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Literature summary for 2.3.1.8 extracted from

  • Hibbert, F.; Kyrtopoulos, S.A.; Satchell, D.P.N.
    Kinetic studies with phosphotransacetylase (1971), Biochim. Biophys. Acta, 242, 39-54.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
p-chloromercuribenzoate
-
Clostridium kluyveri

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic studies Clostridium kluyveri

Metals/Ions

Metals/Ions Comment Organism Structure
K+
-
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
-
-
-

Reaction

Reaction Comment Organism Reaction ID
acetyl-CoA + phosphate = CoA + acetyl phosphate reaction mechanism Clostridium kluyveri

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
Clostridium kluyveri
-

Substrates and Products (Substrate)

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