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Biocatalytic stereoinversion of D-para-bromophenylalanine in a one-pot three-enzyme reaction
Date Issued
2016-10-07
Date Available
2018-01-23T17:53:06Z
Abstract
Halogenated derivatives of phenylalanine can be used as cross-coupling reagents for making drug-like molecules, and pure enantiomers of these precursors are therefore highly desirable. In our exploration of enzymatic routes to simplify the deracemisation process, the application of two enzymes, D-amino acid transaminase and phenylalanine dehydrogenase, both from Lysinibacillus sphaericus, has given promising results for the stereo-inversion of D-enantiomers of para-bromophenylalanine as the model substrate and also p-chloro/fluorophenylalanine and tyrosine. The addition of a coenzyme recycling system using ethanol and alcohol dehydrogenase reduced the amount of coenzyme needed for the reaction catalysed by phenylalanine dehydrogenase, reducing cost and permitting efficient and complete conversion of the racemic amino acids to the L-enantiomer. Relative proportions of the enzymes were optimized. The high purity of the L-enantiomer, with an ee over 99%, and the ease of the process make it an ideal alternative for deracemisation of the studied compounds.
Sponsorship
Irish Research Council
Type of Material
Journal Article
Publisher
Royal Society of Chemistry
Journal
Green Chemistry
Volume
19
Issue
2
Start Page
503
End Page
510
Copyright (Published Version)
2016 Royal Society of Chemistry
Language
English
Status of Item
Peer reviewed
This item is made available under a Creative Commons License
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