Michael hydratase alcohol dehydrogenase or just alcohol dehydrogenase?

2Citations
Citations of this article
19Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

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.

Cite

CITATION STYLE

APA

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

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free