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Literature summary for 2.7.7.49 extracted from

  • Jozwiakowski, S.; Connolly, B.
    A modified family-B archaeal DNA polymerase with reverse transcriptase activity (2011), ChemBioChem, 12, 35-37.
    View publication on PubMed

Protein Variants

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/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
deoxynucleoside triphosphate + DNAn Thermococcus gorgonarius
-
diphosphate + DNAn+1
-
?

Organism

Organism UniProt Comment Textmining
Thermococcus gorgonarius
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
deoxynucleoside triphosphate + DNAn
-
Thermococcus gorgonarius diphosphate + DNAn+1
-
?

Synonyms

Synonyms Comment Organism
reverse transcriptase
-
Thermococcus gorgonarius
Tgo-Pol
-
Thermococcus gorgonarius

General Information

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