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Updated: Apr 27, 2026

Preparation of SNS CobaltII Pincer Model Complexes of Liver Alcohol Dehydrogenase
Published on: March 19, 2020
Michael hydratase alcohol dehydrogenase or just alcohol dehydrogenase?
Verena Resch1, Jianfeng Jin1, Bi-Shuang Chen1
1Biocatalysis, Department of Biotechnology, Delft University of Technology, Julianalaan 136, Delft, 2628 BL, The Netherlands.
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.
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