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Literature summary 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)

EC Number Crystallization (Comment) Organism
4.1.2.38 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

EC Number Protein Variants Comment Organism
4.1.2.38 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

EC Number Organism UniProt Comment Textmining
4.1.2.38 Pseudomonas fluorescens
-
 biovar I
-

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
4.1.2.38 BAL
-
 Pseudomonas fluorescens
4.1.2.38 benzaldehyde lyase
-
 Pseudomonas fluorescens

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.2.38 thiamine diphosphate
-
 Pseudomonas fluorescens