EC 2.2.1.6 - Acetolactate synthase

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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
Systematic name:
pyruvate:pyruvate acetaldehydetransferase (decarboxylating)

Reactions

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
Structural data: CSA , EC2PDB
Gene Ontology: GO:0003984
CAS Registry Number: 9027-45-6
UniProtKB/Swiss-Prot: (79) [show] [UniProt]

References

  1. Bauerle, R.H., Freundlich, M., Størmer, F.C. and Umbarger, H.E.
    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).
  2. Huseby, N.E., Christensen, T.B., Olsen, B.R. and Størmer, F.C.
    The pH 6 acetolactate-forming enzyme from Aerobacter aerogenes. Subunit structure.
    Eur. J. Biochem. 20: 209-214 (1971). [PMID: 5560406]
  3. Størmer, F.C., Solberg, Y. and Hovig, T.
    The pH 6 acetolactate-forming enzyme from Aerobacter aerogenes. Molecular properties.
    Eur. J. Biochem. 10: 251-260 (1969). [PMID: 5823101]
  4. Barak, Z., Chipman, D.M. and Gollop, N.
    Physiological implications of the specificity of acetohydroxy acid synthase isozymes of enteric bacteria.
    J. Bacteriol. 169: 3750-3756 (1987). [PMID: 3301814]
  5. Pang, S. S., Duggleby, R. G., Schowen, R. L., Guddat, L. W.
    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]