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Literature summary extracted from

  • Shen, Y.; Tang, X.F.; Matsui, I.
    Subunit interaction and regulation of activity through terminal domains of the family D DNA polymerase from Pyrococcus horikoshii (2003), J. Biol. Chem., 278, 21247-21257.
    View publication on PubMed

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
2.7.7.7 additional information deletion of the COOH-terminal zinc finger region (1289–1308) does not abolish the subunit interaction. Instead, while the polymerization of the deletion mutants remains, the 3'-5' exonuclease is completely inactivated. Deletion of DP1Pho(1–200) increases the exonuclease and DNA binding activities of PolDPho. Adding DP1Pho(1–200) to the truncated protein suppresses the elevated exonuclease activity Pyrococcus horikoshii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.7 deoxynucleoside triphosphate + DNAn Pyrococcus horikoshii the enzyme plays an essential role in DNA replication, repair, and recombination diphosphate + DNAn+1
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 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.7 Pyrococcus horikoshii
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.7
-
 Pyrococcus horikoshii

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.7 deoxynucleoside triphosphate + DNAn the enzyme plays an essential role in DNA replication, repair, and recombination Pyrococcus horikoshii diphosphate + DNAn+1
-
 ?
2.7.7.7 deoxynucleoside triphosphate + DNAn the carboxyl-terminal (1255–1332) of the large subunit (DP2Pho) and two regions, the 201–260 and 599–622, of the small subunit (DP1Pho) are critical for the complex formation, and probable subunit interaction of PolDPho. The amino-terminal (1–300) of DP2Pho is essential for the folding of PolDPho and is likely the oligomerization domain of PolDPho Pyrococcus horikoshii diphosphate + DNAn+1
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.7.7 PolDPho
-
 Pyrococcus horikoshii

General Information

EC Number General Information Comment Organism
2.7.7.7 physiological function the enzyme plays an essential role in DNA replication, repair, and recombination Pyrococcus horikoshii