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Literature summary for 3.1.26.13 extracted from

  • Starnes, M.; Cheng, Y.
    Human immunodeficiency virus reverse transcriptase-associated RNase H activity (1989), J. Biol. Chem., 264, 7073-7077.
    View publication on PubMed
Search for more literature for 3.1.26.13

Metals/Ions

Metals/Ions Comment Organism Structure
KCl optimum concentration 50 mM Human Immunodeficiency Virus
Mg2+ required, with more than 90% of maximum activity between 4 and 12 mM Human Immunodeficiency Virus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
110000
-
 glycerol gradient centrifugation Human Immunodeficiency Virus

Organism

Organism UniProt Comment Textmining
Human Immunodeficiency Virus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information no substrate: single-stranded RNA or the DNA component of DNA-RNA hybrids. Products consist primarily of monomers, dimers, and trimers with 3'-OH groups Human Immunodeficiency Virus ?
-
 ?
poly(dC)-poly(rG) + H2O
-
 Human Immunodeficiency Virus ?
-
 ?
poly(dT)-poly(rA) + H2O substrate poly(dC)-poly(rG) is markedly preferred over substrate poly(dT)-poly(rA) Human Immunodeficiency Virus ?
-
 ?

Subunits

Subunits Comment Organism
More RNase H activity is associated with the p66 component of reverse transcriptase Human Immunodeficiency Virus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8 8.5
-
 Human Immunodeficiency Virus