| acetolactate decarboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 4.1.1.5 | ||||||||
| CAS no. | 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 / QuickGO | ||||||||
| |||||||||
The enzyme acetolactate decarboxylase (EC 4.1.1.5) 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.[1]
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, 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.