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Asymmetric Bioreduction of Activated C=C Bonds Using Zymomonas mobilis NCR Enoate Reductase and Old Yellow Enzymes OYE 1–3 from Yeasts

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Abstract

The asymmetric bioreduction of C=C-bonds bearing an electron-withdrawing group, such as an aldehyde, ketone, imide, nitro, carboxylic acid, or ester moiety by a novel enoate reductase from Zymomonas mobilis and Old Yellow Enzymes OYE 1–3 from yeasts furnished the corresponding saturated products in up to >99 % ee. Depending on the substrate type, stereocontrol was achieved by variation of the substrate structure, by switching the (E/Z) geometry of the alkene or by choice of the appropriate enzyme. This substrate- orenzyme-based stereocontrol allowed access to the opposite enantiomeric products.(© Wiley-VCH Verlag GmbH & Co. KGaA, 69451 Weinheim, Germany, 2008)

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