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

BRENDA support

Literature summary for 3.1.13.2 extracted from

  • Purohit, V.; Roques, B.P.; Kim, B.; Bambara, R.A.
    Mechanisms that prevent template inactivation by HIV-1 reverse transcriptase RNase H cleavages (2007), J. Biol. Chem., 282, 12598-12609.
    View publication on PubMed
Search for more literature for 3.1.13.2

Inhibitors

Inhibitors Comment Organism Structure
3'-azido-3'-deoxythymidine
-
 Human immunodeficiency virus 1

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Human immunodeficiency virus 1

Organism

Organism UniProt Comment Textmining
Human immunodeficiency virus 1
-
 i.e. HIV-1
-

Reaction

Reaction Comment Organism Reaction ID
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid RNase H catalytic cleavage mechanism for end-directed primary and secondary cleavages Human immunodeficiency virus 1
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DNA-RNA hybrid + H2O the RNaseH activity of HIV-1 reverse transcriptase cleaves the viral genome concomitant with minus strand synthesis during pausing of the reverse transcriptase activity, RNase H cleavage on a hairpin containing RNA template system, overview, pause-related 3' end-directed secondary cuts decreased primer extendibility, relationship between cleavage of the RNA template and extension of a DNA primer, mechanism, overview Human immunodeficiency virus 1 ?
-
 ?

Synonyms

Synonyms Comment Organism
RNase H
-
 Human immunodeficiency virus 1

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Human immunodeficiency virus 1

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at Human immunodeficiency virus 1