Stereochemical control in diastereoselective reduction of alpha-substituted-beta-ketoesters using a reductase purified from Kluyveromyces marxianus

Abstract

An NADPH-dependent carbonyl reductase that shows (3R)-selective reducing activity for alpha-substituted-beta-ketoesters was purified from Kluyveromyces marxianus and racemic alkyl 2-substituted-3-oxobutanoates were reduced to the corresponding (2S,3R)- or (2R,3R)-2-substituted-3-hydroxybutanoates with enantiomeric purity (>99%) and diastereoselectivity (24 similar to 98%).