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Literature summary for 2.7.7.7 extracted from
- Single-molecule investigation of substrate binding kinetics and protein conformational dynamics of a B-family replicative DNA polymerase (2013), J. Biol. Chem., 288, 11590-11600.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | biphasic dissociation kinetics of the polymerase-DNA binary complex | Saccharolobus solfataricus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| deoxynucleoside triphosphate + DNAn | Saccharolobus solfataricus | - |
diphosphate + DNAn+1 | - |
? |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharolobus solfataricus | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| deoxynucleoside triphosphate + DNAn | - |
Saccharolobus solfataricus | diphosphate + DNAn+1 | - |
? | |
| deoxynucleoside triphosphate + DNAn | the enzyme binds to DNA in at least three distinct conformations. The relative frequency of each conformation can be modulated by both the identity of the primer 3' terminus and the presence of an incoming dNTP | Saccharolobus solfataricus | diphosphate + DNAn+1 | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| B-family replicative DNA polymerase | - |
Saccharolobus solfataricus |
| DNA polymerase B1 | - |
Saccharolobus solfataricus |
| POlB1 | - |
Saccharolobus solfataricus |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | replicative DNA polymerases use a complex, multistep mechanism for efficient and accurate DNA replication, kinetics and conformational dynamics by single-molecule Förster resonance energy transfer techniques, overview. The replicative polymerase can bind to DNA in at least three conformations, corresponding to an open and closed conformation of the finger domain as well as a conformation with the DNA substrate bound to the exonuclease active site of PolB1. PolB1 can transition between these conformations without dissociating from a primer-template DNA substrate. The closed conformation is promoted by a matched incoming dNTP but not by a mismatched dNTP and that mismatches at the primer-template terminus lead to an increase in the binding of the DNA to the exonuclease site | Saccharolobus solfataricus |
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Release 2023.1 (January 2023)
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