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Literature summary extracted from

  • Bera, A.K.; Polovnikova, L.S.; Roestamadji, J.; Widlanski, T.S.; Kenyon, G.L.; McLeish, M.J.; Hasson, M.S.
    Mechanism-based inactivation of benzoylformate decarboxylase, a thiamin diphosphate-dependent enzyme (2007), J. Am. Chem. Soc., 129, 4120-4121.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.7 acetylphosphonate
-
 Pseudomonas putida
4.1.1.7 benzoylphosphonate competitive inhibitor Pseudomonas putida
4.1.1.7 methyl acetylphosphonate
-
 Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.7 Pseudomonas putida P20906
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.7 benzoylformate
-
 Pseudomonas putida benzaldehyde + CO2
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.1.1.7 BFD
-
 Pseudomonas putida

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.7 thiamine diphosphate dependent Pseudomonas putida

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.1.1.7 0.36
-
 benzoylphosphonate prolonged incubation of BFD with benzoylphosphonate results in permanent inactivation of the enzyme Pseudomonas putida