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ILVBL  -  ilvB (bacterial acetolactate synthase)-like

Homo sapiens

Synonyms: 209L8, AHAS, Acetolactate synthase-like protein, FLJ39061, ILV2H, ...
 
 
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Disease relevance of ILVBL

  • Acetohydroxyacid synthase I (AHAS I), one of three isozymes in Escherichia coli catalyzing the first common step in the biosynthesis of branched amino acids, is composed of two kinds of subunits [1].
 

High impact information on ILVBL

  • Acetohydroxy acid synthase (AHAS; EC 4.1.3.18) catalyzes the following two parallel, physiologically important reactions: condensation of two molecules of pyruvate to form acetolactate (AL), in the pathway to valine and leucine, and condensation of pyruvate plus 2-ketobutyrate to form acetohydroxybutyrate (AHB), in the pathway to isoleucine [2].
  • Risk for mutated AHAS protein in imidazolinone-tolerant wheat most likely would be low, but there are not sufficient effect and exposure data to adequately characterize risk [3].
  • This information could in principle be used, together with an independent specific assay for AHB, to determine the composition of an AHAS product mixture; it would, however, be less accurate than a simultaneous chromatographic method [4].
  • The activity of AHAS is most frequently analyzed using the Westerfeld method, in which the acetoin formed upon decarboxylation of AL is determined by colorimetric reaction with creatine and alpha-naphthol [4].
  • Based on the crystal structure of AHAS/sulfonylurea complex, we have carried out computational screening of the ACD-3D database in order to look for novel non-sulfonylurea inhibitors of AHAS for the first time [5].

References

  1. Construction of an active acetohydroxyacid synthase I with a flexible linker connecting the catalytic and the regulatory subunits. Vyazmensky, M., Engel, S., Kryukov, O., Berkovich-Berger, D., Kaplun, L. Biochim. Biophys. Acta (2006) [Pubmed]
  2. Physiological implications of the substrate specificities of acetohydroxy acid synthases from varied organisms. Gollop, N., Damri, B., Chipman, D.M., Barak, Z. J. Bacteriol. (1990) [Pubmed]
  3. A comparative risk assessment of genetically engineered, mutagenic, and conventional wheat production systems. Peterson, R.K., Shama, L.M. Transgenic Res. (2005) [Pubmed]
  4. Determination of products of acetohydroxy acid synthase by the colorimetric method, revisited. Epelbaum, S., Chipman, D.M., Barak, Z. Anal. Biochem. (1990) [Pubmed]
  5. Identification of some novel AHAS inhibitors via molecular docking and virtual screening approach. Wang, J.G., Xiao, Y.J., Li, Y.H., Ma, Y., Li, Z.M. Bioorg. Med. Chem. (2007) [Pubmed]
 
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