Biology:Benzoylformate decarboxylase
benzoylformate decarboxylase | |||||||||
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![]() Benzoylformate decarboxlyase tetramer, Pseudomonas putida | |||||||||
Identifiers | |||||||||
EC number | 4.1.1.7 | ||||||||
CAS number | 9025-00-7 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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The enzyme benzoylformate decarboxylase (EC 4.1.1.7) catalyzes the following chemical reaction:
- benzoylformate + H+ [math]\displaystyle{ \rightleftharpoons }[/math] benzaldehyde + CO2
Hence, this enzyme has one substrate, benzoylformate, and two products, benzaldehyde and CO2.
This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is benzoylformate carboxy-lyase (benzaldehyde-forming). Other names in common use include phenylglyoxylate decarboxylase, and benzoylformate carboxy-lyase. This enzyme participates in benzoate degradation via hydroxylation and toluene and xylene degradation. It employs one cofactor, thiamin diphosphate.
Structural studies
As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1BFD, 1MCZ, 1PI3, 1PO7, 1Q6Z, 1YNO, 2FN3, and 2FWN.
References
- "The enzymatic conversion of mandelic acid to benzoic acid. III Fractionation and properties of the soluble enzymes". J. Bacteriol. 66 (5): 548–53. 1953. doi:10.1128/JB.66.5.548-553.1953. PMID 13108854.
![]() | Original source: https://en.wikipedia.org/wiki/Benzoylformate decarboxylase.
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