The Michael hydratase - alcohol dehydrogenase (MhyADH) from Alicycliphilus denitrificans was previously identified as a bi-functional enzyme performing a hydration of ci,(3-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. © 2014 Resch et al.; licensee Springer.
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Resch, V., Jin, J., Chen, B. S., & Hanefeld, U. (2014). Michael hydratase alcohol dehydrogenase or just alcohol dehydrogenase? AMB Express, 4(1), 1–7. https://doi.org/10.1186/s13568-014-0030-2