An NADPH-dependent reductase that shows reducing activity for 1-chloro-2-hexanone has been purified from bakers' yeast. SDS−PAGE and gel filtration suggested that the purified reductase is a monomeric enzyme with a molecular weight of ca. 37 kDa. Asymmetric reduction of several carbonyl compounds using the purified reductase has been carried out. 1-Chloro-2-hexanone, 1-acetoxy-2-heptanone, methyl acetoacetate, ethyl pyruvate, 1-chloro-2,4-pentanedione, and 2,4-hexanedione were reduced to the corresponding alcohols with high enantiomeric purities (>98% ee). The reductase showed high specificity constants (k cat/K m = 103−105 s-1 M-1) and relatively low Michaelis constants (K m = 10-4−10-3 M) for all the substrates examined.

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