The potential of quinoprotein alcohol dehydrogenase from thermotolerant acetobacter in biocatalysis

Corrigendum to: The enantioselectivity of quinohaemoprotein alcohol dehydrogenases: mechanistic and structural aspects (J. Mol. Catal. B-Enzym. 8 (2000) p. 121-163).

Enzymes involved in the glycidaldehyde (2,3-epoxy-propanal) oxidation step in the kinetic resolution of racemic glycidol (2,3-epoxy-1-propanol) by Acetobacter pasteurianus.