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Literature summary for 2.3.1.8 extracted from

  • Kyrtopoulos, S.A.; Satchell, D.P.N.
    Kinetic studies with phosphotransacetylase. V. The mechanism of activation by univalent cations (1973), Biochim. Biophys. Acta, 321, 126-142.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Na+ acts as inhibitor in the presence of NH4+ or K+, competitive inhibition Clostridium kluyveri

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information effects of monovalent kations Clostridium kluyveri

Metals/Ions

Metals/Ions Comment Organism Structure
K+ enzyme is activated by low concentrations of NH4+, K+ and Na+, sequence of effectiveness: NH4+, K+, Na+ Clostridium kluyveri
additional information mechanism of activation by univalent cations Clostridium kluyveri
Na+ less effective than NH4+ and K+ Clostridium kluyveri
NH4+ enzyme is activated by low concentrations of NH4+, K+ and Na+, sequence of effectiveness: NH4+, K+, Na+ Clostridium kluyveri

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + phosphate Clostridium kluyveri
-
CoA + acetyl phosphate
-
r

Organism

Organism UniProt Comment Textmining
Clostridium kluyveri
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + phosphate
-
Clostridium kluyveri CoA + acetyl phosphate
-
r