Substrate range of acetohydroxy acid synthase I from Escherichia coli in the stereoselective synthesis of α-hydroxy ketones

Stanislav Engel, Maria Vyazmensky, Dvora Berkovich, Ze'ev Barak, David M. Chipman

Research output: Contribution to journalArticlepeer-review

25 Scopus citations


Acetohydroxy acid synthase I appears to be the most effective of the AHAS isozymes found in Escherichia coli in the chiral synthesis of phenylacetyl carbinol from pyruvate and benzaldehyde. We report here the exploration of a range of aldehydes as substrates for AHAS I and demonstrate that the enzyme can accept a wide variety of substituted benzaldehydes, as well as heterocyclic and heteroatomic aromatic aldehydes, to produce chiral carbinols. The active site of AHAS I does not appear to impose serious steric constraints on the acceptor substrate. The influence of electronic effects on the reaction has been probed using substituted benzaldehydes as substrates. The electrophilicity of the aldehyde acceptor substrates is most important to their reactivity, but the lipophilicity of substituents also affects their reactivity. AHAS I is an effective biosynthetic platform for production of a variety of α-hydroxy ketones, compounds with considerable potential as pharmacological precursors.

Original languageEnglish
Pages (from-to)825-831
Number of pages7
JournalBiotechnology and Bioengineering
Issue number7
StatePublished - 30 Dec 2004


  • Acetolactate synthase
  • Aromatic aldehydes
  • Chiral synthon
  • Pyruvate
  • Quantitative structure-activity relationship
  • Thiamine diphosphate


Dive into the research topics of 'Substrate range of acetohydroxy acid synthase I from <i>Escherichia coli </i>in the stereoselective synthesis of α-hydroxy ketones'. Together they form a unique fingerprint.

Cite this