acetolactate decarboxylase
Identifiers
EC no.4.1.1.5
CAS no.9025-02-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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

  1. 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.


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