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Transaminase‐Catalyzed Racemization with Potential for Dynamic Kinetic Resolutions
Dynamic kinetic resolution (DKR) reactions in which a stereoselective enzyme and a racemization step are coupled in one pot would represent powerful tools for the production of enantiopure amines through enantioconvergence of racemates. The exploitation of DKR strategies is currently hampered by the...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6282829/ https://www.ncbi.nlm.nih.gov/pubmed/30546495 http://dx.doi.org/10.1002/cctc.201801049 |
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author | Ruggieri, Federica van Langen, Luuk M. Logan, Derek T. Walse, Björn Berglund, Per |
author_facet | Ruggieri, Federica van Langen, Luuk M. Logan, Derek T. Walse, Björn Berglund, Per |
author_sort | Ruggieri, Federica |
collection | PubMed |
description | Dynamic kinetic resolution (DKR) reactions in which a stereoselective enzyme and a racemization step are coupled in one pot would represent powerful tools for the production of enantiopure amines through enantioconvergence of racemates. The exploitation of DKR strategies is currently hampered by the lack of effective, enzyme‐compatible and scalable racemization strategies for amines. In the present work, the proof of concept of a fully biocatalytic method for amine racemization is presented. Both enantiomers of the model compound 1‐methyl‐3‐phenylpropylamine could be racemized in water and at room temperature using a couple of wild‐type, non‐proprietary, enantiocomplementary amine transaminases and a minimum amount of pyruvate/alanine as a co‐substrate couple. The biocatalytic simultaneous parallel cascade reaction presented here poses itself as a customizable amine racemization system with potential for the chemical industry in competition with traditional transition‐metal catalysis. |
format | Online Article Text |
id | pubmed-6282829 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-62828292018-12-11 Transaminase‐Catalyzed Racemization with Potential for Dynamic Kinetic Resolutions Ruggieri, Federica van Langen, Luuk M. Logan, Derek T. Walse, Björn Berglund, Per ChemCatChem Full Papers Dynamic kinetic resolution (DKR) reactions in which a stereoselective enzyme and a racemization step are coupled in one pot would represent powerful tools for the production of enantiopure amines through enantioconvergence of racemates. The exploitation of DKR strategies is currently hampered by the lack of effective, enzyme‐compatible and scalable racemization strategies for amines. In the present work, the proof of concept of a fully biocatalytic method for amine racemization is presented. Both enantiomers of the model compound 1‐methyl‐3‐phenylpropylamine could be racemized in water and at room temperature using a couple of wild‐type, non‐proprietary, enantiocomplementary amine transaminases and a minimum amount of pyruvate/alanine as a co‐substrate couple. The biocatalytic simultaneous parallel cascade reaction presented here poses itself as a customizable amine racemization system with potential for the chemical industry in competition with traditional transition‐metal catalysis. John Wiley and Sons Inc. 2018-10-11 2018-11-07 /pmc/articles/PMC6282829/ /pubmed/30546495 http://dx.doi.org/10.1002/cctc.201801049 Text en © 2018 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA. This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes. |
spellingShingle | Full Papers Ruggieri, Federica van Langen, Luuk M. Logan, Derek T. Walse, Björn Berglund, Per Transaminase‐Catalyzed Racemization with Potential for Dynamic Kinetic Resolutions |
title | Transaminase‐Catalyzed Racemization with Potential for Dynamic Kinetic Resolutions |
title_full | Transaminase‐Catalyzed Racemization with Potential for Dynamic Kinetic Resolutions |
title_fullStr | Transaminase‐Catalyzed Racemization with Potential for Dynamic Kinetic Resolutions |
title_full_unstemmed | Transaminase‐Catalyzed Racemization with Potential for Dynamic Kinetic Resolutions |
title_short | Transaminase‐Catalyzed Racemization with Potential for Dynamic Kinetic Resolutions |
title_sort | transaminase‐catalyzed racemization with potential for dynamic kinetic resolutions |
topic | Full Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6282829/ https://www.ncbi.nlm.nih.gov/pubmed/30546495 http://dx.doi.org/10.1002/cctc.201801049 |
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