Transaminase-Catalyzed Racemization with Potential for Dynamic Kinetic Resolutions
(2018) In ChemCatChem 10(21). p.5012-5018- Abstract
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... (More)
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.
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- author
- Ruggieri, Federica ; van Langen, Luuk M. ; Logan, Derek T. LU ; Walse, Björn LU and Berglund, Per
- publishing date
- 2018-11-07
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Chiral amines, Enzyme catalysis, Racemization, Transaminase
- in
- ChemCatChem
- volume
- 10
- issue
- 21
- pages
- 7 pages
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- scopus:85054710134
- ISSN
- 1867-3880
- DOI
- 10.1002/cctc.201801049
- language
- English
- LU publication?
- no
- additional info
- Publisher Copyright: © 2018 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.
- id
- c1aaa065-1f36-4872-b69c-35b040b01a45
- date added to LUP
- 2022-04-08 08:55:40
- date last changed
- 2022-04-11 12:14:48
@article{c1aaa065-1f36-4872-b69c-35b040b01a45, abstract = {{<p>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.</p>}}, author = {{Ruggieri, Federica and van Langen, Luuk M. and Logan, Derek T. and Walse, Björn and Berglund, Per}}, issn = {{1867-3880}}, keywords = {{Chiral amines; Enzyme catalysis; Racemization; Transaminase}}, language = {{eng}}, month = {{11}}, number = {{21}}, pages = {{5012--5018}}, publisher = {{John Wiley & Sons Inc.}}, series = {{ChemCatChem}}, title = {{Transaminase-Catalyzed Racemization with Potential for Dynamic Kinetic Resolutions}}, url = {{http://dx.doi.org/10.1002/cctc.201801049}}, doi = {{10.1002/cctc.201801049}}, volume = {{10}}, year = {{2018}}, }