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Literature summary for 2.3.1.54 extracted from

  • Ulissi-DeMario, L.; Brush, E.J.; Kozarich, J.W.
    Mechanism-based inactivation of pyruvate formate-lyase reaction in Clostridiae (1991), J. Am. Chem. Soc., 113, 4341-4342.
No PubMed abstract available

Inhibitors

Inhibitors Comment Organism Structure
Acetylphosphinate mechanism-based inactivator Escherichia coli
hypophosphite
-
Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
170000
-
-
Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pyruvate + CoA Escherichia coli
-
acetyl-CoA + formate
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Oxidation Stability

Oxidation Stability Organism
obligate anaerobic enzyme, enzymatic conversion by a unique homolytic mechanism that involves a free radical harbored in the protein structure, protein based organic free radical is essential for catalysis, oxygen destruction of the protein radical Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate + CoA
-
Escherichia coli acetyl-CoA + formate
-
?

Subunits

Subunits Comment Organism
dimer
-
Escherichia coli

Synonyms

Synonyms Comment Organism
PFL
-
Escherichia coli