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Literature summary for 2.3.1.8 extracted from

  • Henkin, J.; Abeles, R.H.
    Evidence against an acyl-enzyme intermediate in the reaction catalyzed by clostridial phosphotransacetylase (1976), Biochemistry, 15, 3472-3479.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
5,5'-dithiobis(2-nitrobenzoic acid)
-
Clostridium kluyveri
acetyl-CoA competitive Clostridium kluyveri
arsenate
-
Clostridium kluyveri
coenzyme A competitive Clostridium kluyveri
desulfo-CoA competitive Clostridium kluyveri
diphosphate non competitive Clostridium kluyveri
N-ethylmaleimide
-
Clostridium kluyveri
phosphate competitive with respect to acyl phosphate, non competitive with respect to CoA Clostridium kluyveri

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
70000
-
x * 70000, SDS-PAGE 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
acetyl-CoA + phosphate = CoA + acetyl phosphate evidence against an acyl-enzyme intermediate Clostridium kluyveri

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
? x * 70000, SDS-PAGE Clostridium kluyveri