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Literature summary for 2.7.7.7 extracted from

  • Truniger, V.; Lazaro, J.M.; Salas, M.; Blanco, L.
    phi29 DNA polymerase requires the N-terminal domain to bind terminal protein and DNA primer substrates (1998), J. Mol. Biol., 278, 741-755.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
truncated enzyme Salasvirus phi29

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+
-
Salasvirus phi29

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
44000
-
C-terminal fragment, SDS-PAGE 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 44kDa C-terminal fragment has no exonuclease activity, reduced efficiency with Mn2+ and reduced capacity to initiate terminal protein-primed DNA replication Salasvirus phi29 diphosphate + DNAn+1
-
?