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Literature summary for 3.1.13.2 extracted from

  • Boyer, P.L.; Stenbak, C.R.; Clark, P.K.; Linial, M.L.; Hughes, S.H.
    Characterization of the polymerase and RNase H activities of human foamy virus reverse transcriptase (2004), J. Virol., 78, 6112-6121.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.13.2

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type reverse transcriptase in fusion with the viral inactivated protease mutant D24A in Escherichia coli, the recombinant fusion protein shows reverse transcriptase activity, i.e. DNA polymerase activity with an RNA template, and RNase activity, and also strand displacement activity, overview human foamy virus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 human foamy virus
NaCl
-
 human foamy virus

Organism

Organism UniProt Comment Textmining
human foamy virus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DNA-RNA hybrid + H2O cleavage site specificity at -17, -12 and -8 from the 5' end positions of the RNA strand in 3' to 5' direction, overview human foamy virus ?
-
 ?
additional information the enzyme is part of the viral reverse transcriptase, RNase H substrate synthesis by the enzyme's RT activity human foamy virus ?
-
 ?

Subunits

Subunits Comment Organism
More the enzyme is part of the viral reverse transcriptase containing a basic loop in the RNase H domain with a unique sequence human foamy virus

Synonyms

Synonyms Comment Organism
More the enzyme is part of the reverse transcriptase human foamy virus
RNase H
-
 human foamy virus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at human foamy virus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
 assay at human foamy virus