Asymmetric bioreduction of activated C = C bonds using Zymomonas mobilis NCR enoate reductase and old yellow enzymes OYE 1-3 from yeasts

摘要

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 (EIZ) geometry of the alkene or by choice of the appropriate enzyme. This substrate- or enzyme-based stereocontrol allowed access to the opposite enantiomeric products.