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Transaminase-Catalyzed Racemization with Potential for Dynamic Kinetic Resolutions

Ruggieri, Federica ; van Langen, Luuk M. ; Logan, Derek T. LU orcid ; Walse, Björn LU and Berglund, Per (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
; ; ; and
publishing date
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}},
}