Issue 2, 2017

Biocatalytic stereoinversion of d-para-bromophenylalanine in a one-pot three-enzyme reaction

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.

Graphical abstract: Biocatalytic stereoinversion of d-para-bromophenylalanine in a one-pot three-enzyme reaction

Supplementary files

Article information

Article type
Paper
Submitted
14 ⵢⵓⵍ 2016
Accepted
07 ⴽⵜⵓ 2016
First published
07 ⴽⵜⵓ 2016

Green Chem., 2017,19, 503-510

Biocatalytic stereoinversion of D-para-bromophenylalanine in a one-pot three-enzyme reaction

F. Khorsand, C. D. Murphy, A. J. Whitehead and P. C. Engel, Green Chem., 2017, 19, 503 DOI: 10.1039/C6GC01922F

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements