From Wikipedia, the free encyclopedia
In enzymology, an acetolactate decarboxylase (EC 220.127.116.11) is an enzyme that catalyzes the chemical reaction
- (S)-2-hydroxy-2-methyl-3-oxobutanoate (R)-2-acetoin + CO2
Hence, this enzyme has one substrate, (S)-2-hydroxy-2-methyl-3-oxobutanoate, and two products, (R)-2-acetoin 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 (S)-2-hydroxy-2-methyl-3-oxobutanoate carboxy-lyase [(R)-2-acetoin-forming]. Other names in common use include alpha-acetolactate decarboxylase, and (S)-2-hydroxy-2-methyl-3-oxobutanoate carboxy-lyase. This enzyme participates in butanoate metabolism and c5-branched dibasic acid metabolism.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1XV2.
- Hill RK, Sawada S and Arfin SM (1979). [Expression error: Missing operand for > "Stereochemistry of valine and isoleucine biosynthesis. IV Synthesis, configuration, and enzymatic specificity of alpha-acetolactate and alpha-aceto-alpha-hydroxybutyrate"]. Bioorg. Chem. 8: 175–189. doi:10.1016/0045-2068(79)90003-8.
- Stormer FC (1967). [Expression error: Missing operand for > "Isolation of crystalline pH 6 acetolactate-forming enzyme from Aerobacter aerogenes"]. J. Biol. Chem. 242: 1756–9. PMID 6024768.