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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 ?,?-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.

SUBMITTER: Resch V

PROVIDER: S-EPMC4052635 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

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Michael hydratase alcohol dehydrogenase or just alcohol dehydrogenase?

Resch Verena V Jin Jianfeng J Chen Bi-Shuang BS Hanefeld Ulf U

AMB Express 20140315

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 ...[more]

PMID: 24949265

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