mutant shows 2 to 3fold increase in infectivity
T288A
-
mutant shows 2 to 3fold increase in infectivity
V108I
-
mutant shows 2 to 3fold increase in infectivity
F227L
-
mutant shows 2 to 3fold increase in infectivity
-
I257M
-
mutant shows 2 to 3fold increase in infectivity
-
K412E
-
mutant demonstrates a 12fold increase in infectivity compared to the parental virus SIVmneCl8 indicating a role for mutations in the connection domain of reverse transcriptase in influencing viral infectivity and replication
-
R173K
-
mutant shows 2 to 3fold increase in infectivity
-
V108I
-
mutant shows 2 to 3fold increase in infectivity
-
C232A
mutation in CP2 motif, modest defect in RNA binding
F230A
mutation in CP2 motif, no effect on RNA binding
H234A
mutation in CP2 motif, modest defect in RNA binding
I229A
mutation in CP2 motif, modest defect in RNA binding
R226A
mutation in CP2 motif, strong defect in RNA binding
R237A
mutation in CP2 motif, strong defect in RNA binding
Y231A
mutation in CP2 motif, no effect on RNA binding
D215A
-
enzyme mutant devoid of 3'-5' exonuclease activity
F388A
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
L329A
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
L329A/Q384A
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
L329A/Y438A
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
M408A
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
Q384A
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
Q384A/Y438A
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
T326A
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
Y438A
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
F388A
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
-
L329A
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
-
Q384A
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
-
T326A
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
-
Y438A
-
site-directed mutagenesis, the mutant exhibits DNA-dependent and RNA-dependent DNA polymerase activities, while the wild-type enzyme is a DNA-depedent DNA polymerase
-
A608T/E520G/W827R
-
substitution rates per base for RNA-dependent DNA is similar or lower than that of avian myeloblastosis virus reverse transcriptase. Rate constants kcat of about two orders of magnitude larger than those of the Stoffel fragment
M747K/E742K
-
substitution rates per base for RNA-dependent DNA is similar to that of avian myeloblastosis virus reverse transcriptase
M761T/D547G/I584V
-
fidelity which is about 10-times higher than that of avian myeloblastosis virus reverse transcriptase. Almost tenfold improved catalytic efficiency as measured by the kcat/Km ratio when compared with the Stoffel fragment
N483Q/S486Q/T539N/Y545Q/D547T/P548Q/A570Q/D578Q/A597T/W604R/S612N/V730L/R736Q/S739N/M747R
-
selection of a polymerase with 15 mutations, mostly located at the template binding interface, by directed evolution of Thermus aquaticus DNA polymerase I, the mutant enzyme is a single variant of the Stoffel fragment of Taq DNA polymerase I, the enzyme shows broad template specificity and is a thermostable DNA-dependent and RNA-dependent DNA-polymerase, see also EC 2.7.7.7
K103R
site-directed mutagenesis, the mutant is resistant to inhibition by tenofovir and 3'-azido-3'-deoxythymidine
Q190M
site-directed mutagenesis, the mutant is resistant to inhibition by tenofovir and 3'-azido-3'-deoxythymidine
K103N
-
site-directed mutagenesis
K103N
-
mutation shows only moderate effects on either polymerase or RNAse H inhibitory potencies of GW8248 and TMC-125. IC50 for nevirapine is strongly enhanced. 1.6fold decrease in IC50-value for capravirine, 18.8fold increase in IC50-value for efavirenz
K103N
-
site-directed mutagenesis, the DNA polymerase function of the enzyme is sensitive to alizarine inhibitors like the wild-type enzyme
K103N
-
clinically important mutant
K65R
-
site-directed mutagenesis
K65R
-
exhibits an 8-fold resistance to ddATP. 22fold decrease of the catalytic rate constant
K65R
-
mutant maintains a susceptibility to GS-9148 that is similar to wild type enzyme
K65R
-
a HIV-1 O RT variant that shows increased fidelity and stability compared to the wild-type enzyme
M184V
-
site-directed mutagenesis
M184V
-
mutant maintains a susceptibility to GS-9148 that is similar to wild type enzyme
M184V
the fidelity of DNA polymerization of the mutant HIV-1 RT is significantly higher than that of wild-type enzyme
Q151N
-
reduced dNTP binding affinity, mutant loses the interaction with the 3'-OH of the incoming dTTP, mutant enzyme binds to AZTTP 12 times more tightly than to dTTP
Q151N
-
mutant is catalytically active only at high dNTP concentrations because of its reduced dNTP binding affinity. The modified HIV-1 vector harboring the Q151N mutant reverse transcriptase preferentially transduces tumor cells containing higher cellular dNTP concentrations than primary cells (e.g. human lung fibroblasts and human keratinocytes). The wild type HIV-1 vector transduces both human lung fibroblasts and tumor cells. The Q151N vector fails to transduce human lung fibroblasts and keratinocytes but efficiently transduces tumor cells. Pretreatment of human lung fibroblasts with deoxynucleosides, which increase cellular dNTP pools, enables the mutant vector to transduce human lung fibroblasts, suggesting that the transduction failure of the RT mutant vector to primary cells is because of inefficient reverse transcription in low cellular dNTP environments
Y181C
-
site-directed mutagenesis
Y181C
-
mutation shows only moderate effects on either polymerase or RNAse H inhibitory potencies of GW8248 and TMC-125. IC50 for nevirapine is strongly enhanced. 2.1fold increase in IC50-value for capravirine, IC50 for efavirenz is nearly identical to wild-type value
Y181C
-
site-directed mutagenesis, the DNA polymerase function of the enzyme is insensitive to alizarine inhibitors
Y181C
-
clinically important mutant
M184V
-
the fidelity of DNA polymerization of the mutant HIV-1 RT is significantly higher than that of wild-type enzyme
-
M184V
-
the fidelity of DNA polymerization of the mutant HIV-1 RT is significantly higher than that of wild-type enzyme
-
additional information
-
the isolated RNase H domain of HIV-1 reverse transcriptase is inactive. Two chimeric proteins, carrying the hybrid binding domain of either Thermotoga maritima RNase H1 or Geobacillus stearothermophilus RNase H2 bind to RNA/DNA hybrids more strongly than the RNase H domain of HIV and exhibit enzymatic activity in the presence of Mn2+ ions. Activity in the presence of Mg2+ ions is very weak or absent
additional information
multi-drug resistant (MR) HIV-1 reverse transcriptase (RT), subcloned from a patient derived subtype CRF02 AG, harboring 45 amino acid exchanges, amongst them four thymidine analog mutations (TAMs) relevant for high-level AZT (azidothymidine) resistance by AZTMP excision (M41L, D67N, T215Y, K219E) as well as four substitutions of the AZTTP discrimination pathway (A62V, V75I, F116Y and Q151M). In addition, K65R, known to antagonize AZTMP excision in HIV-1 subtype B is present. Analyses with subtype B reverse transcriptase indicates that K65R and the TAM T215F/Y are not compatible in the absence of the Q151M complex and are rarely found if Q151M or Q151M and at least two additional mutations of the complex are present. A strong functional antagonism of K65R and T215F/Y in the presence of two or more additional TAMs may exist. Subtype AGMR reverse transcriptase which harbors K65R, T215F and three additional TAMs concomitantly is still functional as a polymerase and RNase H. Moreover, in the presence of the Q151M complex K65R does not lead to AZT sensitivity. In the MR-RT, AZT resistance appears to be retained via the discrimination pathway. Only if both codons 65 and 151 of the discrimination pathway are restored to the WT residues (i.e. K65, M151), excision can occur, indicating that both exchanges are essential to prevent excision
additional information
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multi-drug resistant (MR) HIV-1 reverse transcriptase (RT), subcloned from a patient derived subtype CRF02 AG, harboring 45 amino acid exchanges, amongst them four thymidine analog mutations (TAMs) relevant for high-level AZT (azidothymidine) resistance by AZTMP excision (M41L, D67N, T215Y, K219E) as well as four substitutions of the AZTTP discrimination pathway (A62V, V75I, F116Y and Q151M). In addition, K65R, known to antagonize AZTMP excision in HIV-1 subtype B is present. Analyses with subtype B reverse transcriptase indicates that K65R and the TAM T215F/Y are not compatible in the absence of the Q151M complex and are rarely found if Q151M or Q151M and at least two additional mutations of the complex are present. A strong functional antagonism of K65R and T215F/Y in the presence of two or more additional TAMs may exist. Subtype AGMR reverse transcriptase which harbors K65R, T215F and three additional TAMs concomitantly is still functional as a polymerase and RNase H. Moreover, in the presence of the Q151M complex K65R does not lead to AZT sensitivity. In the MR-RT, AZT resistance appears to be retained via the discrimination pathway. Only if both codons 65 and 151 of the discrimination pathway are restored to the WT residues (i.e. K65, M151), excision can occur, indicating that both exchanges are essential to prevent excision
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introduction of N- and C-terminal deletions into simian foamy virus proteaase-reverse transcriptase. Both, the RNase H domain and the connection subdomain contribute substantially to polymerase integrity and stability as well as to polymerase activity and substrate binding. The 42 amino acids long region C-terminal of the protease domain is important for polymerase stability and activity. Protease activation via binding of PR-RT to viral RNA requires the presence of the full length virus proteaase-reverse transcriptase including the RNase H domain. Deletions either at the C- or N-terminus of protease-reverse transcriptase disturb the structural integrity of the proteins. Isolated reverse transcriptase domains RT(107-454) and PR-RT(1-454) exhibit very little polymerization and extension activity
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construction of deletions at the 3' terminus of the gene results in a 4fold increase in the level of the reverse transcriptase activity in the soluble fraction of crude lysates
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generation of enzyme mutants with increased thermostability using compartmentalized ribosome display evolution in vitro technique, overview. Identification of a large set of mutations that enable cDNA synthesis at elevated temperatures. Altered substrate-binding affinity and progressivity of mutant enzymes, overview
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Z derivatives have the fingers domain of Tgo-Pol replaced with that from Pol zeta, insertion of the Pol zeta finger domains into the Thermococcus gorgonarius Tgo-Pol resulting in the Z derivatives increase the enzyme activity. Z1 shows increased activity, which is further increased with Z2, created by fusion of Z1 with the processivity-increasing DNA binding protein Sso7d, overview
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chimeric DNA polymerase, termed CS5 pol, constructed from T. Z05 pol and Tma pol and containing the 5'-3' nuclease domain from Thermus sp. Z05 DNA polymerase (residues 1-291) and the 3'-5' exonuclease and polymerase domains from Thermotoga maritima DNA polymerase (residues 292-893). This chimera retains thermostable DNA polymerase activity, as well as proofreading activity. Using the CS5 chimera, a series of mutant proteins is constructed in which the amino acid side chains are mutated to modulate the 3'-5'?exonuclease activity. A thermoactive and thermostable enzyme with reverse transcriptase and 3'-5'exonuclease activity is described
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directed polymerase-evolution experiment yields variants endowed with RNA-dependent DNA polymerization. To further estimate the fidelity during reverse transcription, the variants A608T/E520G/W827R, M747K/E742K, and M761T/D547G/I584V are used to copy a part of messenger RNA(mRNA) into complementary DNA (cDNA) prior to subcloning for sequencing of reverse transcription products. The sequences showsd that selected variants can polymerize more than 300 nucleotides and are not limited to the addition of single nucleotides at the 3 end of DNA primers. The substitution rates per base for RNA-dependent DNA polymerization of the most active variants, A608T/E520G/W827R and M747K/E742K are similar or lower than that of avian myeloblastosis virus reverse transcriptase, which is used as a standard. The most abundant variant and M761T/D547G/I584V has a fidelity which is about 10-times higher than that of avian myeloblastosis virus reverse transcriptase
additional information
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chimeric DNA polymerase, termed CS5 pol, constructed from T. Z05 pol and Tma pol and containing the 5'-3' nuclease domain from Thermussp. Z05 DNA polymerase (residues 1-291) and the 3'-5' exonuclease and polymerase domains from Thermotoga maritima DNA polymerase (residues 292-893). This chimera retains thermostable DNA polymerase activity, as well as proofreading activity. Using the CS5 chimera, a series of mutant proteins is constructed in which the amino acid side chains are mutated to modulate the 3'-5' exonuclease activity. A thermoactive and thermostable enzyme with reverse transcriptase and 3'-5'?exonuclease activity is described
additional information
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chimeric DNA polymerase, termed CS5 pol, constructed from T. Z05 pol and Tma pol and containing the 5'-3' nuclease domain from Thermussp. Z05 DNA polymerase (residues 1-291) and the 3'-5' exonuclease and polymerase domains from Thermotoga maritima DNA polymerase (residues 292-893). This chimera retains thermostable DNA polymerase activity, as well as proofreading activity. Using the CS5 chimera, a series of mutant proteins is constructed in which the amino acid side chains are mutated to modulate the 3'-5' exonuclease activity. A thermoactive and thermostable enzyme with reverse transcriptase and 3'-5'?exonuclease activity is described
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