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Inverting hydrolases and their use in enantioconvergent biotransformations
Owing to the more abundant occurrence of racemic compounds compared to prochiral or meso forms, most enantiomerically pure products are obtained via racemate resolution. This review summarizes (chemo)enzymatic enantioconvergent processes based on the use of hydrolytic enzymes, which are able to inve...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Elsevier Science Publishers
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3725421/ https://www.ncbi.nlm.nih.gov/pubmed/23809848 http://dx.doi.org/10.1016/j.tibtech.2013.05.005 |
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author | Schober, Markus Faber, Kurt |
author_facet | Schober, Markus Faber, Kurt |
author_sort | Schober, Markus |
collection | PubMed |
description | Owing to the more abundant occurrence of racemic compounds compared to prochiral or meso forms, most enantiomerically pure products are obtained via racemate resolution. This review summarizes (chemo)enzymatic enantioconvergent processes based on the use of hydrolytic enzymes, which are able to invert a stereocenter during catalysis that can overcome the 50%-yield limitation of kinetic resolution. Recent developments are presented in the fields of inverting or retaining sulfatases, epoxide hydrolases and dehalogenases, which allow the production of secondary alcohols or vicinal diols at a 100% theoretical yield from a racemate via enantioconvergent processes. |
format | Online Article Text |
id | pubmed-3725421 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Elsevier Science Publishers |
record_format | MEDLINE/PubMed |
spelling | pubmed-37254212013-08-01 Inverting hydrolases and their use in enantioconvergent biotransformations Schober, Markus Faber, Kurt Trends Biotechnol Review Owing to the more abundant occurrence of racemic compounds compared to prochiral or meso forms, most enantiomerically pure products are obtained via racemate resolution. This review summarizes (chemo)enzymatic enantioconvergent processes based on the use of hydrolytic enzymes, which are able to invert a stereocenter during catalysis that can overcome the 50%-yield limitation of kinetic resolution. Recent developments are presented in the fields of inverting or retaining sulfatases, epoxide hydrolases and dehalogenases, which allow the production of secondary alcohols or vicinal diols at a 100% theoretical yield from a racemate via enantioconvergent processes. Elsevier Science Publishers 2013-08 /pmc/articles/PMC3725421/ /pubmed/23809848 http://dx.doi.org/10.1016/j.tibtech.2013.05.005 Text en © 2013 Elsevier Ltd. https://creativecommons.org/licenses/by/4.0/This work is licensed under a Creative Commons Attribution 4.0 International License (https://creativecommons.org/licenses/by/4.0/) , which allows reusers to distribute, remix, adapt, and build upon the material in any medium or format, so long as attribution is given to the creator. The license allows for commercial use. |
spellingShingle | Review Schober, Markus Faber, Kurt Inverting hydrolases and their use in enantioconvergent biotransformations |
title | Inverting hydrolases and their use in enantioconvergent biotransformations |
title_full | Inverting hydrolases and their use in enantioconvergent biotransformations |
title_fullStr | Inverting hydrolases and their use in enantioconvergent biotransformations |
title_full_unstemmed | Inverting hydrolases and their use in enantioconvergent biotransformations |
title_short | Inverting hydrolases and their use in enantioconvergent biotransformations |
title_sort | inverting hydrolases and their use in enantioconvergent biotransformations |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3725421/ https://www.ncbi.nlm.nih.gov/pubmed/23809848 http://dx.doi.org/10.1016/j.tibtech.2013.05.005 |
work_keys_str_mv | AT schobermarkus invertinghydrolasesandtheiruseinenantioconvergentbiotransformations AT faberkurt invertinghydrolasesandtheiruseinenantioconvergentbiotransformations |