Michael hydratase alcohol dehydrogenase or just alcohol dehydrogenase?

Title

Michael hydratase alcohol dehydrogenase or just alcohol dehydrogenase?

 Author

Resch, V.A.
Jin, J.
Chen, B.S.
Hanefeld, U.

Faculty

Applied Sciences

 Department

BT/Biotechnology

 Date

2014-03-15

 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.

 Subject

Michael addition
?,?-Unsaturated carbonyl compounds
hydratase
alcohol dehydrogenase
OA-Fund TU Delft

 To reference this document use:

http://resolver.tudelft.nl/uuid:6a0febc0-9e21-4ade-be37-9aaa05fd4da8

 DOI

https://doi.org/10.1186/s13568-014-0030-2

 Publisher

SpringerOpen

 ISSN

2191-0855

 Source

http://www.amb-express.com/content/4/1/30

 Source

AMB Express, 4, 2014

 Part of collection

Institutional Repository

 Document type

journal article

 Rights

© 2014 The Author(s); licensee Springer
This is an Open Access article distributed under the terms of the Creative Commons
Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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