Effect of coenzyme analogues on enantioselectivity of alcohol dehydrogenase

Abstract

Secondary alcohol dehydrogenase from Thermoanaerobacter ethanolicus catalyzes the reduction of butan-2-one with much higher enantioselectivity when NADP is replaced by APADP, SNADP or NAD; as expected, the enantiomeric ratios [(k_cat/k_m)_R/(k_cat/k_m)_s] of the reaction of SADH with (R)- and (S)-butan-2-ol increase with the coenzyme analogues.