The alcohol dehydrogenase from Lactobacillus kefir simultaneously catalyzes carbonyl reductions and NADPH regeneration in the presence of 2-propanol. Representative synthesis of a number of chiral alcohols was accomplished in good yield and high enantiomeric excess (94-99%). This NADPH-requiring enzyme transfers the pro-R hydride from the cofactor to the si face of carbonyls to give (R) alcohols. The enzyme exhibits a very broad substrate specificity and high enantioselectivity for the synthesis of chiral aromatic, cyclic, polycyclic, and aliphatic alcohols.