Grogan, Gideon James orcid.org/0000-0003-1383-7056, Frese, Amina, Barrass, Sarah et al. (2 more authors) (2018) An Aminocaprolactam Racemase from Ochrobactrum anthropi with Promiscuous Amino Acid Ester Racemase Activity. Chembiochem. pp. 1-5. ISSN 1439-7633
Abstract
The kinetic resolution of amino acid esters (AAEs) is a useful synthetic strategy for the preparation of single enantiomer amino acids. The development of an enzymatic dynamic kinetic resolution (DKR) process for AAEs, which would give a theoretical yield of 100% of the enantiopure product, would require an amino acid ester racemase (AAER), however, no such enzyme has been described. We have identified low AAER activity of 15 U mg-1 in a homolog of a PLP-dependent α-amino ε-caprolactam racemase (ACLR) from Ochrobactrum anthropi. We have determined the structure of this enzyme, OaACLR, to a resolution of 1.87 Å and using structure-guided saturation mutagenesis, in combination with a colorimetric screen for AAER activity, we have identified a mutant, L293C, in which the promiscuous AAER activity of this enzyme towards L-phenylalanine methyl ester is improved 3.7 fold.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2018 Wiley-VCH Verlag GmbH &Co. KGaA, Weinheim. This is an author-produced version of the published paper. Uploaded in accordance with the publisher’s self-archiving policy. Further copying may not be permitted; contact the publisher for details. |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) |
Depositing User: | Pure (York) |
Date Deposited: | 24 Aug 2018 08:20 |
Last Modified: | 07 Feb 2025 00:21 |
Published Version: | https://doi.org/10.1002 /cbic.201 800265 |
Status: | Published online |
Refereed: | Yes |
Identification Number: | 10.1002 /cbic.201 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:134975 |
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