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Michael hydratase alcohol dehydrogenase or just alcohol dehydrogenase?

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 s...

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Detalles Bibliográficos
Autores principales: Resch, Verena, Jin, Jianfeng, Chen, Bi-Shuang, Hanefeld, Ulf
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4052635/
https://www.ncbi.nlm.nih.gov/pubmed/24949265
http://dx.doi.org/10.1186/s13568-014-0030-2
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author Resch, Verena
Jin, Jianfeng
Chen, Bi-Shuang
Hanefeld, Ulf
author_facet Resch, Verena
Jin, Jianfeng
Chen, Bi-Shuang
Hanefeld, Ulf
author_sort Resch, Verena
collection PubMed
description 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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spelling pubmed-40526352014-06-19 Michael hydratase alcohol dehydrogenase or just alcohol dehydrogenase? Resch, Verena Jin, Jianfeng Chen, Bi-Shuang Hanefeld, Ulf AMB Express Research Paper 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. Springer 2014-03-15 /pmc/articles/PMC4052635/ /pubmed/24949265 http://dx.doi.org/10.1186/s13568-014-0030-2 Text en Copyright © 2014 Resch et al.;licensee Springer http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative CommonsAttribution 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.
spellingShingle Research Paper
Resch, Verena
Jin, Jianfeng
Chen, Bi-Shuang
Hanefeld, Ulf
Michael hydratase alcohol dehydrogenase or just alcohol dehydrogenase?
title Michael hydratase alcohol dehydrogenase or just alcohol dehydrogenase?
title_full Michael hydratase alcohol dehydrogenase or just alcohol dehydrogenase?
title_fullStr Michael hydratase alcohol dehydrogenase or just alcohol dehydrogenase?
title_full_unstemmed Michael hydratase alcohol dehydrogenase or just alcohol dehydrogenase?
title_short Michael hydratase alcohol dehydrogenase or just alcohol dehydrogenase?
title_sort michael hydratase alcohol dehydrogenase or just alcohol dehydrogenase?
topic Research Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4052635/
https://www.ncbi.nlm.nih.gov/pubmed/24949265
http://dx.doi.org/10.1186/s13568-014-0030-2
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