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Literature summary for 4.1.1.7 extracted from

  • Palmen, T.G.; Nieveler, J.; Froelich, B.; Treffenfeldt, W.; Pohl, M.; Buechs, J.
    Physiological relation between respiration activity and heterologous expression of selected benzoylformate decarboxylase variants in Escherichia coli (2010), Microb. Cell Fact., 9, 76.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Escherichia coli SG13009 pKK233-2 Pseudomonas putida

Protein Variants

Protein Variants Comment Organism
H281A mutant with high cofactor binding affinity Pseudomonas putida
L476H mutant with low cofactor binding affinity Pseudomonas putida
L476P mutant with low cofactor binding affinity Pseudomonas putida
L476P/S181T mutant with low cofactor binding affinity Pseudomonas putida
L476Q the mutant has an intermediate cofactor binding strength Pseudomonas putida
S181T mutant with high cofactor binding affinity Pseudomonas putida

General Stability

General Stability Organism
the wild type BFD has about 100% enzyme activity after 24 h incubation in 50 mM KPi-buffer without thiamine diphosphate Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography Pseudomonas putida

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzaldehyde + acetaldehyde
-
Pseudomonas putida 2-hydroxypropiophenone
-
?
benzoylformate
-
Pseudomonas putida benzaldehyde + CO2
-
?

Synonyms

Synonyms Comment Organism
BFD
-
Pseudomonas putida

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate
-
Pseudomonas putida