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Literature summary for 3.1.26.13 extracted from
- Substituting a conserved residue of ribonuclease H domain alters substrate hydrolysis by retroviral reverse transcriptase (1997), J. Biol. Chem., 272, 8602-8610.
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D549A | mutation in polypeptide p66, decrease in RNase H activity | Human Immunodeficiency Virus |
| D549N | mutation in polypeptide p66, decrease in RNase H activity | Human Immunodeficiency Virus |
| E478Q | mutation in polypeptide p66, loss of RNase H activity | 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 | evaluation of activity by enzyme's ability to select and extend the 3' polypurine tract primers into (+) strand DNA. Evaluation via concerted and two-step reactions for (+) strand priming, the latter of which allows discrimination between selection end extension events | Human Immunodeficiency Virus | ? | 3' polypurine tract primer selection appears to represent a specialized form of RNase H activity that is more sensitive to minor structural alterations within this domain | ? |  |
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