Protein Variants | Comment | Organism |
---|---|---|
D259E | moderate decrease of the polymerizing activity | Pyrococcus horikoshii |
D259G | moderate decrease of the polymerizing activity | Pyrococcus horikoshii |
D259K | the exonuclease activity of the mutant enzyme decreases drastically to 0.58% compared with that of the wild-type DNA polymerase | Pyrococcus horikoshii |
D259N | moderate decrease of the polymerizing activity | Pyrococcus horikoshii |
K253E | exonuclease activity of mutant increases 2.7fold compared to wild-type activity | Pyrococcus horikoshii |
K253E/R255E | exonuclease activity of mutant increases 1.8fold compared to wild-type activity | Pyrococcus horikoshii |
R255D | exonuclease activity of mutant increases 2.9fold compared to wild-type activity | Pyrococcus horikoshii |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | the negative charge and the side-chain length of D259 might play a supporting role in coordinating the conserved Mg2+ to the correct position at the active center in the exonuclease domain | Pyrococcus horikoshii |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pyrococcus horikoshii | O59610 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Pyrococcus horikoshii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
deoxynucleoside triphosphate + DNAn | the functional motif, K253xRxxxD259 (outside known motifs Exo I, II, and III), that is important not only for exonuclease activity but also for polymerizing activity, confirms functional interdependence between the polymerase and exonuclease domains. The short loop region, K253G254R255, probably contributes to binding to DNA substrates | Pyrococcus horikoshii | diphosphate + DNAn+1 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
DNA polymerase I | - |
Pyrococcus horikoshii |