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Literature summary for 3.1.13.2 extracted from

  • Mueller, G.A.; Pari, K.; DeRose, E.F.; Kirby, T.W.; London, R.E.
    Backbone dynamics of the RNase H domain of HIV-1 reverse transcriptase (2004), Biochemistry, 43, 9332-9342.
    View publication on PubMed
Search for more literature for 3.1.13.2

Activating Compound

Activating Compound Comment Organism Structure
AMP activates, causes conformational changes on some sites of the enzyme N-terminus near strand beta2 and beta3 andhelix alphaA, residues 28-69 Human immunodeficiency virus 1

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information backbone and reaction dynamics, kinetics, NMR relaxation study of the isolated RNase H domain, effect of pH on backbone dynamics, different motional models, overview Human immunodeficiency virus 1

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activates, causes conformational changes on some sites of the enzyme N-terminus near strand beta2 and beta3 and helix alphaA, residues 28-69 Human immunodeficiency virus 1

Organism

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

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DNA-RNA hybrid + H2O
-
 Human immunodeficiency virus 1 ?
-
 ?
additional information the enzyme is part of the viral reverse transcriptase, the isolated RNase H domain is inactive at low pH Human immunodeficiency virus 1 ?
-
 ?

Synonyms

Synonyms Comment Organism
More the enzyme is part of the viral reverse transcriptase Human immunodeficiency virus 1
ribonuclease H
-
 Human immunodeficiency virus 1
RNase H
-
 Human immunodeficiency virus 1

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.4 6.8 assay at pH 5.4, pH 5.5, and pH 6.8 Human immunodeficiency virus 1