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Literature summary for 2.7.7.7 extracted from

  • Truniger, V.; Lazaro, J.M.; Salas, M.
    Two positively charged residues of phi29 DNA polymerase, conserved in protein-primed DNA polymerases, are involved in stabilisation of the incoming nucleotide (2004), J. Mol. Biol., 335, 481-494.
    View publication on PubMed
Search for more literature for 2.7.7.7

Protein Variants

Protein Variants Comment Organism
K366T mutant enzyme shows a wild-type like phenotype in DNA-primed polymerisation in the presence of DNA as template, in terminal protein-primed reactions as initiation and transition it is impaired, especially in the presence of the Phi29 DNA-binding protein, protein p6 Salasvirus phi29

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
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 additional information
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 Salasvirus phi29

Organism

Organism UniProt Comment Textmining
Salasvirus phi29
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
deoxynucleoside triphosphate + DNAn Phi29 DNA polymerase belongs to the family B DNA polymerases able to start replication by protein-priming Salasvirus phi29 diphosphate + DNAn+1
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