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

@article{Engel2004SubstrateRO,
  title={Substrate range of acetohydroxy acid synthase I from Escherichia coli in the stereoselective synthesis of alpha-hydroxy ketones.},
  author={Stanislav Engel and Maria Vyazmensky and Dvora Berkovich and Ze'ev Barak and David M. Chipman},
  journal={Biotechnology and bioengineering},
  year={2004},
  volume={88 7},
  pages={825-31}
}
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… CONTINUE READING

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