Protein Variants | Comment | Organism |
---|---|---|
D215A | enzyme mutant devoid of 3'-5' exonuclease activity | Thermococcus gorgonarius |
additional information | Z derivatives have the fingers domain of Tgo-Pol replaced with that from Pol zeta, insertion of the Pol zeta finger domains into the Thermococcus gorgonarius Tgo-Pol resulting in the Z derivatives increase the enzyme activity. Z1 shows increased activity, which is further increased with Z2, created by fusion of Z1 with the processivity-increasing DNA binding protein Sso7d, overview | Thermococcus gorgonarius |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
deoxynucleoside triphosphate + DNAn | Thermococcus gorgonarius | - |
diphosphate + DNAn+1 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Thermococcus gorgonarius | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
deoxynucleoside triphosphate + DNAn | - |
Thermococcus gorgonarius | diphosphate + DNAn+1 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
reverse transcriptase | - |
Thermococcus gorgonarius |
Tgo-Pol | - |
Thermococcus gorgonarius |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the family B polymerases | Thermococcus gorgonarius |
malfunction | mutations in a loop in the fingers domain leads to a decrease accuracy of the arhcaeal enzyme | Thermococcus gorgonarius |
additional information | in family B polymerases, the fingers domain interacts with dNTPs and undergoes a catalytically essential conformational change that depends on correct pairing of the dNTP with its templating base | Thermococcus gorgonarius |