Acetolactate decarboxylase
| acetolactate decarboxylase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| EC number | 4.1.1.5 | ||||||
| CAS number | 9025-02-9 | ||||||
| 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 / EGO | ||||||
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In enzymology, an acetolactate decarboxylase (EC 4.1.1.5) 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.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1XV2.
References
- Hill RK, Sawada S and Arfin SM (1979). "Stereochemistry of valine and isoleucine biosynthesis. IV Synthesis, configuration, and enzymatic specificity of alpha-acetolactate and alpha-aceto-alpha-hydroxybutyrate". Bioorg. Chem. 8 (2): 175–189. doi:10.1016/0045-2068(79)90003-8.
- Stormer FC (1967). "Isolation of crystalline pH 6 acetolactate-forming enzyme from Aerobacter aerogenes". J. Biol. Chem. 242 (8): 1756–9. PMID 6024768.