Information on EC 3.1.26.13 - retroviral ribonuclease H:
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EC NUMBERCOMMENTARY
3.1.26.13-

RECOMMENDED NAMEGeneOntology No.
retroviral ribonuclease H-

REACTIONREACTION DIAGRAMCOMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.
show the reaction diagram		----
Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.
show the reaction diagram		cleavage reaction mechanism and substrate specificity of HIV-1 RNase H, overviewHuman immunodeficiency virus 1P03366717535

REACTION TYPEORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

PATHWAYKEGG LinkMetaCyc Link
No entries in this field

SYSTEMATIC NAMEIUBMB Comments
No entries in this field

SYNONYMSORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
HIV-1 reverse transcriptaseHuman immunodeficiency virus 1P03366-717535
HIV-1 RT-associated RNase HHuman immunodeficiency virus 1--716995
human immunodeficiency virus reverse transcriptaseHuman immunodeficiency virus 1--650155
human immunodeficiency virus reverse transcriptase-associated ribonuclease HHuman immunodeficiency virus 1--715864
M-MuLV RT RNase HMoloney murine leukemia virus--716354
ribonuclease HHuman immunodeficiency virus 1--707709, 714972, 715864, 716995, 717535
ribonuclease HHuman Immunodeficiency Virus--714908
ribonuclease HHuman immunodeficiency virus 2--716995
RNase HHuman immunodeficiency virus 1--650155, 690924, 696192, 707709, 713770, 713774, 714475, 714972, 715532, 715864, 716064, 716067, 716827, 716993, 716994, 716995, 717535
RNase HMoloney murine leukemia virus--707794, 714822, 715859
RNase HHuman Immunodeficiency Virus--714908
RNase HHuman immunodeficiency virus 2--716995
RT-RNase HHuman Immunodeficiency Virus, Moloney murine leukemia virus--696182

CAS REGISTRY NUMBERCOMMENTARY
9050-76-4-

ORGANISMCOMMENTARYLITERATURESEQUENCE CODESEQUENCE DB SOURCE
Avian myeloblastosis virus-696182--Manually annotated by BRENDA team
Human Immunodeficiency Virus-696182, 696185, 698685, 698709--Manually annotated by BRENDA team
Human Immunodeficiency VirusHIV-1714908--Manually annotated by BRENDA team
Human immunodeficiency virus 1-652865, 652907, 665720, 666034, 695644, 695645, 696181, 696183, 696189, 696192, 696194, 698692, 698694, 698701, 699509, 699893, 699894, 700927, 701025, 701113, 701116, 701216, 701386, 708108, 709451, 710132, 710144, 710674--Manually annotated by BRENDA team
Human immunodeficiency virus 1-707178, 707509, 710577P03366UniProtManually annotated by BRENDA team
Human immunodeficiency virus 1; HIV-1707709--Manually annotated by BRENDA team
Human immunodeficiency virus 1derived from clade B; derived from clade C; derived from CRF01 A_E693579--Manually annotated by BRENDA team
Human immunodeficiency virus 1HIV-1650155, 690924, 713770, 713774, 714475, 714972, 715532, 715864, 716067, 716827, 716993, 716994, 716995--Manually annotated by BRENDA team
Human immunodeficiency virus 1HIV-1716064P0C6F2UniProtManually annotated by BRENDA team
Human immunodeficiency virus 1HIV-1717535P03366UniProtManually annotated by BRENDA team
Human immunodeficiency virus 1 HXB-2HIV-1715532--Manually annotated by BRENDA team
Human immunodeficiency virus 2HIV-2716995--Manually annotated by BRENDA team
Human immunodeficiency virus 2strain D-194, low level of RNase H activity; strain ROD, low level of RNase H activity652865--Manually annotated by BRENDA team
Human immunodeficiency virus 2 D-194strain D-194, low level of RNase H activity652865--Manually annotated by BRENDA team
Human immunodeficiency virus 2 RODstrain ROD, low level of RNase H activity652865--Manually annotated by BRENDA team
Moloney murine leukemia virus-643436, 665720, 666034, 693579, 695645, 696182, 698714, 699509, 699895, 701049, 707794, 710674, 715859, 716354--Manually annotated by BRENDA team
Moloney murine leukemia virusMoMuLV714822--Manually annotated by BRENDA team
murine leukemia virus-698711--Manually annotated by BRENDA team
Saccharomyces cerevisiaeretrotransposon Ty3, gypsy-group652277--Manually annotated by BRENDA team

GENERAL INFORMATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
malfunctionMoloney murine leukemia virus-antiviral activity of 2-hydroxy-4-methoxycarbonylisoquinoline-1,3(2H,4H)-dione is probably due to the RNase H inhibition715859
malfunctionHuman immunodeficiency virus 1-severe defects in RNase H activity alone, exemplified by the P236L mutant, appear sufficient to cause a substantial reduction in fitness. Reductions in reverse transcriptase content decrease both polymerization and RNase H activity in virions716067
malfunctionMoloney murine leukemia virus-PEGylation as a tool for engineering the M-MuLV RT derivative deficient in RNase H activity, overview716354
physiological functionMoloney murine leukemia virus-increasing the stoichiometry of RNase H relative to the amount of functional DNA polymerase by virions engineered to contain phenotypic mixtures of wild-type and RNase H catalytic site point mutant D524N reverse transcriptase, has minimal effects on direct repeat deletion frequency. DNA synthesis is error prone when directed principally by RNase H mutant reverse transcriptase, suggesting a role for RNase H catalytic integrity in the fidelity of intracellular reverse transcription699895
physiological functionMoloney murine leukemia virus-the retroviral RNase H degrades the RNA template following first strand synthesis, generates primers for second strand synthesis, and eliminates the t-RNA primer714822
physiological functionHuman immunodeficiency virus 1-the reverse transcriptase generates an RNA/DNA hybrid that is a substrate for RNase H. The RNA/DNA hybrid is degraded to generate a nascent minus-strand single-stranded DNA. As DNA synthesis proceeds, RNase H degrades the RNA strand716994
physiological functionHuman immunodeficiency virus 1, Human immunodeficiency virus 2-the process of reverse transcription involves the copying of the single-stranded RNA of the viral genome into double-stranded DNA. This requires that reverse transcriptase is able to act at times as a RNA-dependent DNA polymerase, a DNA-dependent DNA polymerase, and as an RNase H that cleaves the RNA of RNA/DNA hybrids. These activities are coordinated temporally and spatially. As all three of these processes are absolutely required for the successful completion of reverse transcription, role of RNase H in (+)-strand priming and in strand transfer and (-)-strand primer removal, overview716995
physiological functionHuman immunodeficiency virus 1P03366the enzyme activity and substrate specificity is controlled by the RNase H primer grip, and the width of the minor groove and the trajectroy of the RNA:DNA, both in a sequence-dependent manner717535
malfunctionHuman immunodeficiency virus 1-patients treated with nucleoside reverse transcriptase inhibitors develop classical patterns of resistance-associated mutations in the pol domain. Thymidine analogue mutations, TAMs, arise with zidovudine and stavudine treatment, which encompass M41L, D67N, K70R, L210W, T215F/Y, and K219Q/E/N. Different patterns of thymidine analogue mutations accumulate in patients, which segregate into two distinct pathways named TAM-1 and TAM-2. The TAM-1 pathway includes M41L, L210W and T215Y, whereas the TAM-2 pathway includes D67N, K70R, T215F and K219Q/E/N716993
additional informationMoloney murine leukemia virus-catalytically important residues of the RNase H activity are Asp524 and Asp583707794
additional informationHuman immunodeficiency virus 1-HIV-1 reverse transcriptase has two associated activities, DNA polymerase and RNase H, both essential for viral replication and validated drug targets714972
additional informationHuman immunodeficiency virus 1-the active site of RNase H consists of four highly conserved carboxylate residues, D443, E478, D498, and D549, and requires Mg2+ or Mn2+ for its catalytic activity716827
additional informationHuman immunodeficiency virus 1-RT is a unique viral protein containing two enzymatic properties, i.e. RNase H cleavage activity and RNA- and DNA-dependent DNA polymerase activity716993
additional informationHuman immunodeficiency virus 1-the RNase H activity, which degrades RNA from RNA/DNA hybrids endonucleolytically, is part of the HIV reverse transcriptase716994
additional informationHuman immunodeficiency virus 1-role of RNase H activity in drug resistance, the RNase H domains can affect the susceptibility of RT to non-nucleoside reverse transcriptase inhibitors and nucleos(t)ide reverse transcriptase inhibitors. Furthermore, RNase H activity itself is implicated in the mechanism of resistance to nucleoside reverse transcriptase inhibitors such as 3'-azidodeoxythymidine, and also to non-nucleoside reverse transcriptase inhibitors such as nevirapine. RNase H exists as a domain in the larger enzyme HIV-1 reverse transcriptase, structure and function of HIV-1 RNase H, overview716995
additional informationHuman immunodeficiency virus 2-Q294 is highly conserved in HIV-2 isolates716995
additional informationHuman immunodeficiency virus 1P03366the polypurine tract, PPT, a purine-rich segment from the HIV-1 genome, is resistant to RNase H cleavage and is used as a primer for second DNA strand synthesis. PPT-enzyme complex structure, detailed overview717535

SUBSTRATEPRODUCT                      REACTION DIAGRAMORGANISM UNIPROT ACCESSION NO. COMMENTARY/
Substrate		 LITERATURE/
Substrate		 COMMENTARY/
Product		 LITERATURE/
Product		 Reversibility
r=reversible
ir=irreversible
?=not specified
5'-end-labeled 267 nt-long RNA annealed to 20 nt-long synthetic DNA + H2O?
show the reaction diagram		Human immunodeficiency virus 1--652907--?
5'-rGrGrGrCrGrArArUrUrCrGrArGrCrUrCrGrGrUrArCrCrC-dGdGdGdGdAdTdCdCdTdCdTdAdG-3'/3'-dTdCdGdAdGdCdCdAdTdGdGdG-dCdCdCdCdTdAdGdGdAdGdTdC-5' + H2O5'-rGrGrGrCrGrArArUrUrCrGrArGrCrUrCrGrGrUrArCrCrC/dGdGdGdGdAdTdCdCdTdCdTdAdG-3' + 3'-dTdCdGdAdGdCdCdAdTdGdGdG/dCdCdCdCdTdAdGdGdAdGdTdC-5'
show the reaction diagram		Avian myeloblastosis virus-model substrate, designed to be structurally similar to the DNA-extended tRNA created by initiation of minus-strand DNA synthesis during retroviral replication, contains sequences from the HIV genome and sequences unrelated to the HIV viral genome696182hydrolyzation of the phosphodiester bond at the DNA-RNA junction-?
5'-rGrGrGrUrCrCrCrUrGrUrUrCrGrGrGrCrGrCrCrA-dCdTdGdCdTdAdGdAdGdAdTdTdTdTdT-3'/3'-dGdAdCdAdAdGdCdCdCdGdCdGdGdT-dGdAdCdGdAdTdCdTdCdTdAdAdAdAdA-5' + H2O5'-rGrGrGrUrCrCrCrUrGrUrUrCrGrGrGrCrGrCrCrA/dCdTdGdCdTdAdGdAdGdAdTdTdTdTdT-3' + 3'-dGdAdCdAdAdGdCdCdCdGdCdGdGdT/dGdAdCdGdAdTdCdTdCdTdAdAdAdAdA-5'
show the reaction diagram		Avian myeloblastosis virus-model substrate containing sequences from the HIV genome, designed to be structurally similar to the DNA-extended tRNA created by initiation of minus-strand DNA synthesis during retroviral replication. The DNA-extended RNA was a template and was annealed to a DNA oligonucleotide that primed reverse transcription of the RNA in the template696182hydrolyzation of the phosphodiester bond at the DNA-RNA junction-?
5-rGrGrGrCrGrArArUrUrCrGrArGrCrUrCrGrGrUrArCrCrC-dGdGdGdGdAdTdCdCdTdCdTdAdG-3 + 3-dTdCdGdAdGdCdCdAdTdGdGdG-dCdCdCdCdTdAdGdGdAdGdTdC-5' + H2O?
show the reaction diagram		Moloney murine leukemia virus, Human Immunodeficiency Virus-model substrate, designed to be structurally similar to the DNA-extended tRNA created by initiation of minus-strand DNA synthesis during retroviral replication, contains sequences from the HIV genome and sequences unrelated to the HIV viral genome696182hydrolysis of the substrate to leave a single ribonucleotide 5-phosphate at the 5-terminus of the model DNA genome-?
5-rGrGrGrUrCrCrCrUrGrUrUrCrGrGrGrCrGrCrCrA-dCdTdGdCdTdAdGdAdGdAdTdTdTdTdT-3 + 3-dGdAdCdAdAdGdCdCdCdGdCdGdGdT-dGdAdCdGdAdTdCdTdCdTdAdAdAdAdA-5 + H2O?
show the reaction diagram		Moloney murine leukemia virus-model substrate containing sequences from the HIV genome, designed to be structurally similar to the DNA-extended tRNA created by initiation of minus-strand DNA synthesis during retroviral replication. The DNA-extended RNA is a template and is annealed to a DNA oligonucleotide that primed reverse transcription of the RNA in the template696182hydrolysis of the substrate to leave a single ribonucleotide 5-phosphate at the 5-terminus of the model DNA genome-?
poly(A)+ mRNA primed with oligo(dT) + H2Odouble-stranded DNA copies between 1.3 and 9.9 kilobases in length + ?
show the reaction diagram		Moloney murine leukemia virus-multifunctional enzyme containing RNase H and reverse transcriptase activity643436--?
poly(dC)-poly(rG) + H2O?
show the reaction diagram		Human Immunodeficiency Virus--698685--?
poly(dT)-poly(rA) + H2O?
show the reaction diagram		Human Immunodeficiency Virus-substrate poly(dC)-poly(rG) is markedly preferred over substrate poly(dT)-poly(rA)698685--?
poly(rA)/oligo(dT)+ H2O?
show the reaction diagram		Human immunodeficiency virus 1- synthetic hybrid698692--?
poly(rA)n-poly(dT)n + H2O?
show the reaction diagram		Human immunodeficiency virus 1--652907--?
poly(rG)/poly(dC) + H2O?
show the reaction diagram		Moloney murine leukemia virus, Human immunodeficiency virus 1--695645--?
RNA-DNA hybrid containing the polypurine tract + H2O?
show the reaction diagram		Moloney murine leukemia virus-extension of the polypurine tract primer by at least 2 nucleotides is sufficient for recognition and correct cleavage by RNase H at the RNA-DNA junction to remove the primer. Primer removal occurs by cleavage one nucleotide away from the RNA-DNA junction. The same polypurine tract specificity determinants responsible for generation of the polypurine tract primer also direct polypurine tract primer removal. Once the primer has been extended and removed from the nascent plus-strand DNA, reinitiation at the resulting plus-strand primer terminus does not occur698714--?
RNA:DNA hybrid + H2OAMP + ?
show the reaction diagram		Moloney murine leukemia virus--643436--?
5-rGrGrGrUrCrCrCrUrGrUrUrCrGrGrGrCrGrCrCrA-dCdTdGdCdTdAdGdAdGdAdTdTdTdTdT-3 + 3-dGdAdCdAdAdGdCdCdCdGdCdGdGdT-dGdAdCdGdAdTdCdTdCdTdAdAdAdAdA-5 + H2O?
show the reaction diagram		Human Immunodeficiency Virus-model substrate containing sequences from the HIV genome, designed to be structurally similar to the DNA-extended tRNA created by initiation of minus-strand DNA synthesis during retroviral replication. The DNA-extended RNA was a template and was annealed to a DNA oligonucleotide that primed reverse transcription of the RNA in the template696182hydrolyzation of the substrate to leave a single ribonucleotide 5-phosphate at the 5-terminus of the model DNA genome-?
additional information?-Moloney murine leukemia virus-a nick separating an upstream RNA and a downstream RNA annealed to DNA is essentially ignored by RNase H, indicating that the RNA 5' end at a nick is not sufficient to position 5' end-directed cleavages. Cleavage sites that are located close to the 5' end of the downstream RNA are not recognized in the absence of the upstream RNA, and the 5' ends of the shorter upstream RNAs enhance cleavage at these sites. The recognition of an internal cleavage site depends on local sequence features found both upstream and downstream of the cleavage site, designated as the -1/+1 position. Preferred nucleotides have been identified in the flanking sequences spanning positions -11 to +1666034---
additional information?-Human immunodeficiency virus 1-a nick separating an upstream RNA and a downstream RNA annealed to DNA is essentially ignored by RNase H, indicating that the RNA 5' end at a nick is not sufficient to position 5' end-directed cleavages. Cleavage sites that are located close to the 5' end of the downstream RNA are not recognized in the absence of the upstream RNA, and the 5' ends of the shorter upstream RNAs enhance cleavage at these sites. The recognition of an internal cleavage site depends on local sequence features found both upstream and downstream of the cleavage site, designated as the -1/+1 position. Preferred nucleotides have been identified in the flanking sequences spanning positions -14 to +1666034---
additional information?-Human Immunodeficiency Virus-evaluation of activity by enzyme's ability to select and extend the 3' polypurine tract primers into (+) strand DNA. Evaluation via concerted and two-step reactions for (+) strand priming, the latter of which allows discrimination between selection end extension events698709 3' polypurine tract primer selection appears to represent a specialized form of RNase H activity that is more sensitive to minor structural alterations within this domain--
additional information?-Human immunodeficiency virus 1-interdependence of the polymerase and RNase H activities of HIV-1 reverse transcription during viral DNA synthesis701025---
additional information?-Human Immunodeficiency Virus-no substrate: single-stranded RNA or the DNA component of DNA-RNA hybrids. Products consist primarily of monomers, dimers, and trimers with 3'-OH groups698685---
additional information?-Human immunodeficiency virus 1-RNase H acts at or about 14 to 18 nucleotides from the 5' end of the template, the cleavage site for the RNase H is therefore held at around this distance behind the DNA polymerase activity. For the intact protein, the RNase H and reverse transcriptase activities may work in a coupled or coordinate manner. More than 80% of the residual 5' oligonucleotides remain base paired to the RNA-directed DNA product. Under certain conditions, these short RNAs can act as efficient primers for an associated DNA-directed DNA synthesis in the reverse direction699894---
additional information?-Human immunodeficiency virus 1-study on specificity of RNase H cleavage by use of synthetic DNA-RNA hybrids based on the same 81-base RNA template. First series of RNase H substrates is prepared with complementary DNA oligonucleotides of different lengths, ranging from 6 to 20 nucleotides, all of which share a common 5' end and are successively shorter at their 3' ends. The second series of oligonucleotides has a common 3' end but shorter 5' ends. The DNA oligonucleotides in the third series are all 20 bases long but have non-complementary stretches at either the 5' end, 3' end, or both ends. Enzyme cleaves fairly efficiently if the duplex region is at least eight bases long, but not if it is shorter. Although enzyme requires the substrate to have a region of RNA-DNA duplex, Moloney murine leukemia virus RT can cleave RNA outside the region that is part of the RNA-DNA duplex. The polymerase domain of HIV-1 RT uses certain mismatched segments of RNA-DNA to position the enzyme for RNase H cleavage. A mismatched region near the RNase H domain can interfere with RNase H cleavage, cleavage is usually but not always more efficient if the mismatched segment is deleted699509---
additional information?-Moloney murine leukemia virus-study on specificity of RNase H cleavage by use of synthetic DNA-RNA hybrids based on the same 81-base RNA template. First series of RNase H substrates is prepared with complementary DNA oligonucleotides of different lengths, ranging from 6 to 20 nucleotides, all of which share a common 5' end and are successively shorter at their 3' ends. The second series of oligonucleotides has a common 3' end but shorter 5' ends. The DNA oligonucleotides in the third series are all 20 bases long but have non-complementary stretches at either the 5' end, 3' end, or both ends. Enzyme cleaves fairly efficiently if the duplex region is at least eight bases long, but not if it is shorter. Although enzyme requires the substrate to have a region of RNA-DNA duplex, Moloney murine leukemia virus RT can cleave RNA outside the region that is part of the RNA-DNA duplex. The polymerase domain of Moloney murine leukemia virus RT does not use the same mismatched segments to define the position for RNase H cleavage699509---
additional information?-Human immunodeficiency virus 1-substrate heteropolymeric 90-nt 5' end-labeled RNA template-annealed to a 36-nt DNA primer is cleaved by wild-type p66/p51 RT precisely at the RNA/DNA junction to liberate a 20-nt (+) strand DNA696189---
additional information?-Human immunodeficiency virus 1-substrates consist of SP6 runoff transcripts from a portion of the gag region of the HIV-1 genome hybridized to complementary single-stranded DNA from either an M 13 subclone or a phagemid transcription vector subclone. The corresponding hybrids are fully base-paired696181products formed from the fully complementary hybrid consist of a nonuniform distribution of oligonucleotides ranging in size from 4 to 15 nt--
additional information?-Human immunodeficiency virus 1-substrates consist of SP6 runoff transcripts from a portion of the gag region of the HIV-1 genome hybridized to complementary single-stranded DNA from either an M 13 subclone or a phagemid transcription vector subclone. The corresponding hybrids carry a 5'-mismatch of seven nucleotides696181products are a few prominent intermediates of 24-42 nt in size with relatively little accumulation of larger products--
additional information?-Human Immunodeficiency Virus-the HIV polymerase and RNase H active sites are separated by a distance equivalent to the length of a 15-nucleotide RNA-DNA heteroduplex696182---
additional information?-Human immunodeficiency virus 1-the recognition and precise cleavage of the polypurine tract of the human immunodeficiency virus type 1 is an essential step in HIV-1 reverse transcription. Mutations at positions 2 and 5 of the 3'-end of the polypurine tract do significantly alter the cleavage specificity at the polypurine tract/U3 junction. The structure of the polypurine tract primer, rather than the base-specific contacts between the polypurine tract and HIV-1 RT, are the primary determinants of RNase H cleavage specificity at the polypurine tract/U3 junction701386---
additional information?-Human immunodeficiency virus 1-the selection of 5' end-directed cleavage sites by retroviral RNases H results from a combination of nucleotide sequence, permissible distance, and accessibility to the RNA 5' end. Enzyme strongly prefers A or U at the +1 position and C or G at the -2 position, and A is disfavored at the -4 position. 5' End-directed cleavages occur when sites are positioned between the 13th and 20th nucleotides from the RNA 5' end. The extent of 5' end-directed cleavages observed in substrates containing a free recessed RNA 5' end is most comparable to substrates with a gap of 2 or 3 bases between the upstream and downstream RNAs665720---
additional information?-Moloney murine leukemia virus-the selection of 5' end-directed cleavage sites by retroviral RNases H results from a combination of nucleotide sequence, permissible distance, and accessibility to the RNA 5' end. Enzyme strongly prefers A or U at the +1 position and C or G at the -2 position. 5' End-directed cleavages occurr when sites are positioned between the 13th and 20th nucleotides from the RNA 5' end. The extent of 5' end-directed cleavages observed in substrates containing a free recessed RNA 5' end is most comparable to substrates with a gap of 2 or 3 bases between the upstream and downstream RNAs665720---
additional information?-Human immunodeficiency virus 1-5'end-directed RNase H of reverse transcriptase716067---
additional information?-Human immunodeficiency virus 1-HIV-1 reverse transcriptase has two enzymatic functions, DNA polymerase and RNase H activities714475---
additional information?-Moloney murine leukemia virus-Moloney murine leukemia virus reverse transcriptase, M-MuLV RT, is a domain structured enzyme that has the N-terminally located DNA polymerization activity and C-terminally located RNase H activity, which interferes with the efficient synthesis of long cDNA molecules716354---
additional information?-Moloney murine leukemia virus-Moloney murine leukemia virus reverse transcriptase, MMLV RT, shows DNA polymerization activity and RNase H activity. Stabilization of the reverse transcriptase activity by eliminating the RNase H activity, overview707794---
additional information?-Moloney murine leukemia virus-retroviral reverse transcriptase also possesses a ribonuclease H activity, an enzyme which cleaves the RNA strand of RNA/DNA hetroduplex714822---
additional information?-Human immunodeficiency virus 1, Human immunodeficiency virus 2-RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids, substrate binding and reaction mechanism, overview716995---
additional information?-Human immunodeficiency virus 1-cleavage of DNA-RNA and RNA-DNA primer templates715532---
additional information?-Moloney murine leukemia virus-DNA binding by M-MuLV RT assay using 5'-end labeled 48/36 bp RNA-DNA oligonucleotide duplex, method, overview. RNA-DNA hybrid binding and 5'-end labeled 48/36 bp RNA-DNA oligonucleotide duplex by M-MuLV RT derivatives, overview716354---
additional information?-Human immunodeficiency virus 1-RNA-DNA duplex substrate from a 41-mer 5'-labeled 32P-heteropolymeric RNA template kim40R annealed to complementary 32-mer DNA oligomer kim32D713770---
additional information?-Human immunodeficiency virus 1-RNA-DNA substrate716827---
additional information?-Human immunodeficiency virus 1-RNA-DNA substrate in a tRNA removal assay, the cleavage patterns for the recombinant HIV-1 reverse transcriptase and mutant p51-G-TCR construct correspond to the release of the 11mer RNA, corresponding with the authentic cleavage identified in vivo. The relative activity of the isolated HIV-1 RNaseH(p51-G-TCR) is comparable to that of the full-length HIV reverse transcriptase713774---
additional information?-Human immunodeficiency virus 1P0C6F2RNA/DNA hybrid duplex substrate716064---
additional information?-Human immunodeficiency virus 1-substrate is 18-nucleotide 3'-fluourescein-labeled RNA annealed to a complementary 18-nucleotide 5'-dabsyl-labeled DNA715864---
additional information?-Moloney murine leukemia virus-substrate is a 3H-UTP-labeled RNA: RNA-DNA hybrid, synthesis, overview714822---
additional information?-Moloney murine leukemia virus-the active site of the RNase H function contains four acidic residues, D443, E478, D498, and D549, that likely coordinate two divalent metal ions that are essential for catalysis715859---
additional information?-Human immunodeficiency virus 1-the tC5U-p12 hybrid is used as reaction substrate the RNase H activity714972---
additional information?-Human immunodeficiency virus 1-conserved residues in the connection subdomain and C-terminal ribonuclease H, RNase H, domain of HIV-1 RT contact the nascent DNA primer and modulate the trajectory of the template relative to the RNase H catalytic center. Within the RNase H domain, these residues include Thr473, Glu475, Lys476, Tyr501, and Ile505, while His539 and Asn474 interact with the scissile phosphate of the RNA template,m substrate recognition and binding, overview650155---
additional information?-Human immunodeficiency virus 1-a 5'-32P-labeled AZT-MP chain-terminated RNA/DNA template/primer substrate690924---

NATURAL SUBSTRATESNATURAL PRODUCTSREACTION DIAGRAMORGANISM UNIPROT ACCESSION NO.COMMENTARY SUBSTRATELITERATURE
(Substrate)		COMMENTARY PRODUCTLITERATURE
(Product)
additional information?-Human immunodeficiency virus 1-5'end-directed RNase H of reverse transcriptase716067--
additional information?-Human immunodeficiency virus 1-HIV-1 reverse transcriptase has two enzymatic functions, DNA polymerase and RNase H activities714475--
additional information?-Moloney murine leukemia virus-Moloney murine leukemia virus reverse transcriptase, M-MuLV RT, is a domain structured enzyme that has the N-terminally located DNA polymerization activity and C-terminally located RNase H activity, which interferes with the efficient synthesis of long cDNA molecules716354--
additional information?-Moloney murine leukemia virus-Moloney murine leukemia virus reverse transcriptase, MMLV RT, shows DNA polymerization activity and RNase H activity. Stabilization of the reverse transcriptase activity by eliminating the RNase H activity, overview707794--
additional information?-Moloney murine leukemia virus-retroviral reverse transcriptase also possesses a ribonuclease H activity, an enzyme which cleaves the RNA strand of RNA/DNA hetroduplex714822--
additional information?-Human immunodeficiency virus 1, Human immunodeficiency virus 2-RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids, substrate binding and reaction mechanism, overview716995--
additional information?-Human immunodeficiency virus 1-conserved residues in the connection subdomain and C-terminal ribonuclease H, RNase H, domain of HIV-1 RT contact the nascent DNA primer and modulate the trajectory of the template relative to the RNase H catalytic center. Within the RNase H domain, these residues include Thr473, Glu475, Lys476, Tyr501, and Ile505, while His539 and Asn474 interact with the scissile phosphate of the RNA template,m substrate recognition and binding, overview650155--

COFACTORORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATUREIMAGE
No entries in this field

METALS and IONS ORGANISM UNIPROT ACCESSION NO.COMMENTARY LITERATURE
Ca2+Moloney murine leukemia virus-Ca2+ is non-competent analogue of the Mg2+ ion cofactor716354
K+Human immunodeficiency virus 1-required713774
KClHuman Immunodeficiency Virus-optimum concentration 50 mM698685
Mg2+Moloney murine leukemia virus-required for synthesis of long DNA strands643436
Mg2+Human immunodeficiency virus 1-required650155, 690924, 714972, 716064
Mg2+Human Immunodeficiency Virus-required, with more than 90% of maximum activity between 4 and 12 mM698685
Mg2+Moloney murine leukemia virus-Mn2+ is preferred over Mg2+. One-metal catalytic mechanism for the Mn2+/Mg2+-dependent activities701049
Mg2+Moloney murine leukemia virus-dependent on707794
Mg2+Human immunodeficiency virus 1-prefered over Mn2+710674
Mg2+Moloney murine leukemia virus-may substitute for Mn2+710674
Mg2+Human immunodeficiency virus 1-dependent on713774
Mg2+Moloney murine leukemia virus-required715859, 716354
Mg2+Human immunodeficiency virus 1-required for catalytic activity716827
Mg2+Human immunodeficiency virus 1, Human immunodeficiency virus 2-one Mg2+ ion in the RNase H active site, required716995
Mn2+Moloney murine leukemia virus-required for synthesis of long DNA strands643436
Mn2+Human Immunodeficiency Virus-required for hydrolysis of double-stranded RNA696185
Mn2+Moloney murine leukemia virus-activation at 0.01-1 mM, inhibitory above. Mn2+ is preferred over Mg2+. One-metal catalytic mechanism for the Mn2+/Mg2+-dependent activities701049
Mn2+Human immunodeficiency virus 1-solid state strucuture, two Mn2+ ions bound to the RNase H active site709451
Mn2+Human immunodeficiency virus 1-may partially substitute for Mg2+710674
Mn2+Moloney murine leukemia virus-prefered over Mg2+710674
Mn2+Human immunodeficiency virus 1-modeling of the HIV-1 RNase H domain in complex with an inhibitor and two Mn2+ cations from crystal structure of manicol-bound enzyme715864
Mn2+Human immunodeficiency virus 1-activates, required for catalytic activity716827
additional informationHuman immunodeficiency virus 1-in the crystal structure, two divalent metal cations bind in the active site surrounded by a cluster of four conserved acidic amino acid residues701216
additional informationMoloney murine leukemia virus-the active site of the RNase H function contains four acidic residues, D443, E478, D498, and D549, that likely coordinate two divalent metal ions that are essential for catalysis715859
additional informationHuman immunodeficiency virus 1P0C6F2metal coordination, structure, overview716064

INHIBITORSORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
(2S)-5,7-dihydroxy-2-(2-hydroxy-1-(phenylsulfonyl)propan-2-yl)-9-methyl-3,4-dihydro-1H-benzo[7]annulen-6(2H)-oneHuman immunodeficiency virus 1--715864 2D-image
(4-N,N-dimethylaminobenzoyl)-2-hydroxy-1-naphthyl hydrazoneHuman immunodeficiency virus 1-specific716995-
(6,6,12,12,18,18,18-heptaoxido-5,7,11,13,17-pentaoxa-6l5,12l5,18l5-triphosphaoctadec-1-yl)phosphonateMoloney murine leukemia virus--714822 2D-image
1,2-bis(2-oxopropoxy)anthracene-9,10-dioneHuman immunodeficiency virus 1-9% inhibition714972 2D-image
1,2-bis[(3-oxobutan-2-yl)oxy]anthracene-9,10-dioneHuman immunodeficiency virus 1-20% inhibition714972 2D-image
1,2-dihydroxyanthracene-9,10-dioneHuman immunodeficiency virus 1-i.e. alizarine, 8% inhibition714972 2D-image
1,3,4,5-tetrahydrogalloylapitolHuman immunodeficiency virus 1--715864 2D-image
1,6,8-trihydroxy-3-methylanthraquinoneHuman immunodeficiency virus 1-i.e. frangula-emodin708108-
1-(2-2-hydroxyethoxymethyl)-6-(phenylthio)thymineHuman immunodeficiency virus 1--716994-
2'-deoxy-2'-fluoro-P-thioadenylyl-(3'->5')-guanosineHuman immunodeficiency virus 1-40% inhibition of RNase H at 0.05 microM695645-
2'-deoxy-P-thioguanylyl-(3'->5')-guanosineHuman immunodeficiency virus 1-65% inhibition of RNase H at 0.05 microM695645-
2,7-dihydroxy-4-(propan-2-yl)cyclohepta-2,4,6-trien-1-oneHuman immunodeficiency virus 1-inhibition of enzymatic activity, but no antiviral effect709451 2D-image
2,7-dihydroxy-4-(propan-2-yl)cyclohepta-2,4,6-trien-1-oneHuman immunodeficiency virus 1--716995 2D-image
2,7-dihydroxy-4-isopropyl-cyclohepta-2,4,6-trieneHuman immunodeficiency virus 1-i.e. beta-thujaplicinol715864-
2-(1,2-dihydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-oneHuman immunodeficiency virus 1--715864 2D-image
2-(1-benzylamino-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-oneHuman immunodeficiency virus 1--715864 2D-image
2-(2,3-dihydro-1H-inden-1-ylamino)-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
2-(2,3-dihydro-1H-inden-2-ylamino)-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
2-(2-benzylsulfanyl-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-oneHuman immunodeficiency virus 1--715864 2D-image
2-(2-diethylamino-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-oneHuman immunodeficiency virus 1--715864 2D-image
2-(2-ethanesulfonyl-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-oneHuman immunodeficiency virus 1--715864 2D-image
2-(2-ethylsulfanyl-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-oneHuman immunodeficiency virus 1--715864 2D-image
2-(3,4-dichlorobenzyl)-5,6-dihydroxypyrimidine-4-carboxylic acidHuman immunodeficiency virus 1-inhibition of enzymatic activity, but no antiviral effect709451 2D-image
2-(3,4-dichlorobenzyl)-5,6-dihydroxypyrimidine-4-carboxylic acidHuman immunodeficiency virus 1--716995 2D-image
2-(3-bromo-4-methoxybenzyl)-5,6-dihydroxypyrimidine-4-carboxylic acidHuman immunodeficiency virus 1-inhibition of enzymatic activity, but no antiviral effect709451-
2-(tert-butylamino)-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
2-amino-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
2-amino-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamideHuman immunodeficiency virus 1--716995 2D-image
2-hydroxy-4-(2-phenyl)ethylisoquinoline-1,3(2H,4H)-dioneHuman Immunodeficiency Virus-enol-form714908 2D-image
2-hydroxy-4-(3-phenyl)propylisoquinoline-1,3(2H,4H)-dioneHuman Immunodeficiency Virus-mixture of th mixed ketoenol forms or keto-form714908-
2-hydroxy-4-(4-methylbenzyl)isoquinoline-1,3(2H,4H)-dioneHuman Immunodeficiency Virus-mixture of th mixed ketoenol forms or keto-form714908-
2-hydroxy-4-(4-trifluoromethylbenzyl)isoquinoline-1,3(2H-4H)-dioneHuman Immunodeficiency Virus-keto-form714908 2D-image
2-hydroxy-4-butylisoquinoline-1,3(2H,4H)-dioneHuman Immunodeficiency Virus-mixture of th mixed ketoenol forms or keto-form714908-
2-hydroxy-4-ethylisoquinoline-1,3(2H,4H)-dioneHuman Immunodeficiency Virus--714908 2D-image
2-hydroxy-4-isopropylisoquinoline-1,3(2H,4H)-dioneHuman Immunodeficiency Virus--714908 2D-image
2-hydroxy-4-methoxycarbonylisoquinoline-1,3(2H,4H)-dioneMoloney murine leukemia virus-shows antiviral activity715859-
2-hydroxy-4-methylisoquinoline-1,3(2H,4H)-dioneHuman Immunodeficiency Virus--714908 2D-image
2-hydroxy-4-methylisoquinoline-1,3(2H,4H)-dioneMoloney murine leukemia virus--715859 2D-image
2-hydroxy-4-pentylisoquinoline-1,3(2H,4H)-dioneHuman Immunodeficiency Virus--714908 2D-image
2-hydroxy-4-propylisoquinoline-1,3(2H,4H)-dioneHuman Immunodeficiency Virus--714908 2D-image
2-hydroxyisoquinoline-1,3(2H,4H)-dioneHuman immunodeficiency virus 1-inhibition of enzymatic activity, but no antiviral effect709451 2D-image
2-hydroxyisoquinoline-1,3(2H,4H)-dioneHuman Immunodeficiency Virus--714908 2D-image
2-hydroxyisoquinoline-1,3(2H,4H)-dioneMoloney murine leukemia virus--715859 2D-image
2-hydroxyisoquinoline-1,3(2H,4H)-dioneHuman immunodeficiency virus 1--716995 2D-image
2-hydroxyisoquinoline-1,3(2H,4H)-dione magnesium complexMoloney murine leukemia virus--715859-
2-oxo-2-(1,2,3,4-tetrahydronaphthalen-1-ylamino)ethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
2-oxo-2-(propan-2-yloxy)ethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
2-oxo-2-(tetrahydrofuran-2-ylamino)ethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
2-oxo-2-[(2,3,4-trichlorophenyl)amino]ethyl benzyl(phenyl)carbamodithioateHuman immunodeficiency virus 1--707709 2D-image
2-oxo-2-[(2,3,4-trichlorophenyl)amino]ethyl dibenzylcarbamodithioateHuman immunodeficiency virus 1--707709 2D-image
2-oxo-2-[(2-phenylpropan-2-yl)amino]ethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
2-[(2,3,4-trichlorophenyl)amino]-2-oxoethyl dibenzylcarbamodithioateHuman immunodeficiency virus 1-inhibitor indentified by FRET-based high-throughput screening assay707709-
2-[(2,4-dichlorophenyl)amino]-2-oxoethyl dibenzylcarbamodithioateHuman immunodeficiency virus 1--707709 2D-image
2-[(2,4-dimethylphenyl)amino]-2-oxoethyl dibenzylcarbamodithioateHuman immunodeficiency virus 1-; inhibitor indentified by FRET-based high-throughput screening assay707709 2D-image
2-[(2-methoxy-5-methylphenyl)amino]-2-oxoethyl benzyl(phenyl)carbamodithioateHuman immunodeficiency virus 1--707709 2D-image
2-[(2-methyl-1-phenylpropan-2-yl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
2-[(2-methylbutan-2-yl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
2-[(3-cyanophenyl)amino]-2-oxoethyl benzyl(phenyl)carbamodithioateHuman immunodeficiency virus 1--707709 2D-image
2-[(3-cyanophenyl)amino]-2-oxoethyl dibenzylcarbamodithioateHuman immunodeficiency virus 1--707709 2D-image
2-[(4-hydroxybenzyl)(tetrahydrofuran-2-ylmethyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
2-[2-(2-fluoro-benzylamino)-1-hydroxy-1-methyl-ethyl]-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-oneHuman immunodeficiency virus 1--715864 2D-image
2-[2-(4-bromophenyl)-2-oxoethoxy]-9,10-dioxo-9,10-dihydroanthracen-1-yl acetateHuman immunodeficiency virus 1--714972 2D-image
2-[2-(biphenyl-4-yl)-2-oxoethoxy]-9,10-dioxo-9,10-dihydroanthracen-1-yl acetateHuman immunodeficiency virus 1--714972 2D-image
2-[4-benzyl-5-(benzylsulfanyl)-4H-1,2,4-triazol-3-yl]pyridineHuman immunodeficiency virus 1-; inhibitor indentified by FRET-based high-throughput screening assay707709 2D-image
2-[4-benzyl-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]pyridineHuman immunodeficiency virus 1--707709 2D-image
2-[benzyl(tetrahydrofuran-2-ylmethyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
2-[bis(4-methoxyphenyl)(phenyl)methoxy]ethyl 2-cyanoethyl dipropan-2-ylphosphoramidoiteMoloney murine leukemia virus--714822 2D-image
2-[tert-butyl(2-phenylethyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
2-[tert-butyl(3-nitrobenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
2-[tert-butyl(3-oxo-3-phenylpropyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
2-[tert-butyl(3-phenylpropyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
2-[tert-butyl(4-fluorobenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
2-[tert-butyl(4-methoxybenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
2-[tert-butyl(4-nitrobenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
2-[tert-butyl(pentafluorobenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
2-[tert-butyl(phenyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
2-[tert-butyl[2-(trifluoromethyl)benzyl]amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
2-[tert-butyl[3-(trifluoromethyl)benzyl]amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
2-[tert-butyl[4-(trifluoromethyl)benzyl]amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
2-[[2-(acetyloxy)benzyl](tert-butyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
2-[[4-(acetyloxy)benzyl](tert-butyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
2-[[4-(benzyloxy)benzyl](tert-butyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
3,3-dimethyl-2-oxobutyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1--714475 2D-image
3,4-dihydroxy-N'-[(E)-(2-methoxynaphthalen-1-yl)methylidene]benzohydrazideHuman immunodeficiency virus 1--716995 2D-image
3-(furan-2-yl)-4-(4-methoxybenzyl)-5-[[4-(trifluoromethyl)benzyl]sulfanyl]-4H-1,2,4-triazoleHuman immunodeficiency virus 1--707709 2D-image
3-(furan-2-yl)-4-phenyl-5-[[4-(trifluoromethyl)benzyl]sulfanyl]-4H-1,2,4-triazoleHuman immunodeficiency virus 1--707709 2D-image
3-cyclopentyl-1,4-dihydroxy-1,8-naphthyridin-2(1H)-oneHuman immunodeficiency virus 1P0C6F2-716064 2D-image
3-[2-(4-bromophenyl)-2-oxoethoxy]-1,8-dihydroxy-6-methylanthracene-9,10-dioneHuman immunodeficiency virus 1--708108-
3-[4-(2-methyl-imidazo[4,5-c]pyridin-1-yl)-benzyl]-3H-benzothiazol-2-oneHuman immunodeficiency virus 1--716994-
4-([[4-benzyl-5-(furan-2-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]methyl)pyridineHuman immunodeficiency virus 1--707709 2D-image
4-([[4-benzyl-5-(thiophen-2-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]methyl)pyridineHuman immunodeficiency virus 1-; inhibitor indentified by FRET-based high-throughput screening assay707709 2D-image
4-benzyl-2-hydroxy-isoquinoline-1,3(2H,4H)-dioneHuman Immunodeficiency Virus-keto-form; mixture of th mixed ketoenol forms714908 2D-image
4-benzyl-3-(benzylsulfanyl)-5-(furan-2-yl)-4H-1,2,4-triazoleHuman immunodeficiency virus 1-; inhibitor indentified by FRET-based high-throughput screening assay707709 2D-image
4-benzyl-3-(benzylsulfanyl)-5-(thiophen-2-yl)-4H-1,2,4-triazoleHuman immunodeficiency virus 1-; inhibitor indentified by FRET-based high-throughput screening assay707709 2D-image
4-benzyl-3-(benzylsulfanyl)-5-phenyl-4H-1,2,4-triazoleHuman immunodeficiency virus 1-; inhibitor indentified by FRET-based high-throughput screening assay707709 2D-image
4-benzyl-3-(furan-2-yl)-5-[(4-methoxybenzyl)sulfanyl]-4H-1,2,4-triazoleHuman immunodeficiency virus 1--707709 2D-image
4-benzyl-3-[(4-chlorobenzyl)sulfanyl]-5-(furan-2-yl)-4H-1,2,4-triazoleHuman immunodeficiency virus 1--707709 2D-image
4-benzyl-3-[(4-chlorobenzyl)sulfanyl]-5-(thiophen-2-yl)-4H-1,2,4-triazoleHuman immunodeficiency virus 1-; inhibitor indentified by FRET-based high-throughput screening assay707709 2D-image
4-benzyl-3-[(4-chlorobenzyl)sulfanyl]-5-phenyl-4H-1,2,4-triazoleHuman immunodeficiency virus 1--707709 2D-image
4-benzyl-3-[(4-methoxybenzyl)sulfanyl]-5-(thiophen-2-yl)-4H-1,2,4-triazoleHuman immunodeficiency virus 1--707709 2D-image
4-benzyl-3-[(4-methoxybenzyl)sulfanyl]-5-phenyl-4H-1,2,4-triazoleHuman immunodeficiency virus 1-inhibitor indentified by FRET-based high-throughput screening assay707709-
4-heptyl-2-hydroxy-isoquinoline-1,3(2H,4H)-dioneHuman Immunodeficiency Virus-enol form714908-
4-hexyl-2-hydroxy-isoquinoline-1,3(2H,4H)-dioneHuman Immunodeficiency Virus-keto-form; mixture of th mixed ketoenol forms714908 2D-image
4-[[4-([4-[(E)-2-cyanovinyl]-2,6-dimethylphenyl]amino)pyrimidin-2-yl]amino]benzonitrileHuman immunodeficiency virus 1-i.e. TMC278 or rilpivirine, enzyme-bound structure, overview715864 2D-image
5,7-dihydroxy-2-(1-hydroxy-1-methyl-2-phenylaminoethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-oneHuman immunodeficiency virus 1--715864 2D-image
5,7-dihydroxy-2-(1-hydroxy-1-methyl-2-phenylsulfanylethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-oneHuman immunodeficiency virus 1--715864 2D-image
5,7-dihydroxy-2-(1-hydroxy-1-methyl-2-piperidin-1-ylethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-oneHuman immunodeficiency virus 1--715864 2D-image
5,7-dihydroxy-2-(1-hydroxy-2-imadazol-1-yl-1-methyl ethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-oneHuman immunodeficiency virus 1--715864 2D-image
5,7-dihydroxy-2-(1-hydroxy-ethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-oneHuman immunodeficiency virus 1--715864 2D-image
5,7-dihydroxy-2-isopropenyl-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-oneHuman immunodeficiency virus 1-i.e. manicol, the alpha-hydroxytroplone potently and specifically inhibits HIV RT ribonuclease H, enzyme-bound structure, overview715864 2D-image
5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl esterHuman immunodeficiency virus 1-inhibitor has little effect on bacterial RNase H activity in vitro693579 2D-image
5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl esterMoloney murine leukemia virus--693579 2D-image
5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl]-methyl esterHuman immunodeficiency virus 1-additionally inhibits HIV-1 replication effectively. Inhibitor has little effect on bacterial RNase H activity in vitro693579 2D-image
5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl]-methyl esterMoloney murine leukemia virus--693579 2D-image
6-[4-(diethylamino)phenoxy]-3-[ethoxy(hydroxy)methyl]-1,4-dihydroxy-1,8-naphthyridin-2(1H)-oneHuman immunodeficiency virus 1P0C6F2-716064 2D-image
9,10-dioxo-2-(2-oxo-2-phenylethoxy)-9,10-dihydroanthracen-1-yl acetateHuman immunodeficiency virus 1--714972 2D-image
9,10-dioxo-2-(2-oxopropoxy)-9,10-dihydroanthracen-1-yl acetateHuman immunodeficiency virus 1-10% inhibition714972 2D-image
9,10-dioxo-2-(prop-2-en-1-yloxy)-9,10-dihydroanthracen-1-yl acetateHuman immunodeficiency virus 1--714972 2D-image
9,10-dioxo-2-(prop-2-yn-1-yloxy)-9,10-dihydroanthracen-1-yl acetateHuman immunodeficiency virus 1--714972 2D-image
9,10-dioxo-2-[(2-oxopentan-3-yl)oxy]-9,10-dihydroanthracen-1-yl acetateHuman immunodeficiency virus 1-inhibits the RNase H function and is inactive on the DNA polymerase function714972 2D-image
9,10-dioxo-2-[(3-oxobutan-2-yl)oxy]-9,10-dihydroanthracen-1-yl acetateHuman immunodeficiency virus 1--714972 2D-image
9,10-dioxo-9,10-dihydroanthracene-1,2-diyl diacetateHuman immunodeficiency virus 1-12% inhibition714972 2D-image
9,10-dioxo-9,10-dihydroanthracene-1,2-diyl dibenzoateHuman immunodeficiency virus 1--714972 2D-image
AbacavirHuman immunodeficiency virus 1-a nucleoside reverse transcriptase inhibitor716993 2D-image
AbacavirHuman immunodeficiency virus 1--716994 2D-image
actinomycin DMoloney murine leukemia virus-limits the enzyme to the first strand synthesis643436 2D-image
ARK-2452Human immunodeficiency virus 1--713774-
beta-thujaplicinolHuman immunodeficiency virus 1-slow-binding RNase H inhibitor with noncompetitive kinetics that forms a tropylium ion that interacts favorably with reverse transcriptase and the RNA:DNA substrate710577 2D-image
beta-thujaplicinolHuman immunodeficiency virus 1--713774 2D-image
beta-thujaplicinolMoloney murine leukemia virus--715859 2D-image
bis[3-(phosphonatooxy)propyl] phosphateMoloney murine leukemia virus--714822 2D-image
DelavirdineHuman immunodeficiency virus 1--716994 2D-image
delaviridineHuman immunodeficiency virus 1-a nonnucleoside reverse transcriptase inhibitor716993-
Dextran sulfateHuman immunodeficiency virus 1-more potent inhibitor of RNase H than of reverse transcriptase. 50% infective dose corresponds to 0.1 nM699893-
didanosineHuman immunodeficiency virus 1-a nucleoside reverse transcriptase inhibitor716993 2D-image
didanosineHuman immunodeficiency virus 1--716994 2D-image
diketoacidMoloney murine leukemia virus--715859 2D-image
EfavirenzHuman immunodeficiency virus 1-second generation non-nucleoside reverse transcriptase inhibitor, shows the effect of simultaneously reorienting domain motions and obstructing the p66 thumb fluctuations701116 2D-image
EfavirenzHuman immunodeficiency virus 1--714972, 716994 2D-image
EfavirenzHuman immunodeficiency virus 1-stronger effect of mutation N348I on RNase H susceptibility to nevirapine as compared with efavirenz715532 2D-image
EfavirenzHuman immunodeficiency virus 1-a nonnucleoside reverse transcriptase inhibitor716993 2D-image
EmtricitabineHuman immunodeficiency virus 1-a nucleoside reverse transcriptase inhibitor716993 2D-image
EmtricitabineHuman immunodeficiency virus 1--716994 2D-image
ethyl (5E)-6-[1-(4-fluorobenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoateHuman immunodeficiency virus 1--716995 2D-image
ethyl 1,4-dihydroxy-2-oxo-1,2-dihydro-1,8-naphthyridine-3-carboxylateHuman immunodeficiency virus 1P0C6F2interactions between MK1 and two Mn2+ ions, which are coordinated by the RNase H active site residues D443, E478, D498, and D549, binding structure, overview. In addition, G444, S499, A538, H539, V552, and S553 contribute to the binding site716064 2D-image
EtravirineHuman immunodeficiency virus 1-a nonnucleoside reverse transcriptase inhibitor716993 2D-image
EtravirineHuman immunodeficiency virus 1--716994 2D-image
FoscarnetHuman immunodeficiency virus 1--716994 2D-image
guanylyl-(3'->5')-guanosineHuman immunodeficiency virus 1-89% inhibition of RNase H at 0.05 microM695645 2D-image
heparinHuman immunodeficiency virus 1-more potent inhibitor of RNase H than of reverse transcriptase. 50% infective dose corresponds to 0.5-1.5 nM699893 2D-image
L-708,906Moloney murine leukemia virus--715859 2D-image
L-870,810Moloney murine leukemia virus--715859 2D-image
lamivudineHuman immunodeficiency virus 1-a nucleoside reverse transcriptase inhibitor716993 2D-image
lamivudineHuman immunodeficiency virus 1--716994 2D-image
lovirideHuman immunodeficiency virus 1--716994 2D-image
madurohydroxylactoneHuman immunodeficiency virus 1--715864-
nevirapineHuman immunodeficiency virus 1-non-nucleoside RT inhibitors such as nevirapine interfere directly with the global hinge-bending mechanism that controls the cooperative motions of the p66 fingers and thumb subdomains. The net effect of nevirapine binding is to change the direction of domain movements rather than suppress their mobilities701116 2D-image
nevirapineHuman immunodeficiency virus 1-a non-nucleoside RT inhibitor, NNRTI, stronger effect of mutation N348I on RNase H susceptibility to nevirapine as compared with efavirenz715532 2D-image
nevirapineHuman immunodeficiency virus 1P0C6F2a nonnucleoside reverse transcriptase inhibitor, NNRTI716064 2D-image
nevirapineHuman immunodeficiency virus 1-a nonnucleoside reverse transcriptase inhibitor716993 2D-image
nevirapineHuman immunodeficiency virus 1--716994 2D-image
NSC727447Human immunodeficiency virus 1-mutation T473C increases sensitivity of the enzyme for NSC727447 by 50fold716995-
P-thioguanylyl-(3'->5')-guanosineHuman immunodeficiency virus 1-50% inhibition of RNase H at 0.05 microM695645-
raltegravirMoloney murine leukemia virus--715859-
sodium 2'-deoxy-2'-fluoro-P-thioadenylyl-(3'->5')-N-naphthalen-1-ylguanosineHuman immunodeficiency virus 1-61% inhibition of RNase H at 0.05 microM695645-
sodium 2'-deoxy-2'-fluoro-P-thioadenylyl-(3'->5')-N-naphthalen-1-ylguanosineMoloney murine leukemia virus-11% inhibition of RNase H at 0.05 microM695645-
sodium 2'-deoxy-2'-fluoro-P-thioadenylyl-(3'->5')-N-[2-(4-nitrophenyl)ethyl]guanosineHuman immunodeficiency virus 1-69% inhibition of RNase H at 0.05 microM695645-
stavudineHuman immunodeficiency virus 1-a nucleoside reverse transcriptase inhibitor716993 2D-image
stavudineHuman immunodeficiency virus 1--716994 2D-image
tenofovir disoproxil fumarateHuman immunodeficiency virus 1-a nucleoside reverse transcriptase inhibitor716993-
tetrahydroimidazo[4,5,1-jkj][1,4]benzodiazepin-2(1H)-oneHuman immunodeficiency virus 1--716994-
xylan polysulfateHuman immunodeficiency virus 1-more potent inhibitor of RNase H than of reverse transcriptase. 50% infective dose corresponds to 8 nM699893-
zalcitabineHuman immunodeficiency virus 1-a nucleoside reverse transcriptase inhibitor716993-
zidovudineHuman immunodeficiency virus 1-a nucleoside reverse transcriptase inhibitor716993 2D-image
zidovurineHuman immunodeficiency virus 1--716994-
[2-(4-chlorophenyl)hydrazinylidene]propanedioic acidHuman immunodeficiency virus 1-additionally inhibits DNA strand transfer and DNA polymerase activity of the retroviral reverse transcriptase696192 2D-image
[2-(4-chlorophenyl)hydrazinylidene]propanedioic acidHuman immunodeficiency virus 1-inhibits RNase H activity, does not significantly affect DNA polymerase activity of reverse transcriptase. In the absence of DNA synthesis, [2-(4-chlorophenyl)hydrazinylidene]propanedioic acid interferes with the translocation, or repositioning, of the enzyme on the RNA-DNA template duplex. Inhibitor is highly specific for human immunodeficiency virus. The dicarboxylic acid moiety is essential for activity, and Mg2+ chelates directly with a Kd value of 2.4 mM696194 2D-image
Mn2+Moloney murine leukemia virus-activation at 0.01-1 mM, inhibitory above701049 2D-image
additional informationHuman immunodeficiency virus 1-identification and evaluation of thiocarbamate and triazole inhibitors targeting RNase H activity of HIV reverse transcriptase, overview707709-
additional informationHuman immunodeficiency virus 1-design, synthesis, and screening of derivatives of 5-nitro-furan-2-carboxylic acid as inhibitors of the RNAse H activity of HIV-1 reverse transcriptase, overview. Modulation of the 5-nitro-furan-2-carboxylic moiety results in a drastic decrease in inhibitory potency. Binding mode of active derivatives, in which three oxygen atoms aligned in a straight form at the nitro-furan moiety are coordinated to two divalent metal ions located at RNase H reaction site. The nitro-furan-carboxylic moiety is one of the critical scaffolds for RNase H inhibition. Cytotoxicity of the synthesized compounds, overview714475-
additional informationMoloney murine leukemia virus-inhibitory potency and binding of dumbbell oligonucleotides to MoMuL virus RNase H, overview. The best dumbbell oligonucleotide, inhibitor contained phosphorothioate residues in both the loops714822-
additional informationHuman Immunodeficiency Virus-synthesis of 2-hydroxyisoquinoline-1,3(2H,4H)-dione derivatives as inhibitors of the RNase H activity of the reverse transcriptase of HIV-1, docking, study, overview. No inhibition by keto-5i and 5l714908-
additional informationHuman immunodeficiency virus 1-non-nucleoside RT inhibitors, NNRTIs, bind to an allosteric site that is 10 A from the polymerase active site and 60 A from the RNase H active site715532-
additional informationMoloney murine leukemia virus-magnesium chelating 2-hydroxyisoquinoline-1,3(2H,4H)-diones, as inhibitors of HIV-1 integrase and/or the HIV-1 reverse transcriptase ribonuclease H domain, overview. 2-Hydroxyisoquinoline-1,3(2H,4H)-dione forms a 1:1 complex with Mg2+, but a 1:2 complex with Mn2+,715859-
additional informationHuman immunodeficiency virus 1-no inhibition by 5,7-dihydroxy-2-(1-hydroxy-1-methyl-2-piperidin-1-ylethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one, 5,7-dihydroxy-2-(1-hydroxy-2-imadazol-1-yl-1-methyl ethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one, 2-(2-diethylamino-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one, and 2-(1-benzylamino-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one715864-
additional informationHuman immunodeficiency virus 1P0C6F2structures of naphthyridinone-containing inhibitors bound to the RNase H active site, overview. This class of compounds binds to the active site via two metal ions that are coordinated by catalytic site residues, D443, E478, D498, and D549. The directionality of the naphthyridinone pharmacophore is restricted by the ordering of D549 and H539 in the RNase H domain716064-
additional informationHuman immunodeficiency virus 1-C-terminal domain mutations reduce RNase H activity either directly by affecting the RNase H cleavage activity of the enzyme, or indirectly by affecting the overall positioning of the template/primer strand, which in turn affects RNase H activity, template switching, polymerization and/or nucleotide excision. Effects of enzyme mutations on treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors, detailed overview. Nucleoside reverse transcriptase inhibitors are nucleoside analogues that lack the 3' OH on the sugar ring and competitively block reverse transcription by causing chain termination during DNA polymerization. Nucleoside reverse transcriptase inhibitors are prodrugs that require intracellular phosphorylation to the 5'-triphosphate formed by host cell kinases in order to become active. Nonnucleoside reverse transcriptase inhibitors in general are non-competitive inhibitors of RT that bind to a hydrophobic pocket near the polymerase active site, inducing conformational changes that inhibit RT enzymatic activity. Inhibition mechanisms of the two inhibitor classes, overview716993-
additional informationHuman immunodeficiency virus 1-mechanisms of catalysis and drug inhibition of polymerase and RNase H functions of RT by nucleos(t)ide reverse transcriptase inhibitor and non-nucleoside reverse transcriptase inhibitor drugs, and molecular mechanisms of drug resistance, detailed overview716994-
additional informationHuman immunodeficiency virus 1-discovery and development of bona fide RNase H inhibitors, overview716995-

ACTIVATING COMPOUNDORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
ATPHuman immunodeficiency virus 1-activates, effect on kinetics, overview690924 2D-image
nucleocapsid protein NCp7Human immunodeficiency virus 1-enhances ribonuclease H activity and changes the specificity of hydrolysis. As a model, the NCp7 binds to the DNA strand and through interaction with HIV-1 RT facilitates the delivery of the DNA-RNA duplex into the RNase H site for cleavage, thereby altering the rate and location of RNase H cleavage696183-

KM VALUE [mM]KM VALUE [mM] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.003-poly(rA)n-poly(dT)nHuman immunodeficiency virus 1-37°C, wild-type p66/p51652907-
0.0177-poly(rA)n-poly(dT)nHuman immunodeficiency virus 1-37°C, mutant p66C280P/p51652907-
0.0257-poly(rA)n-poly(dT)nHuman immunodeficiency virus 1-37°C, mutant p66/p51C280P652907-
0.0318-poly(rA)n-poly(dT)nHuman immunodeficiency virus 1-37°C, mutant p66C280W/p51652907-
0.0383-poly(rA)n-poly(dT)nHuman immunodeficiency virus 1-37°C, mutant p66/p51C280W652907-
0.0553-poly(rA)n-poly(dT)nHuman immunodeficiency virus 1-37°C, mutant p66C280P/p51C280P652907-
0.0663-poly(rA)n-poly(dT)nHuman immunodeficiency virus 1-37°C, mutant p66C280W/p51C280W652907-
additional information-additional informationHuman immunodeficiency virus 1-presteady-state kinetic analyses, overview690924-
additional information-additional informationHuman immunodeficiency virus 1-pre-steady-state kinetics, overview716067-
additional information-poly(rA)/oligo(dT)Human immunodeficiency virus 1-apparent binding constant 3500 per mM698692-

TURNOVER NUMBER [1/s] TURNOVER NUMBER MAXIMUM[1/s] SUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.024-poly(rA)n-poly(dT)nHuman immunodeficiency virus 1-37°C, mutant p66/p51C280P; 37°C, mutant p66/p51C280W652907-
0.025-poly(rA)n-poly(dT)nHuman immunodeficiency virus 1-37°C, mutant p66C280P/p51652907-
0.029-poly(rA)n-poly(dT)nHuman immunodeficiency virus 1-37°C, mutant p66C280P/p51C280P; 37°C, mutant p66C280W/p51652907-
0.031-poly(rA)n-poly(dT)nHuman immunodeficiency virus 1-37°C, wild-type p66/p51652907-
0.034-poly(rA)n-poly(dT)nHuman immunodeficiency virus 1-37°C, mutant p66C280W/p51C280W652907-

kcat/KM VALUE [1/mMs-1]kcat/KM VALUE [1/mMs-1] MaximumSUBSTRATEORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
510-poly(rA)n-poly(dT)nHuman immunodeficiency virus 1-37°C, mutant p66C280W/p51C280W6529070
520-poly(rA)n-poly(dT)nHuman immunodeficiency virus 1-37°C, mutant p66C280P/p51C280P6529070
620-poly(rA)n-poly(dT)nHuman immunodeficiency virus 1-37°C, mutant p66/p51C280W6529070
910-poly(rA)n-poly(dT)nHuman immunodeficiency virus 1-37°C, mutant p66C280W/p516529070
930-poly(rA)n-poly(dT)nHuman immunodeficiency virus 1-37°C, mutant p66/p51C280P6529070
1460-poly(rA)n-poly(dT)nHuman immunodeficiency virus 1-37°C, mutant p66C280P/p516529070
10300-poly(rA)n-poly(dT)nHuman immunodeficiency virus 1-37°C, wild-type p66/p516529070

Ki VALUE [mM]Ki VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.0115-sodium 2'-deoxy-2'-fluoro-P-thioadenylyl-(3'->5')-N-[2-(4-nitrophenyl)ethyl]guanosineHuman immunodeficiency virus 1--695645-
0.00014-beta-thujaplicinolHuman immunodeficiency virus 1-presence of Mg2+ and DNA:RNA hybrid, pH 8.0710577 2D-image
additional information-additional informationHuman immunodeficiency virus 1-non competitive inhibition kinetics of alizarine derivatives, overview714972-

IC50 VALUE [mM]IC50 VALUE [mM] MaximumINHIBITORORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE IMAGE
0.00051-(2S)-5,7-dihydroxy-2-(2-hydroxy-1-(phenylsulfonyl)propan-2-yl)-9-methyl-3,4-dihydro-1H-benzo[7]annulen-6(2H)-oneHuman immunodeficiency virus 1-pH 8.0, 37°C715864 2D-image
0.075-1,6,8-trihydroxy-3-methylanthraquinoneHuman immunodeficiency virus 1--708108-
0.0006-2,7-dihydroxy-4-(propan-2-yl)cyclohepta-2,4,6-trien-1-oneHuman immunodeficiency virus 1--709451 2D-image
0.0019-2-(1,2-dihydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-oneHuman immunodeficiency virus 1-pH 8.0, 37°C715864 2D-image
0.00096-2-(1-benzylamino-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-oneHuman immunodeficiency virus 1-pH 8.0, 37°C715864 2D-image
0.0061-2-(2,3-dihydro-1H-inden-1-ylamino)-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.0055-2-(2,3-dihydro-1H-inden-2-ylamino)-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.0013-2-(2-benzylsulfanyl-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-oneHuman immunodeficiency virus 1-pH 8.0, 37°C715864 2D-image
0.0005-2-(2-diethylamino-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-oneHuman immunodeficiency virus 1-pH 8.0, 37°C715864 2D-image
0.00024-2-(2-ethanesulfonyl-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-oneHuman immunodeficiency virus 1-pH 8.0, 37°C715864 2D-image
0.00038-2-(2-ethylsulfanyl-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-oneHuman immunodeficiency virus 1-pH 8.0, 37°C715864 2D-image
0.0012-2-(3,4-dichlorobenzyl)-5,6-dihydroxypyrimidine-4-carboxylic acidHuman immunodeficiency virus 1--709451 2D-image
0.0009-2-(3-bromo-4-methoxybenzyl)-5,6-dihydroxypyrimidine-4-carboxylic acidHuman immunodeficiency virus 1--709451-
0.018-2-(tert-butylamino)-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.0071-2-amino-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.0668-2-hydroxy-4-(3-phenyl)propylisoquinoline-1,3(2H,4H)-dioneHuman Immunodeficiency Virus-pH 8.0, 37°C714908-
0.08-2-hydroxy-4-(4-methylbenzyl)isoquinoline-1,3(2H,4H)-dioneHuman Immunodeficiency Virus-pH 8.0, 37°C714908-
0.0427-2-hydroxy-4-(4-trifluoromethylbenzyl)isoquinoline-1,3(2H-4H)-dioneHuman Immunodeficiency Virus-pH 8.0, 37°C714908 2D-image
0.0132-2-hydroxy-4-butylisoquinoline-1,3(2H,4H)-dioneHuman Immunodeficiency Virus-pH 8.0, 37°C714908-
0.0388-2-hydroxy-4-ethylisoquinoline-1,3(2H,4H)-dioneHuman Immunodeficiency Virus-pH 8.0, 37°C714908 2D-image
0.0185-2-hydroxy-4-isopropylisoquinoline-1,3(2H,4H)-dioneHuman Immunodeficiency Virus-pH 8.0, 37°C714908 2D-image
6.1e-05-2-hydroxy-4-methoxycarbonylisoquinoline-1,3(2H,4H)-dioneMoloney murine leukemia virus-pH 8.0, 37°C715859-
0.0388-2-hydroxy-4-methylisoquinoline-1,3(2H,4H)-dioneMoloney murine leukemia virus-pH 8.0, 37°C715859 2D-image
0.07-2-hydroxy-4-methylisoquinoline-1,3(2H,4H)-dioneHuman Immunodeficiency Virus-pH 8.0, 37°C714908 2D-image
0.0336-2-hydroxy-4-pentylisoquinoline-1,3(2H,4H)-dioneHuman Immunodeficiency Virus-pH 8.0, 37°C714908 2D-image
0.0468-2-hydroxy-4-propylisoquinoline-1,3(2H,4H)-dioneHuman Immunodeficiency Virus-pH 8.0, 37°C714908 2D-image
0.00012-2-hydroxyisoquinoline-1,3(2H,4H)-dioneHuman immunodeficiency virus 1--709451 2D-image
0.0059-2-hydroxyisoquinoline-1,3(2H,4H)-dioneHuman Immunodeficiency Virus-pH 8.0, 37°C714908 2D-image
0.0591-2-hydroxyisoquinoline-1,3(2H,4H)-dioneMoloney murine leukemia virus-pH 8.0, 37°C715859 2D-image
0.0301-2-hydroxyisoquinoline-1,3(2H,4H)-dione magnesium complexMoloney murine leukemia virus-pH 8.0, 37°C715859-
0.0043-2-oxo-2-(1,2,3,4-tetrahydronaphthalen-1-ylamino)ethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.0132-2-oxo-2-(propan-2-yloxy)ethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.0042-2-oxo-2-(tetrahydrofuran-2-ylamino)ethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.0266-2-oxo-2-[(2,3,4-trichlorophenyl)amino]ethyl benzyl(phenyl)carbamodithioateHuman immunodeficiency virus 1-pH not specified in the publication, temperature not specified in the publication707709 2D-image
0.0033-2-oxo-2-[(2,3,4-trichlorophenyl)amino]ethyl dibenzylcarbamodithioateHuman immunodeficiency virus 1-pH not specified in the publication, temperature not specified in the publication707709 2D-image
0.0082-2-oxo-2-[(2-phenylpropan-2-yl)amino]ethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.0033-2-[(2,3,4-trichlorophenyl)amino]-2-oxoethyl dibenzylcarbamodithioateHuman immunodeficiency virus 1-pH 8.0, 25°C707709-
0.0058-2-[(2,4-dichlorophenyl)amino]-2-oxoethyl dibenzylcarbamodithioateHuman immunodeficiency virus 1-pH not specified in the publication, temperature not specified in the publication707709 2D-image
0.0019-2-[(2,4-dimethylphenyl)amino]-2-oxoethyl dibenzylcarbamodithioateHuman immunodeficiency virus 1-pH 8.0, 25°C; pH not specified in the publication, temperature not specified in the publication707709 2D-image
0.0083-2-[(2-methoxy-5-methylphenyl)amino]-2-oxoethyl benzyl(phenyl)carbamodithioateHuman immunodeficiency virus 1-pH not specified in the publication, temperature not specified in the publication707709 2D-image
0.0043-2-[(2-methyl-1-phenylpropan-2-yl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.0058-2-[(2-methylbutan-2-yl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.0114-2-[(3-cyanophenyl)amino]-2-oxoethyl benzyl(phenyl)carbamodithioateHuman immunodeficiency virus 1-pH not specified in the publication, temperature not specified in the publication707709 2D-image
0.0047-2-[(3-cyanophenyl)amino]-2-oxoethyl dibenzylcarbamodithioateHuman immunodeficiency virus 1-pH not specified in the publication, temperature not specified in the publication707709 2D-image
0.005-2-[(4-hydroxybenzyl)(tetrahydrofuran-2-ylmethyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.0012-2-[2-(2-fluoro-benzylamino)-1-hydroxy-1-methyl-ethyl]-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-oneHuman immunodeficiency virus 1-pH 8.0, 37°C715864 2D-image
0.021-2-[2-(4-bromophenyl)-2-oxoethoxy]-9,10-dioxo-9,10-dihydroanthracen-1-yl acetateHuman immunodeficiency virus 1-pH not specified in the publication, temperature not specified in the publication714972 2D-image
0.1-2-[2-(biphenyl-4-yl)-2-oxoethoxy]-9,10-dioxo-9,10-dihydroanthracen-1-yl acetateHuman immunodeficiency virus 1-pH not specified in the publication, temperature not specified in the publication714972 2D-image
0.0017-2-[4-benzyl-5-(benzylsulfanyl)-4H-1,2,4-triazol-3-yl]pyridineHuman immunodeficiency virus 1-pH 8.0, 25°C; pH not specified in the publication, temperature not specified in the publication707709 2D-image
0.0026-2-[4-benzyl-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]pyridineHuman immunodeficiency virus 1-pH not specified in the publication, temperature not specified in the publication707709 2D-image
0.0077-2-[benzyl(tetrahydrofuran-2-ylmethyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.0142-2-[tert-butyl(2-phenylethyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.0098-2-[tert-butyl(3-nitrobenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.05-2-[tert-butyl(3-oxo-3-phenylpropyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.05-2-[tert-butyl(3-phenylpropyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.0085-2-[tert-butyl(4-fluorobenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.0075-2-[tert-butyl(4-methoxybenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.0069-2-[tert-butyl(4-nitrobenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.0068-2-[tert-butyl(pentafluorobenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.0009-2-[tert-butyl(phenyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.009-2-[tert-butyl[2-(trifluoromethyl)benzyl]amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.0085-2-[tert-butyl[3-(trifluoromethyl)benzyl]amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.008-2-[tert-butyl[4-(trifluoromethyl)benzyl]amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.0128-2-[[2-(acetyloxy)benzyl](tert-butyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.0087-2-[[4-(acetyloxy)benzyl](tert-butyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.05-2-[[4-(benzyloxy)benzyl](tert-butyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.0219-3,3-dimethyl-2-oxobutyl 5-nitrofuran-2-carboxylateHuman immunodeficiency virus 1-pH 7.5, 37°C714475 2D-image
0.0065-3-(furan-2-yl)-4-(4-methoxybenzyl)-5-[[4-(trifluoromethyl)benzyl]sulfanyl]-4H-1,2,4-triazoleHuman immunodeficiency virus 1-pH not specified in the publication, temperature not specified in the publication707709 2D-image
0.0047-3-(furan-2-yl)-4-phenyl-5-[[4-(trifluoromethyl)benzyl]sulfanyl]-4H-1,2,4-triazoleHuman immunodeficiency virus 1-pH not specified in the publication, temperature not specified in the publication707709 2D-image
0.029-3-[2-(4-bromophenyl)-2-oxoethoxy]-1,8-dihydroxy-6-methylanthracene-9,10-dioneHuman immunodeficiency virus 1--708108-
0.004-4-([[4-benzyl-5-(furan-2-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]methyl)pyridineHuman immunodeficiency virus 1-pH not specified in the publication, temperature not specified in the publication707709 2D-image
0.0002-4-([[4-benzyl-5-(thiophen-2-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]methyl)pyridineHuman immunodeficiency virus 1-pH 8.0, 25°C707709 2D-image
0.2-4-([[4-benzyl-5-(thiophen-2-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]methyl)pyridineHuman immunodeficiency virus 1-pH not specified in the publication, temperature not specified in the publication707709 2D-image
0.0149-4-benzyl-2-hydroxy-isoquinoline-1,3(2H,4H)-dioneHuman Immunodeficiency Virus-pH 8.0, 37°C714908 2D-image
0.0012-4-benzyl-3-(benzylsulfanyl)-5-(furan-2-yl)-4H-1,2,4-triazoleHuman immunodeficiency virus 1-pH 8.0, 25°C; pH not specified in the publication, temperature not specified in the publication707709 2D-image
0.00021-4-benzyl-3-(benzylsulfanyl)-5-(thiophen-2-yl)-4H-1,2,4-triazoleHuman immunodeficiency virus 1-pH 8.0, 25°C; pH not specified in the publication, temperature not specified in the publication707709 2D-image
0.001-4-benzyl-3-(benzylsulfanyl)-5-phenyl-4H-1,2,4-triazoleHuman immunodeficiency virus 1-pH 8.0, 25°C; pH not specified in the publication, temperature not specified in the publication707709 2D-image
0.0038-4-benzyl-3-(furan-2-yl)-5-[(4-methoxybenzyl)sulfanyl]-4H-1,2,4-triazoleHuman immunodeficiency virus 1-pH not specified in the publication, temperature not specified in the publication707709 2D-image
0.0028-4-benzyl-3-[(4-chlorobenzyl)sulfanyl]-5-(furan-2-yl)-4H-1,2,4-triazoleHuman immunodeficiency virus 1-pH not specified in the publication, temperature not specified in the publication707709 2D-image
0.001-4-benzyl-3-[(4-chlorobenzyl)sulfanyl]-5-(thiophen-2-yl)-4H-1,2,4-triazoleHuman immunodeficiency virus 1-pH 8.0, 25°C; pH not specified in the publication, temperature not specified in the publication707709 2D-image
0.006-4-benzyl-3-[(4-chlorobenzyl)sulfanyl]-5-phenyl-4H-1,2,4-triazoleHuman immunodeficiency virus 1-pH not specified in the publication, temperature not specified in the publication707709 2D-image
0.001-4-benzyl-3-[(4-methoxybenzyl)sulfanyl]-5-(thiophen-2-yl)-4H-1,2,4-triazoleHuman immunodeficiency virus 1-pH not specified in the publication, temperature not specified in the publication707709 2D-image
0.0059-4-benzyl-3-[(4-methoxybenzyl)sulfanyl]-5-(thiophen-2-yl)-4H-1,2,4-triazoleHuman immunodeficiency virus 1-pH not specified in the publication, temperature not specified in the publication707709 2D-image
0.001-4-benzyl-3-[(4-methoxybenzyl)sulfanyl]-5-phenyl-4H-1,2,4-triazoleHuman immunodeficiency virus 1-pH 8.0, 25°C707709-
0.045-4-heptyl-2-hydroxy-isoquinoline-1,3(2H,4H)-dioneHuman Immunodeficiency Virus-pH 8.0, 37°C714908-
0.0078-4-hexyl-2-hydroxy-isoquinoline-1,3(2H,4H)-dioneHuman Immunodeficiency Virus-pH 8.0, 37°C714908 2D-image
0.038-4-hexyl-2-hydroxy-isoquinoline-1,3(2H,4H)-dioneHuman Immunodeficiency Virus-pH 8.0, 37°C714908 2D-image
0.0012-5,7-dihydroxy-2-(1-hydroxy-1-methyl-2-phenylaminoethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-oneHuman immunodeficiency virus 1-pH 8.0, 37°C715864 2D-image
0.00093-5,7-dihydroxy-2-(1-hydroxy-1-methyl-2-phenylsulfanylethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-oneHuman immunodeficiency virus 1-pH 8.0, 37°C715864 2D-image
0.00082-5,7-dihydroxy-2-(1-hydroxy-1-methyl-2-piperidin-1-ylethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-oneHuman immunodeficiency virus 1-pH 8.0, 37°C715864 2D-image
0.00911-5,7-dihydroxy-2-(1-hydroxy-2-imadazol-1-yl-1-methyl ethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-oneHuman immunodeficiency virus 1-pH 8.0, 37°C715864 2D-image
0.00068-5,7-dihydroxy-2-(1-hydroxy-ethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-oneHuman immunodeficiency virus 1-pH 8.0, 37°C715864 2D-image
0.0038-5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl esterHuman immunodeficiency virus 1--693579 2D-image
0.0084-5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl esterMoloney murine leukemia virus--693579 2D-image
0.0265-5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl esterHuman immunodeficiency virus 1--693579 2D-image
0.0296-5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl esterHuman immunodeficiency virus 1--693579 2D-image
0.0026-5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl]-methyl esterHuman immunodeficiency virus 1--693579 2D-image
0.0086-5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl]-methyl esterMoloney murine leukemia virus--693579 2D-image
0.0267-5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl]-methyl esterHuman immunodeficiency virus 1--693579 2D-image
0.0322-5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl]-methyl esterHuman immunodeficiency virus 1--693579 2D-image
0.039-9,10-dioxo-2-(2-oxo-2-phenylethoxy)-9,10-dihydroanthracen-1-yl acetateHuman immunodeficiency virus 1-pH not specified in the publication, temperature not specified in the publication714972 2D-image
0.013-9,10-dioxo-9,10-dihydroanthracene-1,2-diyl dibenzoateHuman immunodeficiency virus 1-pH not specified in the publication, temperature not specified in the publication714972 2D-image
0.000186-ARK-2452Human immunodeficiency virus 1-pH 8.0, 37°C, purified recombinant mutant p51-G-TCR construct713774-
0.00047-ARK-2452Human immunodeficiency virus 1-pH 8.0, 37°C, purified recombinant wild-type HIV-1 reverse transcriptase RNase H713774-
0.000176-beta-thujaplicinolHuman immunodeficiency virus 1-pH 8.0, 37°C, purified recombinant mutant p51-G-TCR construct713774 2D-image
0.000257-beta-thujaplicinolHuman immunodeficiency virus 1-pH 8.0, 37°C, purified recombinant wild-type HIV-1 reverse transcriptase RNase H713774 2D-image
0.04-sodium 2'-deoxy-2'-fluoro-P-thioadenylyl-(3'->5')-N-naphthalen-1-ylguanosine, sodium 2'-deoxy-2'-fluoro-P-thioadenylyl-(3'->5')-N-[2-(4-nitrophenyl)ethyl]guanosineHuman immunodeficiency virus 1--695645-
0.0022-[2-(4-chlorophenyl)hydrazinylidene]propanedioic acidHuman immunodeficiency virus 1-pH 7.6, 37°C696194 2D-image
0.003-[2-(4-chlorophenyl)hydrazinylidene]propanedioic acidHuman immunodeficiency virus 1-pH 7.6, 37°C696192 2D-image

SPECIFIC ACTIVITY [µmol/min/mg] SPECIFIC ACTIVITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
7.6-Moloney murine leukemia virus-commercial preparation, pH 7.8, 37°C714822
166-Moloney murine leukemia virus-37°C643436
additional information-Human immunodeficiency virus 2-level of RNase H activity is low in HIV-2 isolates652865

pH OPTIMUMpH MAXIMUMORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
7.5-Human immunodeficiency virus 1-assay at690924, 714475
7.6-Moloney murine leukemia virus-assay at707794
7.8-Human immunodeficiency virus 1-assay at713770
7.8-Moloney murine leukemia virus-assay at714822
7.8-Human immunodeficiency virus 1P0C6F2assay at716064
7.8-Human immunodeficiency virus 1-assay at716827
88.5Human Immunodeficiency Virus--698685
88.5Moloney murine leukemia virus-assay at716354
8-Human immunodeficiency virus 1-assay at650155, 713774, 715532
8-Moloney murine leukemia virus-assay at715859
8-Human immunodeficiency virus 1-assay at715864

pH RANGEpH RANGE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

TEMPERATURE OPTIMUMTEMPERATURE OPTIMUM MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
22-Human immunodeficiency virus 1-assay at room temperature716827
25-Moloney murine leukemia virus-assay at716354
37-Human immunodeficiency virus 1-assay at650155, 690924
37-Moloney murine leukemia virus-assay at707794
37-Human immunodeficiency virus 1-assay at713770, 713774, 714475
37-Moloney murine leukemia virus-assay at714822
37-Human immunodeficiency virus 1-assay at715532
37-Moloney murine leukemia virus-assay at715859
37-Human immunodeficiency virus 1-assay at715864
37-Human immunodeficiency virus 1P0C6F2assay at716064

TEMPERATURE RANGE TEMPERATURE MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

pI VALUEpI VALUE MAXIMUMORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
No entries in this field

SOURCE TISSUE ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE SOURCE
commercial preparationMoloney murine leukemia virus--714822Manually annotated by BRENDA team
commercial preparationMoloney murine leukemia virus-recombinant enzyme715859Manually annotated by BRENDA team
additional informationHuman immunodeficiency virus 1-virus passage in human 293 cells716067Manually annotated by BRENDA team

LOCALIZATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY GeneOntology No. LITERATURE SOURCE
No entries in this field

PDBSCOPCATHORGANISM
3qin, downloadSCOP (3qin)CATH (3qin)Escherichia coli (strain K12)
3qio, downloadSCOP (3qio)CATH (3qio)Escherichia coli (strain K12)
2ykm, downloadSCOP (2ykm)CATH (2ykm)Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
2ykn, downloadSCOP (2ykn)CATH (2ykn)Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
3qlh, downloadSCOP (3qlh)CATH (3qlh)Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
3qo9, downloadSCOP (3qo9)CATH (3qo9)Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
4h4m, downloadSCOP (4h4m)CATH (4h4m)Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
4h4o, downloadSCOP (4h4o)CATH (4h4o)Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
3nbp, downloadSCOP (3nbp)CATH (3nbp)Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
3qip, downloadSCOP (3qip)CATH (3qip)Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
3t19, downloadSCOP (3t19)CATH (3t19)Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
3t1a, downloadSCOP (3t1a)CATH (3t1a)Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
3tam, downloadSCOP (3tam)CATH (3tam)Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
4bac, downloadSCOP (4bac)CATH (4bac)Human spumaretrovirus

MOLECULAR WEIGHT MOLECULAR WEIGHT MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
71000-Moloney murine leukemia virus-glycerol gradient centrifugation643436
110000-Human Immunodeficiency Virus-glycerol gradient centrifugation698685

SUBUNITS ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
dimerHuman immunodeficiency virus 1-HIV-1 RT650155
dimerHuman immunodeficiency virus 1--715864
dimerHuman immunodeficiency virus 1-1 * 51000, p51 subunit, + 1 * 66000, p66 subunit, of HIV reverse transcriptase, SDS-PAGE716994
monomerMoloney murine leukemia virus-1 * 71000, SDS-PAGE of recombinant enzyme with deletion of 204 nucleotides at the 3'-terminus643436
additional informationHuman Immunodeficiency Virus-RNase H activity is associated with the p66 component of reverse transcriptase698685
additional informationHuman immunodeficiency virus 1-the folded structure of the HIV-1 RNase H domain takes the form of a 5-stranded mixed beta-sheet flanked by four alpha helices in an asymmetric distribution, structure comparisons, overview. The p66 subunit is subdivided into three domains: the N-terminal polymerase domain, the C-terminal ribonuclease RNase H domain, and connection domain that links the two functional regions716995

POSTTRANSLATIONAL MODIFICATION ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

Crystallization/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
2.80 A and 2.04 A resolution crystal structures of inhibitor, beta-thujaplicinol, bound at the RNase H active site of both HIV-1 RT and an isolated RNase H domain. beta-Thujaplicinol chelates two divalent metal ions at the RNase H active siteHuman immunodeficiency virus 1-710577
crystal structure analysis, overview. The pyrimidinol carboxylic acids is successful crystallized with Mn2+ and the isolated HIV RNase H domainHuman immunodeficiency virus 1-716995
docking simulation studies. Residue His 539 and two metal ions in the RNase H catalytic center are involved in inhibition by compounds 5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester and 5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl]-methyl esterHuman immunodeficiency virus 1-693579
isolated recombinant RNase H domain, to 2.4 A resolution. The protein folds into a five-stranded mixed beta sheet flanked by an asymmetric distribution of four alpha helices. Two divalent metal cations bind in the active site surrounded by a cluster of four conserved acidic amino acid residues. The peptide bond cleaved by HIV-1 protease near the polymerase-RNase H junction of polypeptide p66 is completely inaccessible to solvent in the structure reported here, suggesting that the homodimeric p66-p66 precursor of mature RT is asymmetric with one of the two RNase H domains at least partially unfoldedHuman immunodeficiency virus 1-701216
modeling of the kinetic refolding intermediate using a C-terminal deletion fragment lacking helix E. Like the kinetic intermediate, this variant folds rapidly and shows a decrease in stabilityHuman immunodeficiency virus 1-701113
purified p66/p51 HIV-1 reverse transcriptase 52A variant in complex with inhibitors manicol and TMC278, 0.0012 ml of 20 mg/mL protein in 9.2 mM Tris, pH 8.0, 68.7 mM NaCl, 3.6 mM manganese sulfate, 0.7 mM tris(2-carboxyethyl) phosphine, 0.27% w/v, beta-ocytl glucopyranoside, 7% v/v DMSO, 0.9 mM manicol, and 0.7 mM TMC278, mixed with 0.0012 ml of reservoir solution containing 50 mM HEPES pH 7.5, 100 mM ammonium sulfate, 15 mM manganese sulfate, 10 mM spermine, 5 mM TCEP, and 11% w/w PEG 8000, X-ray diffraction structure determination and analysis at 2.7 A resolution, modelingHuman immunodeficiency virus 1-715864
purified recombinant detagged enzyme, mixing of 8-10 mg/ml protein in 20 mM potassium phosphate, pH 7.0, and 1 mM inhibitor nevirapine, with reservoir buffer containing 100 mM sodium cacodylate, pH 6.8, and 800 mM sodium citrate, in a 1:1 ratio, X-ray diffraction structure determination and analysis. Isolated RNase H domain is crystallized in a buffer containing 100 mM sodium citrate, pH 5.0, and 15 to 20% PEG-8000. Crystals are harvested for inhibitor soaking in the reservoir solution with the addition of 50 mM MnCl2, and 1 mM inhibitor nevirapine, at 4°C. Mn2+ is used as a surrogate for Mg2+ since soaking experiments with Mg2+ cannot reproducibly yield structures with inhibitor boundHuman immunodeficiency virus 1P0C6F2716064
purified wild-type enzyme in complex with polypurine tract RNA:DNA oligonucleotide, hanging drop vapour diffusion method, mixing of equal volumes of protein and precipitant solution, the latter contains 100 mM cacodylate, pH 5.6, 29-31% saturated ammonium sulfate, 4°C, X-ray diffraction structure determination and analysis at 3.0 A resolution, molecular replacementHuman immunodeficiency virus 1P03366717535
solution structural dynamics. Enzyme is an asymmetric heterodimer of two subunits, p66 and p51. The two subunits have the same N-terminal sequence, with the p51 subunit lacking the C-terminal RNase H domain. The p66 subunit contains the polymerase and RNase H catalytic sites. H/D exchange indicates that the RNase H domain of p66 is very flexibleHuman immunodeficiency virus 1-707509
study on dynamics of RT in unliganded and inhibitor-bound forms by structure-based approach. Non-nucleoside RT inhibitors such as nevirapine interfere directly with the global hinge-bending mechanism that controls the cooperative motions of the p66 fingers and thumb subdomains. The net effect of nevirapine binding is to change the direction of domain movements rather than suppress their mobilities. The second generation non-nucleoside reverse transcriptase inhibitor, efavirenz, on the other hand, shows the stronger effect of simultaneously reorienting domain motions and obstructing the p66 thumb fluctuations. A second hinge site controlling the global rotational reorientations of the RNase H domain is identifiedHuman immunodeficiency virus 1-701116

pH STABILITYpH STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

TEMPERATURE STABILITYTEMPERATURE STABILITY MAXIMUM ORGANISM UNIPROT ACCESSION NO. COMMENTARYLITERATURE
29.7-Moloney murine leukemia virus-melting temperature, mutant H638G; melting temperature, wild-type701049
29.9-Moloney murine leukemia virus-melting temperature, wild-type, presence of 25 mM NaCl701049
34.1-Moloney murine leukemia virus-melting temperature, wild-type, presence of 1 mM Mg2+701049
35.8-Moloney murine leukemia virus-melting temperature, mutant E562Q701049
39.2-Moloney murine leukemia virus-melting temperature, mutant D653N701049
42-Moloney murine leukemia virus-melting temperature, wild-type, presence of 1 mM Mn2+701049
43.5-Moloney murine leukemia virus-melting temperature, mutant H638G, presence of 1 mM Mn2+701049
43.6-Moloney murine leukemia virus-wild-type, 50% residual activity after a 10 min incubation707794
45.8-Moloney murine leukemia virus-melting temperature, mutant D524N701049
46.2-Moloney murine leukemia virus-wild-type, 50% residual activity after a 10 min incubation, presence of primer-template707794
46.3-Moloney murine leukemia virus-melting temperature, mutant D524N, presence of 1 mM Mn2+701049
46.9-Moloney murine leukemia virus-melting temperature, mutant D653N, presence of 1 mM Mn2+701049
47.3-Moloney murine leukemia virus-mutant D524A, 50% residual activity after a 10 min incubation707794
48.4-Moloney murine leukemia virus-melting temperature, mutant D583N, presence of 1 mM Mn2+701049
48.8-Moloney murine leukemia virus-melting temperature, mutant E562Q, presence of 1 mM Mn2+701049
48.9-Moloney murine leukemia virus-melting temperature, mutant D583N701049
49.7-Moloney murine leukemia virus-mutant D524A, 50% residual activity after a 10 min incubation, presence of primer-template707794

GENERAL STABILITYORGANISM UNIPROT ACCESSION NO.LITERATURE
No entries in this field

ORGANIC SOLVENT ORGANISM UNIPROT ACCESSION NO. COMMENTARY LITERATURE
No entries in this field

OXIDATION STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

STORAGE STABILITY ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

Purification/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
a HIV-1 RNase H specific inhibitor from the hydroxyimide class, that contains a primary amine with a long nonfunctional linker, is conjugated to NHS-activated HiTrap HP resins for use in affinity chromatographic HIV reverse transcriptase purifcation. Purification of untagged HIV-1 RT using an avidin affinity column in presence of Mg2+, method evaluations, overviewHuman immunodeficiency virus 1-716827
recombinant His-tagged enzyme by nickel affinity chromatography, the His6 tag is removed by proteolysis with thrombin, followed by gel filtrationHuman immunodeficiency virus 1P0C6F2716064
recombinant His-tagged p66 or p51 HIV-1 RT DNA fragment from Escherichia coli strain BL21(DE3)pLys by nickel affinity chromatography, expression of a heterodimer of wild-type or F160S and C280S mutant p66 and p51 using plasmid vector RT69A in Escherichia coli strain RosettaHuman immunodeficiency virus 1-714475
recombinant His6-tagged p66/p51 HIV-1 reverse transcriptase 52A variant C280S by nickel affinity chromatography, the tag is cleaved by HRV14 3C proteaseHuman immunodeficiency virus 1-715864
soluble recombinant RNase H, in an N-terminally His-tagged construct, p51-G-TCR construct, designed to encode the p51 subunit joined by a linker to the thumb (T), connection (C), and RNase H (R) domains of p66, from Escherichia coli strain MIC2067(DE3) by nickel affinity chromatographyHuman immunodeficiency virus 1-713774

Cloned/COMMENTARY ORGANISM UNIPROT ACCESSION NO. LITERATURE
-Human immunodeficiency virus 1-698694
cloning a His-tagged p66 or p51 HIV-1 RT DNA fragment into the pQE-9 vector and expression in Escherichia coli strain BL21(DE3)pLysHuman immunodeficiency virus 1-714475
expression of His-tagged enzymeHuman immunodeficiency virus 1P0C6F2716064
expression of His6-tagged p66/p51 HIV-1 reverse transcriptase p51/p66 52A variant C280S, the p66 subunit also contains the mutations K172A and K173AHuman immunodeficiency virus 1-715864
expression of RNase H domain from residue Y427 to L560 as fusion protein in Escherichia coliHuman immunodeficiency virus 1-701216
expression of RNase H, in an N-terminally His-tagged construct designed to encode the p51 subunit joined by a linker to the thumb (T), connection (C), and RNase H (R) domains of p66, in Escherichia coli strain MIC2067(DE3) lacking endogenous RNase HI and HII as soluble protein. The construct G provides sufficient RNase H activity to complement Escherichia coli growth at 42°CHuman immunodeficiency virus 1-713774
expression of the isolated RNase H domain in Escherichia coliHuman immunodeficiency virus 1-701113
isolated 125-residue RNase H domain consisiting of residues G436-L560 of polypepitde p6Human immunodeficiency virus 1-698692
separate expression of subunits in Escherichia coliHuman immunodeficiency virus 1-707509
transfection of HEK 293 cellsHuman immunodeficiency virus 1-701025
expression in Escherichia coliMoloney murine leukemia virus-707794
expression in Escherichia coliSaccharomyces cerevisiae-652277

EXPRESSION ORGANISM UNIPROT ACCESSION NO. LITERATURE
No entries in this field

ENGINEERINGORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
D549AHuman Immunodeficiency Virus-mutation in polypeptide p66, decrease in RNase H activity698709
D549NHuman Immunodeficiency Virus-mutation in polypeptide p66, decrease in RNase H activity698709
E478QHuman Immunodeficiency Virus-the efficiency with which mutant RT catalyzes transfer of nascent DNA between RNA templates is severely reduced696185
E478QHuman Immunodeficiency Virus-mutation in polypeptide p66, loss of RNase H activity698709
A360IHuman immunodeficiency virus 1-mutation in the connection domain, the mutation significantly contributes to zidovudine resistance716993
A360I/VHuman immunodeficiency virus 1-site-directed mutagenesis, a connection/RNase H domain mutant716995
A360KHuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching716993
A360VHuman immunodeficiency virus 1-mutation in the connection domain, the mutation significantly contributes to zidovudine resistance716993
A360VHuman immunodeficiency virus 1-naturally occuring mutant from clinical isolates, a connection/RNase H domain mutant that shows reduced RNase H activity716995
A371VHuman immunodeficiency virus 1-the E312Q, G333E, G335D, V365I, A371V and A376S substitutions in RNase H subdomain of HIV-1 reverse transcriptase are present in 26% of subtype B, whereas the G335D and A371V substitutions are commonly observed in 69% and 75% of non-B HIV-1 isolates, respectively707178
A371VHuman immunodeficiency virus 1-mutation in the connection domain716993
A371VHuman immunodeficiency virus 1-site-directed mutagenesis, a connection/RNase H domain mutant716995
A376SHuman immunodeficiency virus 1-the E312Q, G333E, G335D, V365I, A371V and A376S substitutions in RNase H subdomain of HIV-1 reverse transcriptase are present in 26% of subtype B. Mutations N348I, A376S and Q509L do confer varying amounts of nevirapine resistance by themselves, even in the absence of excision-enhancing mutations707178
A376SHuman immunodeficiency virus 1-mutation in the connection domain, the mutation significantly contributes to zidovudine resistance716993
A400THuman immunodeficiency virus 1-mutation in the connection domain716993
A554KHuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors716993
A554LHuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors716993
A554THuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors716993
C280EHuman immunodeficiency virus 1-RNase H activity similar to wild-type652907
C280HHuman immunodeficiency virus 1-RNase H activity similar to wild-type652907
C280LHuman immunodeficiency virus 1-RNase H activity similar to wild-type652907
C280MHuman immunodeficiency virus 1-RNase H activity similar to wild-type652907
C280PHuman immunodeficiency virus 1-significant reduction in RNase H activity. A heterodimer p66C280p/p51C280P shows about 8% of wild-type RNaseH activity, 6% of strand transfer activity, and 105% of DNA polymerase activity. A heterodimer p66C280P/p51 shows about 60% of wild-type RNaseH activity, 80% of strand transfer activity, and 100% of DNA polymerase activity. A heterodimer p66/p51C280W shows about 30% of wild-type RNaseH activity, 6% of strand transfer activity, and 99% of DNA polymerase activity652907
C280QHuman immunodeficiency virus 1-RNase H activity similar to wild-type652907
C280RHuman immunodeficiency virus 1-RNase H activity similar to wild-type652907
C280SHuman immunodeficiency virus 1-RNase H activity similar to wild-type652907
C280SHuman immunodeficiency virus 1-site-directed mutagenesis714475
C280S/K172A/K173AHuman immunodeficiency virus 1-p66/p51 HIV-1 reverse transcriptase 52A mutant variant, the mutation C208S resides in both subunits, the p66 subunit also contains the mutations K172A and K173A715864
C280WHuman immunodeficiency virus 1-significant reduction in RNase H activity. A heterodimer p66C280W/p51C280W shows about 11% of wild-type RNaseH activity, 6% of strand transfer activity, and 100% of DNA polymerase activity. A heterodimer p66C280W/p51 shows about 44% of wild-type RNaseH activity, 80% of strand transfer activity, and 98% of DNA polymerase activity. A heterodimer p66/p51C280W shows about 29% of wild-type RNaseH activity, 7% of strand transfer activity, and 100% of DNA polymerase activity652907
C280YHuman immunodeficiency virus 1-RNase H activity similar to wild-type652907
D549NHuman immunodeficiency virus 1-mutation increases the 3'-azido-3'-deoxythymidine concentration needed to inhibit viral replication by 50% 12fold by increasing the time available for excision of incorporated nucleoside reverse transcriptase inhibitors from terminated primers and results in 5- to 10fold reduction in viral titers in a single-replication cycle assay700927
D67NHuman immunodeficiency virus 1-thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-2 pathway716993
D67NHuman immunodeficiency virus 1-mutation involved in zidovudine resistance716994
D67N/K70R/T215FHuman immunodeficiency virus 1-site-directed mutagenesis690924
D67N/K70R/T215F/Q509LHuman immunodeficiency virus 1-site-directed mutagenesis690924
E312QHuman immunodeficiency virus 1-the E312Q, G333E, G335D, V365I, A371V and A376S substitutions in RNase H subdomain of HIV-1 reverse transcriptase are present in 26% of subtype B707178
E312QHuman immunodeficiency virus 1-mutation in the connection domain, the mutation significantly contributes to zidovudine resistance716993
E396AHuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching716993
E399DHuman immunodeficiency virus 1-mutation in the connection domain716993
E44AHuman immunodeficiency virus 1-mutation involved in lamivudine resistance716994
E44DHuman immunodeficiency virus 1-mutation involved in lamivudine resistance716994
E475AHuman immunodeficiency virus 1-site-directed mutagenesis, the mutant shows only minimally altered substrate specificity or enzyme activity compared to the wild-type enzyme. But the efficiency with which most mutants catalyzed polymerization-independent RNase H cleavage is sharply reduced. This deficiency is more pronounced when the mutant enzyme is challenged to process the (+) strand polypurine tract (PPT) primer from either (+) RNA or a PPT/(+) DNA RNA/DNA chimera650155
E478QHuman immunodeficiency virus 1-mutation in isolated RNase H domain, mutant fails to bind RNA/DNA hybrids. Structure of mutant is similar to wild-type698692
E478QHuman immunodeficiency virus 1-RNase H active site mutant715532
E478Q/N348IHuman immunodeficiency virus 1-mutation of RNase H active site and connection domain715532
E706QHuman immunodeficiency virus 1-site-directed mutagenesis of HIV-1 reverse transcriptase, inactive mutant; site-directed mutagenesis of the recombinant mutant construct G, E706 in construct G corresponds to E478 in HIV-1 reverse transcriptase, inactive mutant713774
E89KHuman immunodeficiency virus 1-mutation involved in foscarnet resistance716994
F160SHuman immunodeficiency virus 1-site-directed mutagenesis714475
F227LHuman immunodeficiency virus 1-mutation involved in non-nucleoside reverse transcriptase inhibitor resistance716994
G190AHuman immunodeficiency virus 1-site-directed mutagenesis, the mutant virus shows moderately reduced fitness compared to that of the wild-type virus716067
G190AHuman immunodeficiency virus 1-mutation involved in non-nucleoside reverse transcriptase inhibitor resistance716994
G190SHuman immunodeficiency virus 1-site-directed mutagenesis, the mutant virus shows moderately reduced fitness compared to that of the wild-type virus716067
G333DHuman immunodeficiency virus 1-mutation in the connection domain716993
G333EHuman immunodeficiency virus 1-the E312Q, G333E, G335D, V365I, A371V and A376S substitutions in RNase H subdomain of HIV-1 reverse transcriptase are present in 26% of subtype B707178
G333EHuman immunodeficiency virus 1-mutation in the connection domain716993
G335CHuman immunodeficiency virus 1-mutation in the connection domain, the mutation significantly contributes to zidovudine resistance716993
G335DHuman immunodeficiency virus 1-the E312Q, G333E, G335D, V365I, A371V and A376S substitutions in RNase H subdomain of HIV-1 reverse transcriptase are present in 26% of subtype B, whereas the G335D and A371V substitutions are commonly observed in 69% and 75% of non-B HIV-1 isolates, respectively707178
G335DHuman immunodeficiency virus 1-mutation in the connection domain, the mutation significantly contributes to zidovudine resistance716993
G359AHuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching716993
G509LHuman immunodeficiency virus 1-Glu to Leu substitution at residue 509 in the ribonuclease H domain of HIV-1 reverse transcriptase confers zidovudine resistance, mechanism, overview. Q509L increases zidovudine monophosphate excision activity of RT on RNA/DNA template/primers, but not DNA/DNA template/primers, due to Q509L decreasing a secondary RNase H cleavage event that reduces the RNA/DNA duplex length to 10 nucleotides and significantly impairs the enzyme's ability to excise the chain-terminating nucleotide. Mutation Q509L does not affect initial rates of the polymerase-directed RNase H activity but only polymerase-independent cleavages that occur after a template/primer dissociation event. Q509L decreases the affinity of the enzyme to bind template/primers with duplex lengths less than 18 nucleotides in the polymerase-independent RNase H cleavage mode, while not affecting the enzyme's affinity to bind the same template/primers in an zidovudine monophosphate excision competent mode690924
G544StopHuman immunodeficiency virus 1-C-terminal truncation of p66 polypeptide. Loss of RNase H activity, while dimerization with polypepitde p51 and DNA polymerase activity are not significantly affected698701
H539FHuman immunodeficiency virus 1-mutation in isolated RNase H domain, mutant fails to bind RNA/DNA hybrids. Structure of mutant is similar to wild-type698692
H539NHuman immunodeficiency virus 1-increases the 3'-azido-3'-deoxythymidine concentration needed to inhibit viral replication by 50% 180fold relative to wild-type by increasing the time available for excision of incorporated nucleoside reverse transcriptase inhibitors from terminated primers700927
I505AHuman immunodeficiency virus 1-no discernible effect on viral titer701025
I505AHuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching716993
I505GHuman immunodeficiency virus 1-site-directed mutagenesis, the mutant exhibits a dimerization defect. The efficiency with which most mutants catalyzed polymerization-independent RNase H cleavage is sharply reduced. This deficiency is more pronounced when the mutant enzyme is challenged to process the (+) strand polypurine tract (PPT) primer from either (+) RNA or a PPT/(+) DNA RNA/DNA chimera650155
K103NHuman immunodeficiency virus 1-site-directed mutagenesis, the mutation does not affect RNase H function714972
K103NHuman immunodeficiency virus 1-a classic NNRTI resistance mutation715532
K103NHuman immunodeficiency virus 1-site-directed mutagenesis, the mutant virus shows fitness similar to that of the wild-type virus716067
K103NHuman immunodeficiency virus 1-mutation involved in non-nucleoside reverse transcriptase inhibitor resistance716994
K219EHuman immunodeficiency virus 1-thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-2 pathway716993
K219NHuman immunodeficiency virus 1-thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-2 pathway716993
K219QHuman immunodeficiency virus 1-thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-2 pathway716993
K219QHuman immunodeficiency virus 1-mutation involved in zidovudine resistance716994
K390AHuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching716993
K395AHuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching716993
K451RHuman immunodeficiency virus 1-mutation present in viral isolates of 11% of antiviral treatment-experienced patients but remaining 100% conserved among treatment-naive patients695644
K476AHuman immunodeficiency virus 1-site-directed mutagenesis, the mutant shows only minimally altered substrate specificity or enzyme activity compared to the wild-type enzyme. But the efficiency with which most mutants catalyzed polymerization-independent RNase H cleavage is sharply reduced. This deficiency is more pronounced when the mutant enzyme is challenged to process the (+) strand polypurine tract (PPT) primer from either (+) RNA or a PPT/(+) DNA RNA/DNA chimera650155
K476AHuman immunodeficiency virus 1-mutation reduces the viral titer less than 2fold701025
K476AHuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching716993
K558EHuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, associated with an increase in thymidine analogue mutations, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors716993
K558GHuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, associated with an increase in thymidine analogue mutations, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors716993
K558RHuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, associated with an increase in thymidine analogue mutations, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors716993
K65RHuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, arises with abacavir, didanosine, emtricitabine, lamivudine, or tenofovir disoproxil fumarate treatment716993
K65RHuman immunodeficiency virus 1-mutation involved in nucleos(t)ide reverse transcriptase inhibitor resistance716994
K65R/Q151M/A62V/V75I/F77L/F116YHuman immunodeficiency virus 1-mutation involved in nucleos(t)ide reverse transcriptase inhibitor resistance716994
K70RHuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, is common to stavudine, tenofovir disoproxil fumarate, and zidovudine therapy; thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-2 pathway716993
K70RHuman immunodeficiency virus 1-mutation involved in zidovudine resistance716994
L100IHuman immunodeficiency virus 1-mutation involved in non-nucleoside reverse transcriptase inhibitor resistance716994
L210WHuman immunodeficiency virus 1-thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-1 pathway716993
L210WHuman immunodeficiency virus 1-mutation involved in zidovudine resistance716994
L469HHuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors716993
L469IHuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors716993
L469MHuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors716993
L469THuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors716993
L74VHuman immunodeficiency virus 1-mutation involved in nucleos(t)ide reverse transcriptase inhibitor resistance716994
M184VHuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, arises with abacavir, emtricitabine, or lamivudine treatment716993
M230LHuman immunodeficiency virus 1-the naturally occuring mutation leads to reduced RNase H activity of the HIV reverse transcriptase713770
M41LHuman immunodeficiency virus 1-thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-1 pathway716993
N348IHuman immunodeficiency virus 1-mutations N348I, A376S and Q509L do confer varying amounts of nevirapine resistance by themselves, even in the absence of excision-enhancing mutations707178
N348IHuman immunodeficiency virus 1-connection domain mutant, altered RNase H cleavage pattern compared to the wild-type HIV-1 RT715532
N348IHuman immunodeficiency virus 1-mutation in the connection domain, the mutation significantly contributes to zidovudine resistance716993
N348IHuman immunodeficiency virus 1-naturally occuring mutant from clinical isolates, a connection/RNase H domain mutant that shows reduced RNase H activity716995
N474AHuman immunodeficiency virus 1-mutation reduces the viral titer less than 2fold701025
N474A/Q475AHuman immunodeficiency virus 1-mutation reduces the viral titer 5- to 10fold, , reduction in the efficiency of DNA synthesis. Mutant is less efficient than the wild-type enzyme in its ability to remove a polypurine tract primer from a model substrate and has an altered RNase H cleavage specificity701025
N494DHuman immunodeficiency virus 1-mutant closely resembles the wild-type RNase H, exhibits an endonuclease activity and a processive RNase H activity, gives rise to small RNA hydrolysis products, and acts in concert with the reverse transcriptase698694
P236LHuman immunodeficiency virus 1-site-directed mutagenesis, the mutant virus shows substantially reduced fitness compared to that of the wild-type virus716067
P537StopHuman immunodeficiency virus 1-C-terminal truncation of p66 polypeptide. Loss of RNase H activity, while dimerization with polypepitde p51 and DNA polymerase activity are not significantly affected698701
Q151MHuman immunodeficiency virus 1-mutation involved in nucleos(t)ide reverse transcriptase inhibitor resistance716994
Q151M/A62V/V75I/F77L/F116YHuman immunodeficiency virus 1-mutation involved in nucleos(t)ide reverse transcriptase inhibitor resistance716994
Q475AHuman immunodeficiency virus 1-mutation reduces the viral titer 5- to 10fold701025
Q475AHuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching716993
Q475EHuman immunodeficiency virus 1-mutant exhibits a retarded endonuclease activity and an impaired 3'-5' processive RNA cleavage activity, gives rise to predominantly larger RNA hydrolysis products, is less processive in the presence of competitor substrate, and is defective in its ability to hydrolyze the polypurine tract and homopolymeric hybrids698694
Q500AHuman immunodeficiency virus 1-mutation reduces the viral titer less than 2-fold701025
Q509LHuman immunodeficiency virus 1-mutations N348I, A376S and Q509L do confer varying amounts of nevirapine resistance by themselves, even in the absence of excision-enhancing mutations707178
Q509LHuman immunodeficiency virus 1-mutation in the RNase H domain, the mutation significantly contributes to zidovudine resistance716993
Q509LHuman immunodeficiency virus 1-site-directed mutagenesis, a connection/RNase H domain mutant716995
R448AHuman immunodeficiency virus 1-no discernible effect on viral titer701025
T215FHuman immunodeficiency virus 1-thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-2 pathway716993
T215FHuman immunodeficiency virus 1-mutation involved in zidovudine resistance716994
T215YHuman immunodeficiency virus 1-thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-1 pathway716993
T215YHuman immunodeficiency virus 1-mutation involved in zidovudine resistance716994
T369IHuman immunodeficiency virus 1-mutation in the connection domain716993
T470EHuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors716993
T470KHuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors716993
T470PHuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors716993
T470SHuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors716993
T473AHuman immunodeficiency virus 1-site-directed mutagenesis, the mutant shows only minimally altered substrate specificity or enzyme activity compared to the wild-type enzyme. But the efficiency with which most mutants catalyzed polymerization-independent RNase H cleavage is sharply reduced. This deficiency is more pronounced when the mutant enzyme is challenged to process the (+) strand polypurine tract (PPT) primer from either (+) RNA or a PPT/(+) DNA RNA/DNA chimera650155
T473AHuman immunodeficiency virus 1-mutation abolishes viral replication701025
T473CHuman immunodeficiency virus 1-the mutation increases the sensitivity of the enzyme for inhibitor NSC727447 by 50fold716995
T473MHuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching716993
V106AHuman immunodeficiency virus 1-site-directed mutagenesis, the mutant virus shows moderately reduced fitness compared to that of the wild-type virus716067
V106AHuman immunodeficiency virus 1-mutation involved in non-nucleoside reverse transcriptase inhibitor resistance716994
V365IHuman immunodeficiency virus 1-the E312Q, G333E, G335D, V365I, A371V and A376S substitutions in RNase H subdomain of HIV-1 reverse transcriptase are present in 26% of subtype B707178
V365IHuman immunodeficiency virus 1-mutation in the connection domain, the mutation significantly contributes to zidovudine resistance716993
V552StopHuman immunodeficiency virus 1-C-terminal truncation of p66 polypeptide. Mutant retains endonuclease activity but lacks the directional processing feature of wild-type and barely supports transfer of nascent (-)-stranded DNA between RNA templates698701
W229FHuman immunodeficiency virus 1-mutation in primer grip residue, specificity of cleavage is not compromised, efficiency is reduced to 33-44% of wild-type696189
W229F/Y232WHuman immunodeficiency virus 1-mutation in primer grip residues, specificity of cleavage is not compromised, efficiency is reduced to 33-44% of wild-type696189
W229YHuman immunodeficiency virus 1-mutation in primer grip residue, specificity of cleavage is not compromised, efficiency is reduced to 33-44% of wild-type696189
W88GHuman immunodeficiency virus 1-mutation involved in foscarnet resistance716994
Y181CHuman immunodeficiency virus 1-site-directed mutagenesis, the mutation does not affect RNase H function714972
Y181CHuman immunodeficiency virus 1-a classic NNRTI resistance mutation715532
Y181CHuman immunodeficiency virus 1-site-directed mutagenesis, the mutant virus shows fitness similar to that of the wild-type virus716067
Y181CHuman immunodeficiency virus 1-mutation involved in non-nucleoside reverse transcriptase inhibitor resistance716994
Y181CHuman immunodeficiency virus 1-site-directed mutagenesis, the mutant shows resistance to non-nucleoside reverse transcriptase inhibitors716995
Y188CHuman immunodeficiency virus 1-mutation involved in non-nucleoside reverse transcriptase inhibitor resistance716994
Y188LHuman immunodeficiency virus 1-mutation involved in non-nucleoside reverse transcriptase inhibitor resistance716994
Y229F/Y232FHuman immunodeficiency virus 1-mutation in primer grip residues, specificity of cleavage is not compromised, efficiency is reduced to 33-44% of wild-type696189
Y232WHuman immunodeficiency virus 1-mutation in primer grip residue, specificity of cleavage is not compromised, efficiency is reduced to 33-44% of wild-type696189
Y318FHuman immunodeficiency virus 1-mutation in the connection domain716993
Y501AHuman immunodeficiency virus 1-site-directed mutagenesis, the mutant shows only minimally altered substrate specificity or enzyme activity compared to the wild-type enzyme. But the efficiency with which most mutants catalyzed polymerization-independent RNase H cleavage is sharply reduced. This deficiency is more pronounced when the mutant enzyme is challenged to process the (+) strand polypurine tract (PPT) primer from either (+) RNA or a PPT/(+) DNA RNA/DNA chimera650155
Y501AHuman immunodeficiency virus 1-mutation reduces the viral titer 5- to 10fold, reduction in the efficiency of DNA synthesis. Mutant is less efficient than the wild-type enzyme in its ability to remove a polypurine tract primer from a model substrate and has an altered RNase H cleavage specificity701025
Q294PHuman immunodeficiency virus 2-site-directed mutagenesis of a residue in the catalytically inactive p54 subunit resulting in an increase in RNase H activity comparable with that of HIV-1 reverse transcriptase716995
A128TMoloney murine leukemia virus-the mutant strain is resistant to 2-hydroxyisoquinoline-1,3(2H,4H)-dione inhibitors in contrast to the wild-type715859
C635VMoloney murine leukemia virus-site-directed mutagenesis, the mutant shows slightly reduced reverse transcriptase and RNAse H activities compared the wild-type enzyme716354
D524AMoloney murine leukemia virus-mutant lacks RNase H activity, but retains reverse transcriptase activity. Elimination of RNase H activity enhances the intrinsic thermal stability of the protein rather than its affinity to template-primer; site-directed mutagenesis, RNase H-inactive mutant, that shows increased intrinsic thermal stability compared to the wild-type enzyme. The mutant loses RNase H activity through abolishing of Mg2+ binding to the RNase H domain707794
D524NMoloney murine leukemia virus-loss of catalytic activity. Construction of vectors encapsidated in virions engineered to contain phenotypic mixtures of wild-type and RNase H catalytic site point mutant D524N reverse transcriptase. There is a steady decline in direct repeat deletion frequency that correlates with decreases in functional RNase H, with greater than fourfold decreases in repeat deletion frequency observed when 95% of virion reverse transcriptase is RNase H defective699895
D524NMoloney murine leukemia virus-less than 0.5% of wild-type activity, no binding of Mn2+701049
D583AMoloney murine leukemia virus-site-directed mutagenesis, RNase H-inactive mutant, that shows increased intrinsic thermal stability compared to the wild-type enzyme. The mutant loses RNase H activity through abolishing of Mg2+ binding to the RNase H domain707794
D583NMoloney murine leukemia virus-less than 0.5% of wild-type activity, no binding of Mn2+701049
D653NMoloney murine leukemia virus-4% of wild-type activity701049
E562QMoloney murine leukemia virus-less than 0.5% of wild-type activity, no binding of Mn2+701049
G140S/Q148HMoloney murine leukemia virus-the mutant strain is resistant to 2-hydroxyisoquinoline-1,3(2H,4H)-dione inhibitors in contrast to the wild-type715859
D358NSaccharomyces cerevisiae-mutation eliminates Mg2+- and Mn2+-dependent RNase H function652277
D426NSaccharomyces cerevisiae-mutation eliminates Mg2+- and Mn2+-dependent RNase H function652277
D469NSaccharomyces cerevisiae-reduced RNase H activity in presence of Mg2+, decrease of turnover rate in presence of Mn2+. Mutant fails to support DNA strand transfer and release of the (+)-strand polypurine tract primer from (+)-RNA652277
E401QSaccharomyces cerevisiae-mutation eliminates Mg2+- and Mn2+-dependent RNase H function652277
H427ASaccharomyces cerevisiae-reduced RNase H activity in presence of Mg2+, decrease of turnover rate in presence of Mn2+. Mutant fails to support DNA strand transfer and release of the (+)-strand polypurine tract primer from (+)-RNA652277
Y459ASaccharomyces cerevisiae-reduced RNase H activity in presence of Mg2+, decrease of turnover rate in presence of Mn2+. Mutant fails to support DNA strand transfer and release of the (+)-strand polypurine tract primer from (+)-RNA652277
M41LHuman immunodeficiency virus 1-mutation involved in zidovudine resistance716994
additional informationHuman immunodeficiency virus 1-RNase H primer grip mutations suppress polymerization-independent RNase H cleavage. Alteration of RNase H primer grip residues Thr473, Asn474, and Gln475 has little influence on cleavage specificity. Altering the RNase H domain of HIV-1 RT can impact significantly on the ability of mutant enzymes to catalyze DNA synthesis, but all RNase H primer grip mutants show little difference in their DNA-dependent DNA polymerase activity650155
additional informationHuman immunodeficiency virus 1-construction of chimeric HIV-1/HIV-2 reverse transcriptases, in which protein segments and/or subunits are exchanged. The RNase H specific activity of the chimeric enzymes is either high like HIV-1 reverse transcriptase or low like HIV-2 reverse transcriptase. The origin of the thumb subdomain in the small subunit of the chimeric reverse transcriptases, residues 244-322 determines the level of the RNase H activity652865
additional informationHuman immunodeficiency virus 1-chemical modifications by thiol-specific reagents of cysteine 280, located in a helix I in the thumb subdomain of the polymerase domain, affect substantially only the RNase H activity652907
additional informationHuman immunodeficiency virus 1-construction of two chimeric enzymes by swapping the RNase H domains between HIV-1 RT and Moloney murine leukemia virus MuLV RT. Chimeric HIV-1 RT, having the RNase H domain of MuLV RT, inherits the divalent cation preference characteristic of MuLV RT on the DNA template with no significant change on the RNA template. Chimeric MuLV RT, likewise partially inherits the metal ion preference of HIV-1 RT. Unlike the wild-type MuLV RT, chimeric MuLV RT is able to use both Mn-dNTP and Mg-dNTP on the RNA template with similar efficiency, while a 30-fold higher preference for Mn.dNTP was seen on the DNA template. The metal preferences for the RNase H activity of chimeric HIV-1 RT and chimeric MuLV RT are, respectively, Mn2+ and Mg2+, a property acquired through their swapped RNase H domains. Chimeric HIV-1 RT displays higher fidelity and discrimination against rNTPs than against dNTPs substrates, a property inherited from MuLV RT. The overall fidelity of the chimeric MuLV RT is decreased in comparison to the parental MuLV RT, suggesting that the RNase H domain profoundly influences the function of the polymerase domain710674
additional informationHuman immunodeficiency virus 1-construction of an N-terminally His-tagged mutant p51-G-TCR construct designed to encode the p51 subunit joined by a linker to the thumb (T), connection (C), and RNase H (R) domains of p66, the p51-G-TCR RNase H construct displays Mg2+-dependent activity using a fluorescent nonspecific assay and shows the same cleavage pattern as HIV-1 reverse transcriptase on substrates that mimic the tRNA removal required for second-strand transfer reactions. The RNase H of the p51-G-TCR RNase H construct and wild-type HIV-1 reverse transcriptase have similar Kms for an RNA-DNA hybrid substrate and show similar inhibition kinetics to two known inhibitors of the HIV-1 reverse transcriptase RNase H, molecular modeling713774
Y501AHuman immunodeficiency virus 1-naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching716993
additional informationHuman immunodeficiency virus 2-construction of chimeric HIV-1/HIV-2 reverse transcriptases, in which protein segments and/or subunits are exchanged. The RNase H specific activity of the chimeric enzymes is either high like HIV-1 reverse transcriptase or low like HIV-2 reverse transcriptase. The origin of the thumb subdomain in the small subunit of the chimeric reverse transcriptases, residues 244-322 determines the level of the RNase H activity652865
H638GMoloney murine leukemia virus-15% of wild-type activity701049
additional informationMoloney murine leukemia virus-deletion of 204 nucleotides at the 3'-terminus results in 4fold increase in activity level upon recombinant expression and allows for high-level production of the protein643436
additional informationMoloney murine leukemia virus-construction of two chimeric enzymes by swapping the RNase H domains between HIV-1 RT and Moloney murine leukemia virus MuLV RT. Chimeric HIV-1 RT, having the RNase H domain of MuLV RT, inherits the divalent cation preference characteristic of MuLV RT on the DNA template with no significant change on the RNA template. Chimeric MuLV RT, likewise partially inherits the metal ion preference of HIV-1 RT. Unlike the wild-type MuLV RT, chimeric MuLV RT is able to use both Mn-dNTP and Mg-dNTP on the RNA template with similar efficiency, while a 30-fold higher preference for Mn.dNTP was seen on the DNA template. The metal preferences for the RNase H activity of chimeric HIV-1 RT and chimeric MuLV RT are, respectively, Mn2+ and Mg2+, a property acquired through their swapped RNase H domains. Chimeric HIV-1 RT displays higher fidelity and discrimination against rNTPs than against dNTPs substrates, a property inherited from MuLV RT. The overall fidelity of the chimeric MuLV RT is decreased in comparison to the parental MuLV RT, suggesting that the RNase H domain profoundly influences the function of the polymerase domain710674
additional informationMoloney murine leukemia virus-site-directed chemical modification of the RNase H domain by selectively PEGylating Cys635, one of the eight cysteine residues present in the reverse transcriptase, specifically inactivates its ribonucleolytic activity, PEGylation as a tool for engineering the M-MuLV RT derivative deficient in RNase H activity, overview716354
additional informationmurine leukemia virus-construction of a chimeric enzyme containing the first 425 amino acid residues from the N-terminal domain of HIV-1 reverse transcriptase, i.e. the polymerase domain, and 200 amino acid residues from the C-terminal domain of murine leukemia virus reverse transcriptase, i.e. RNase H-domain. The chimeric enzyme exists as a monomer with intact DNA polymerase and RNase-H functions. It is able to catalyze both endonucleolytic and processive RNase-H functions in a manner similar to the wild type HIV-1 reverse transcriptase and murineleukemia virus reverse transcriptase698711

Renatured/COMMENTARYORGANISM UNIPROT ACCESSION NO.LITERATURE
Refolding of the isolated HIV RNase H domain shows a kinetic intermediate detectable by stopped-flow far UV circular dichroism and pulse-labeling H/D exchange. In this intermediate, strands 1, 4, and 5 as well as helices A and D appear to be structured. Compared to its homolog from Escherichia coli, the rate limiting step in refolding of HIV RNase H appears closer to the native state. This kinetic intermediate has been modeled using a C-terminal deletion fragment lacking helix E. Like the kinetic intermediate, this variant folds rapidly and shows a decrease in stabilityHuman immunodeficiency virus 1-701113

APPLICATIONORGANISM UNIPROT ACCESSION NO.COMMENTARYLITERATURE
analysisHuman immunodeficiency virus 1-use of a commercially available computed radiography system for dental radiography to produce images from radiolabeled polyacrylamide gel electrophoresis assays and its application for quantitative analyses of the human immunodeficiency virus type 1 reverse transcriptase polymerase-independent ribonuclease H activity monitored by PAGE analysis. The methodology allows quantifying effectively the RNase H catalyses and the obtained data are in good agreement with previous reference works710132
analysisHuman immunodeficiency virus 1-use of 6-phenylpyrrolocytidine as a sensitive fluorescent reporter group being non-disruptive to structure and the enzymatic activity of RNase H. A RNA/DNA hybrid possessing a single 6-phenylpyrrolocytidine insert is an excellent substrate for HIV-1 RT Ribonuclease H and rapidly reports cleavage of the RNA strand with a 14-fold increase in fluorescence intensity. The 6-phenylpyrrolocytidine-based assay for RNase H is superior to the traditional molecular beacon approach in terms of responsiveness, rapidity and ease. The assay is amenable to high-throughput microplate assay format710144
drug developmentHuman immunodeficiency virus 1-RNase H activity is an attractive target for a new class of antiviral drugs714475
medicineHuman immunodeficiency virus 1-genotypical and statistical analyzes in HIV-1 reverse transcriptase from antiretroviral treatment-naive and antiretroviral treatment-experienced patients. Within the RNase H domain, change K451 is present in 11% of treatment-experienced patients, but not in treatment-naive patients; within the RNase domain, mutation K451R is present in viral isolates of 11% of antiviral treatment-experienced patients but remaining 100% conserved among treatment-naive patients695644
medicineHuman immunodeficiency virus 1-the E312Q, G333E, G335D, V365I, A371V and A376S substitutions in RNase H subdomain of HIV-1 reverse transcriptase are present in 26% of subtype B, whereas the G335D and A371V substitutions are commonly observed in 69% and 75% of non-B HIV-1 isolates, respectively. A significant decline is observed in the viral loads of patients that are infected with HIV-1 carrying these substitutions and are subsequently treated with triple drug regimens, even in the case where zidovudine is included in such regimens. Generally, such single substitutions at the connection subdomain or RNase H domain have no influence on drug susceptibility in vitro by themselves. Instead, they generally enhance zidovudine resistance in the presence of excision-enhancing mutations. However, N348I, A376S and Q509L do confer varying amounts of nevirapine resistance by themselves, even in the absence of excision-enhancing mutations707178
pharmacologyHuman immunodeficiency virus 1-mutations in RNase H can significantly contribute to drug resistance either alone or in combination with nucleoside reverse transcriptase inhibitor-resistance mutations in reverse transcriptase. There exists an equilibrium between nucleoside reverse transcriptase inhibitor incorporation, nucleoside reverse transcriptase inhibitor excision, and resumption of DNA synthesis and degradation of the RNA template by RNase H activity, leading to dissociation of the template-primer and abrogation of HIV-1 replication700927

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643436Roth, M.J.; Tanese, N.; Goff, S.P.Purification and characterization of murine retroviral reverse transcriptase expressed in Escherichia coliJ. Biol. Chem.2609326-93351985Moloney murine leukemia virus PubMed
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696183Peliska, J.A.; Balasubramanian, S.; Giedroc, D.P.; Benkovic, S.J.Recombinant HIV-1 nucleocapsid protein accelerates HIV-1 reverse transcriptase catalyzed DNA strand transfer reactions and modulates RNase H activityBiochemistry3313817-138231994Human immunodeficiency virus 1 PubMed
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