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Literature summary for 2.7.7.7 extracted from

  • Truniger, V.; Lazaro, J.M.; Esteban, F.J.; Blanco, L.; Salas, M.
    A positively charged residue of Phi29 DNA polymerase, highly conserved in DNA polymerases from families A and B, is involved in binding the incoming nucleotide (2002), Nucleic Acids Res., 30, 1483-1492.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
-
Salasvirus phi29

Protein Variants

Protein Variants Comment Organism
I364Q binds the substrate with less efficiency than wild-type enzyme Salasvirus phi29
I364R unable binding of the substrate to the enzyme Salasvirus phi29
K371T binds the substrate with the same efficiency as wild-type enzyme Salasvirus phi29

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Salasvirus phi29
Mn2+
-
Salasvirus phi29

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
deoxynucleoside triphosphate + DNAn Salasvirus phi29
-
diphosphate + DNAn+1
-
?

Organism

Organism UniProt Comment Textmining
Salasvirus phi29
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
deoxynucleoside triphosphate + DNAn
-
Salasvirus phi29 diphosphate + DNAn+1
-
?
deoxynucleoside triphosphate + DNAn enzyme has two exonuclease 3'--5' degradative activities: an exonuclease activity and an inorganic diphosphate-dependent degradative activity Salasvirus phi29 diphosphate + DNAn+1
-
?