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Literature summary 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

EC Number Inhibitors Comment Organism Structure
2.3.1.8 5,5'-dithiobis(2-nitrobenzoic acid)
-
Clostridium kluyveri
2.3.1.8 acetyl-CoA competitive Clostridium kluyveri
2.3.1.8 arsenate
-
Clostridium kluyveri
2.3.1.8 coenzyme A competitive Clostridium kluyveri
2.3.1.8 desulfo-CoA competitive Clostridium kluyveri
2.3.1.8 diphosphate non competitive Clostridium kluyveri
2.3.1.8 N-ethylmaleimide
-
Clostridium kluyveri
2.3.1.8 phosphate competitive with respect to acyl phosphate, non competitive with respect to CoA Clostridium kluyveri

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.8 70000
-
x * 70000, SDS-PAGE Clostridium kluyveri

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.8 Clostridium kluyveri
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.3.1.8 acetyl-CoA + phosphate = CoA + acetyl phosphate reaction mechanism Clostridium kluyveri
2.3.1.8 acetyl-CoA + phosphate = CoA + acetyl phosphate evidence against an acyl-enzyme intermediate Clostridium kluyveri

Substrates and Products (Substrate)

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

Subunits

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