Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.26.13 extracted from

  • Beilhartz, G.; Goette, M.
    HIV-1 ribonuclease H: structure, catalytic mechanism and inhibitors (2010), Viruses, 2, 900-926.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure analysis, overview. The pyrimidinol carboxylic acids is successful crystallized with Mn2+ and the isolated HIV RNase H domain Human immunodeficiency virus 1

Protein Variants

Protein Variants Comment Organism
A360I/V site-directed mutagenesis, a connection/RNase H domain mutant Human immunodeficiency virus 1
A360V naturally occuring mutant from clinical isolates, a connection/RNase H domain mutant that shows reduced RNase H activity Human immunodeficiency virus 1
A371V site-directed mutagenesis, a connection/RNase H domain mutant Human immunodeficiency virus 1
N348I naturally occuring mutant from clinical isolates, a connection/RNase H domain mutant that shows reduced RNase H activity Human immunodeficiency virus 1
Q294P 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 transcriptase Human immunodeficiency virus 2
Q509L site-directed mutagenesis, a connection/RNase H domain mutant Human immunodeficiency virus 1
T473C the mutation increases the sensitivity of the enzyme for inhibitor NSC727447 by 50fold Human immunodeficiency virus 1
Y181C site-directed mutagenesis, the mutant shows resistance to non-nucleoside reverse transcriptase inhibitors Human immunodeficiency virus 1

Inhibitors

Inhibitors Comment Organism Structure
(4-N,N-dimethylaminobenzoyl)-2-hydroxy-1-naphthyl hydrazone specific Human immunodeficiency virus 1
2,7-dihydroxy-4-(propan-2-yl)cyclohepta-2,4,6-trien-1-one
-
Human immunodeficiency virus 1
2-(3,4-dichlorobenzyl)-5,6-dihydroxypyrimidine-4-carboxylic acid
-
Human immunodeficiency virus 1
2-amino-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
-
Human immunodeficiency virus 1
2-hydroxyisoquinoline-1,3(2H,4H)-dione
-
Human immunodeficiency virus 1
3,4-dihydroxy-N'-[(E)-(2-methoxynaphthalen-1-yl)methylidene]benzohydrazide
-
Human immunodeficiency virus 1
ethyl (5E)-6-[1-(4-fluorobenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoate
-
Human immunodeficiency virus 1
additional information discovery and development of bona fide RNase H inhibitors, overview Human immunodeficiency virus 1
NSC727447 mutation T473C increases sensitivity of the enzyme for NSC727447 by 50fold Human immunodeficiency virus 1

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ one Mg2+ ion in the RNase H active site, required Human immunodeficiency virus 1
Mg2+ one Mg2+ ion in the RNase H active site, required Human immunodeficiency virus 2

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Human immunodeficiency virus 1 RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids, substrate binding and reaction mechanism, overview ?
-
?
additional information 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, overview ?
-
?

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 1
-
HIV-1
-
Human immunodeficiency virus 2
-
HIV-2
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids, substrate binding and reaction mechanism, overview Human immunodeficiency virus 1 ?
-
?
additional information RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids, substrate binding and reaction mechanism, overview Human immunodeficiency virus 2 ?
-
?

Subunits

Subunits Comment Organism
More 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 regions Human immunodeficiency virus 1

Synonyms

Synonyms Comment Organism
HIV-1 RT-associated RNase H
-
Human immunodeficiency virus 1
ribonuclease H
-
Human immunodeficiency virus 1
ribonuclease H
-
Human immunodeficiency virus 2
RNase H
-
Human immunodeficiency virus 1
RNase H
-
Human immunodeficiency virus 2

General Information

General Information Comment Organism
additional information Q294 is highly conserved in HIV-2 isolates Human immunodeficiency virus 2
additional information 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, overview Human immunodeficiency virus 1
physiological function 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, overview Human immunodeficiency virus 1
physiological function 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, overview Human immunodeficiency virus 2