Category:Complex:acetolactate synthase III

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Comments (originally from EcoCyc[1][2]) Acetohydroxy acid synthase III (AHAS III) is one of two functional isozymes catalyzing the decarboxylation of pyruvate and transfer of the resulting acetaldehyde group to either pyruvate or α-ketobutyrate, producing α-acetolactate for the valine pathway and α-aceto-α-hydroxybutyrate for the isoleucine pathway. This is the first common step in the biosynthesis of the branched-chain amino acids isoleucine, leucine, and valine. A third isozyme, AHAS II, is not functional in E. coli K-12 due to the presence of a frame shift mutation in the gene encoding the large subunit, ilvG. [3][4][4][5].


References

  1. EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  2. EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. Barak, Z et al. (1987) Physiological implications of the specificity of acetohydroxy acid synthase isozymes of enteric bacteria. J. Bacteriol. 169 3750-6 PubMed
  4. 4.0 4.1 Gollop, N et al. (1989) Kinetics and mechanism of acetohydroxy acid synthase isozyme III from Escherichia coli. Biochemistry 28 6310-7 PubMed
  5. Gollop, N et al. (1983) Inhibition of acetohydroxy acid synthase by leucine. Biochim. Biophys. Acta 748 34-9 PubMed

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