title: Michael hydratase alcohol dehydrogenase or just alcohol dehydrogenase?
abstract: The Michael hydratase - alcohol dehydrogenase (MhyADH) from Alicycliphilus denitrificans was previously identified as a bi-functional enzyme performing a hydration of α,β-unsaturated ketones and subsequent oxidation of the formed alcohols. The investigations of the bi-functionality were based on a spectrophotometric assay and an activity staining in a native gel of the dehydrogenase. New insights in the recently discovered organocatalytic Michael addition of water led to the conclusion that the previously performed experiments to identify MhyADH as a bi-functional enzyme and their results need to be reconsidered and the reliability of the methodology used needs to be critically evaluated.
authors.affiliation: Biocatalysis, Department of Biotechnology, Delft University of Technology, Julianalaan 136, Delft, 2628 BL, The Netherlands.
authors.forename: Verena
authors.initials: V
authors.lastname: Resch
authors.affiliation: Biocatalysis, Department of Biotechnology, Delft University of Technology, Julianalaan 136, Delft, 2628 BL, The Netherlands.
authors.forename: Jianfeng
authors.initials: J
authors.lastname: Jin
authors.affiliation: Biocatalysis, Department of Biotechnology, Delft University of Technology, Julianalaan 136, Delft, 2628 BL, The Netherlands.
authors.forename: Bi-Shuang
authors.initials: BS
authors.lastname: Chen
authors.affiliation: Biocatalysis, Department of Biotechnology, Delft University of Technology, Julianalaan 136, Delft, 2628 BL, The Netherlands.
authors.forename: Ulf
authors.initials: U
authors.lastname: Hanefeld
keywords: Alcohol dehydrogenase; Hydratase; Michael addition; α,β-Unsaturated carbonyl compounds