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Literature summary 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)

EC Number Cloned (Comment) Organism
2.7.7.7 expression in Escherichia coli Pyrococcus furiosus
3.1.11.1 expression in Escherichia coli Pyrococcus furiosus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.7 D405A mutant enzyme loses 99.8% of DNA polymerizing activity and 90% of 3'->5' exonucleolytic activity Pyrococcus furiosus
2.7.7.7 D405E mutant enzyme loses 95.8% of DNA polymerizing activity and 90% of 3'->5' exonucleolytic activity Pyrococcus furiosus
2.7.7.7 DELTAH672-S775 mutant enzyme loses 99% of DNA polymerizing activity and 97% of 3'->5' exonucleolytic activity Pyrococcus furiosus
2.7.7.7 DELTAL717-S775 mutant enzyme loses 97% of DNA polymerizing activity and 97% of 3'->5' exonucleolytic activity Pyrococcus furiosus
2.7.7.7 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
3.1.11.1 D405A mutant enzyme loses 99.8% of DNA polymerizing activity and 90% of 3'->5' exonucleolytic activity Pyrococcus furiosus
3.1.11.1 D405E mutant enzyme loses 95.8% of DNA polymerizing activity and 90% of 3'->5' exonucleolytic activity Pyrococcus furiosus
3.1.11.1 DELTAH672-S775 mutant enzyme loses 99% of DNA polymerizing activity and 97% of 3'->5' exonucleolytic activity Pyrococcus furiosus
3.1.11.1 DELTAL717-S775 mutant enzyme loses 97% of DNA polymerizing activity and 97% of 3'->5' exonucleolytic activity Pyrococcus furiosus
3.1.11.1 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

EC Number Organism UniProt Comment Textmining
2.7.7.7 Pyrococcus furiosus
-
-
-
3.1.11.1 Pyrococcus furiosus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.7
-
 Pyrococcus furiosus
3.1.11.1
-
 Pyrococcus furiosus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.7 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
-
 ?
3.1.11.1 single-stranded oligodeoxyribonucleotide + H2O 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 single-stranded oligodeoxyribonucleotide + nucleoside 5'-monophosphate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.7.7 DNA polymerase I
-
 Pyrococcus furiosus
2.7.7.7 Pol BI
-
 Pyrococcus furiosus
3.1.11.1 DNA polymerase I
-
 Pyrococcus furiosus
3.1.11.1 Pol BI
-
 Pyrococcus furiosus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.11.1 74
-
 assay at Pyrococcus furiosus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.11.1 8
-
 assay at Pyrococcus furiosus