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Literature summary for 2.7.7.7 extracted from

  • Komori, K.; Ishino, Y.
    Functional interdependence of DNA polymerizing and 3-->5 exonucleolytic activities in Pyrococcus furiosus DNA polymerase I (2000), Protein Eng., 13, 41-47.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pyrococcus furiosus

Protein Variants

Protein Variants Comment Organism
D405A mutant enzyme loses 99.8% of DNA polymerizing activity and 90% of 3'->5' exonucleolytic activity Pyrococcus furiosus
D405E mutant enzyme loses 95.8% of DNA polymerizing activity and 90% of 3'->5' exonucleolytic activity Pyrococcus furiosus
DELTAH672-S775 mutant enzyme loses 99% of DNA polymerizing activity and 97% of 3'->5' exonucleolytic activity Pyrococcus furiosus
DELTAL717-S775 mutant enzyme loses 97% of DNA polymerizing activity and 97% of 3'->5' exonucleolytic activity Pyrococcus furiosus
DELTAL746-S775 mutant protein has DNA polymerizing activity with 2.3fold higher specific activity than that of the wild-type but retains only 10% of the 3'->5' exonucleolytic activity of the wild-type Pyrococcus furiosus

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pyrococcus furiosus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
deoxynucleoside triphosphate + DNAn measurement of the incorporation of methyl-TTP into acid insoluble material. The single-stranded DNA substrate is more sensitive than the double stranded substrate. The polymerase and exonuclease domains in the family B DNA polymerases are functionally interdependent Pyrococcus furiosus diphosphate + DNAn+1
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Synonyms

Synonyms Comment Organism
DNA polymerase I
-
Pyrococcus furiosus
Pol BI
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Pyrococcus furiosus