Frese, Amina, Sutton, Peter W., Turkenburg, Johan P. et al. (1 more author) (2017) Snapshots of the Catalytic Cycle of the Industrial Enzyme α-Amino-ε-Caprolactam Racemase (ACLR) observed using X-ray Crystallography. ACS Catalysis. pp. 1045-1048. ISSN 2155-5435
Abstract
α-Amino-ε-Caprolactam Racemase (ACLR) is a PLP-dependent enzyme exploited in industry for the racemization of amino acid amides in dynamic kinetic resolutions that produce homochiral amino acids. We report high-resolution structures of wild-type and variant ACLRs from Rhizobium freirei, generated using the chiral substrate ACL and representative of covalent intermediates in the catalytic cycle. These complexes substantiate suggestions of a two-base mechanism, in which the PLP-binding K267 and D210 serve as proton donors in the racemization, and constitute a robust basis on which to engineer ACLRs for improved activity as industrial biocatalysts.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | © 2016 American Chemical Society. 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: | 17 Jan 2017 14:41 |
Last Modified: | 16 Oct 2024 13:28 |
Published Version: | https://doi.org/10.1021/acscatal.6b03056 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1021/acscatal.6b03056 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:110696 |
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