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Literature summary for 4.1.1.7 extracted from

  • Bruning, M.; Berheide, M.; Meyer, D.; Golbik, R.; Bartunik, H.; Liese, A.; Tittmann, K.
    Structural and kinetic studies on native intermediates and an intermediate analogue in benzoylformate decarboxylase reveal a least motion mechanism with an unprecedented short-lived predecarboxylation intermediate (2009), Biochemistry, 48, 3258-3268.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting drop vapor diffusion method, using 25% (w/v) polyethylene glycol 2000 and 0.2 M MgCl2, at pH 6. Pseudomonas putida

Inhibitors

Inhibitors Comment Organism Structure
(R)-mandelate
-
Pseudomonas putida
methyl benzoylphosphonate
-
Pseudomonas putida

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.15
-
p-nitro-benzoylformate at 25°C Pseudomonas putida
0.23
-
benzoylformate in 50 mM potassium phosphate buffer, pH 6.5, at 30°C Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Pseudomonas putida P20906
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pseudomonas putida

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzoylformate
-
Pseudomonas putida benzaldehyde + CO2
-
?
benzylformate
-
Pseudomonas putida benzaldehyde + CO2
-
?
p-nitro-benzoylformate very poor substrate Pseudomonas putida ?
-
?

Subunits

Subunits Comment Organism
homotetramer x-ray crystallography Pseudomonas putida

Synonyms

Synonyms Comment Organism
BFD
-
Pseudomonas putida

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.05
-
p-nitro-benzoylformate at 25°C Pseudomonas putida
426
-
benzoylformate at 30°C, in 50 mM potassium phosphate buffer, pH 6.5 Pseudomonas putida

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate
-
Pseudomonas putida