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Literature summary for 4.1.2.38 extracted from

  • Brandt, G.S.; Kneen, M.M.; Petsko, G.A.; Ringe, D.; McLeish, M.J.
    Active-site engineering of benzaldehyde lyase shows that a point mutation can confer both new reactivity and susceptibility to mechanism-based inhibition (2010), J. Am. Chem. Soc., 132, 438-439.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
cocrystallization of mutant A28S with inhibitors methyl benzoylphosphonate and benzoylphosphonate. The introduced serine residue of the mutant is phosphorylated by benzoylphosphonate Pseudomonas fluorescens

Protein Variants

Protein Variants Comment Organism
A28S point mutation converts BAL into a true benzoylformate decarboxylase. Km value for (R)-benzoin is virtually identical to that of the wild-type enzyme but whose kcat value is reduced ca. 10fold. Can decarboxylate benzoylformate, has a substrate spectrum comparable to that of benzoylformate decarboxylase, albeit with reduced activity. Methyl benzoylphosphonate and benzoylphosphonate act as competitive inhibitors in a time- and concentration-dependent manner Pseudomonas fluorescens

Organism

Organism UniProt Comment Textmining
Pseudomonas fluorescens
-
biovar I
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(R)-benzoin
-
Pseudomonas fluorescens benzaldehyde + benzaldehyde
-
?
Benzoylformate
-
Pseudomonas fluorescens ?
-
?
methyl benzoylphosphonate
-
Pseudomonas fluorescens ?
-
?
additional information shows no reaction with benzoylphosphonate Pseudomonas fluorescens ?
-
?

Synonyms

Synonyms Comment Organism
BAL
-
Pseudomonas fluorescens
benzaldehyde lyase
-
Pseudomonas fluorescens

Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate
-
Pseudomonas fluorescens