EC 2 - Transferases
EC 2.2 - Transferring aldehyde or ketonic groups
EC 2.2.1 - Transketolases and transaldolases
EC 2.2.1.6 - Acetolactate synthase
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 2.2.1.6
Names
Accepted name:
acetolactate synthase
Other
names:
α-acetohydroxy acid synthetase
α-acetohydroxyacid synthase
α-acetolactate synthase
α-acetolactate synthetase
acetohydroxy acid synthetase
acetohydroxyacid synthase
acetolactate pyruvate-lyase (carboxylating)
acetolactic synthetase
α-acetohydroxyacid synthase
α-acetolactate synthase
α-acetolactate synthetase
acetohydroxy acid synthetase
acetohydroxyacid synthase
acetolactate pyruvate-lyase (carboxylating)
acetolactic synthetase
Systematic name:
pyruvate:pyruvate acetaldehydetransferase (decarboxylating)
Reaction
- 2 pyruvate = 2-acetolactate + CO2
Cofactor
Comments:
This enzyme requires thiamine diphosphate. The reaction shown is in the pathway of biosynthesis of valine; the enzyme can also transfer the acetaldehyde from pyruvate to 2-oxobutanoate, forming 2-ethyl-2-hydroxy-3-oxobutanoate, also known as 2-aceto-2-hydroxybutanoate, a reaction in the biosynthesis of isoleucine.
Links to other databases
Enzymes and pathways:
NC-IUBMB
,
BRENDA
,
DIAGRAM
,
DIAGRAM
,
ExplorEnz
,
ENZYME@ExPASy
,
KEGG
,
MetaCyc
,
UniPathway
Protein domains and families:
PROSITE:PDOC00166
Gene Ontology:
GO:0003984
CAS Registry Number:
9027-45-6
References
-
Control of isoleucine, valine and leucine biosynthesis. II. Endproduct inhibition by valine of acetohydroxy acid synthetase in Salmonella typhimurium.Biochim. Biophys. Acta 92 : 142-149 (1964).
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The pH 6 acetolactate-forming enzyme from Aerobacter aerogenes. Subunit structure.Eur. J. Biochem. 20 : 209-214 (1971). [PMID: 5560406]
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The pH 6 acetolactate-forming enzyme from Aerobacter aerogenes. Molecular properties.Eur. J. Biochem. 10 : 251-260 (1969). [PMID: 5823101]
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Physiological implications of the specificity of acetohydroxy acid synthase isozymes of enteric bacteria.J. Bacteriol. 169 : 3750-3756 (1987). [PMID: 3301814]
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The crystal structures of Klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate.J. Biol. Chem. 279 : 2242-2253 (2004). [PMID: 14557277]
[EC 2.2.1.6 created 1972 as EC 4.1.3.18, transferred 2002 to EC 2.2.1.6]