The enantioselectivity of quinohaemoprotein alcohol dehydrogenases: Mechanistic and structural aspects.

Characterization of the enantioselective properties of the quinohemoprotein alcohol dehydrogenase of Acetobacter pasteurianus LMB 1635. 1. Different enantiomeric ratios of whole cells and purified enzyme in the kinetic resolution of racemic glycidol

Entropic and enthalpic contributions to the enantioselectivity of quinohaemoprotein alcohol dehydrogenase of Acetobacter pasteurianus and Comamonas testosteroni in the oxidation of primary and secondary alcohols

Enantioselective properties of Acetobacter pasteurianus and its quinprotein alcohol dehydrogenase