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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...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer
2014
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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. |
format | Online Article Text |
id | pubmed-4052635 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | Springer |
record_format | MEDLINE/PubMed |
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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