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Literature summary for 2.7.7.7 extracted from
- Strand annealing and terminal transferase activities of a B-family DNA polymerase (2011), Biochemistry, 50, 5379-5390.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharolobus solfataricus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| deoxynucleoside triphosphate + DNAn | the enzyme possess a remarkable DNA stabilizing ability for maintaining weak base pairing interactions to facilitate primer extension. This thermal stabilization by Dpo1 allows for template-directed synthesis at temperatures more than 30°C above the melting temperature of naked DNA. Dpo1 elongates single stranded DNA in template-dependent and template-independent manners. Initial deoxyribonucleotide incorporation is complementary to the template. Rate-limiting steps that include looping back and annealing to the template allow for a unique template-dependent terminal transferase activity. Dpo1 also displays a competing terminal deoxynucleotide transferase activity unlike any other B-family DNA polymerase | Saccharolobus solfataricus | diphosphate + DNAn+1 | - |
? |  |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| DNA replication polymerase | - |
Saccharolobus solfataricus |
| Dpo1 | - |
Saccharolobus solfataricus |
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