Issue 9, 1992

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 [(kcat/km)R/(kcat/km)s] of the reaction of SADH with (R)- and (S)-butan-2-ol increase with the coenzyme analogues.

Article information

Article type
Paper

J. Chem. Soc., Perkin Trans. 1, 1992, 1083-1084

Effect of coenzyme analogues on enantioselectivity of alcohol dehydrogenase

C. Zheng and R. S. Phillips, J. Chem. Soc., Perkin Trans. 1, 1992, 1083 DOI: 10.1039/P19920001083

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