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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
human foamy virus | |
NaCl | - |
human foamy virus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
human foamy virus | - |
- |
- |
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 | 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 | Comment | Organism |
---|---|---|
More | the enzyme is part of the reverse transcriptase | human foamy virus |
RNase H | - |
human foamy virus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | human foamy virus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
assay at | human foamy virus |