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Snapshots of the Catalytic Cycle of the Industrial Enzyme α-Amino-ε-Caprolactam Racemase (ACLR) observed using X-ray Crystallography
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Publication details
| Journal | ACS Catalysis |
|---|---|
| Date | Accepted/In press - 20 Dec 2016 |
| Date | E-pub ahead of print - 20 Dec 2016 |
| Date | Published (current) - 2017 |
| Issue number | 2 |
| Volume | 7 |
| Number of pages | 4 |
| Pages (from-to) | 1045-1048 |
| Early online date | 20/12/16 |
| Original language | English |
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.
Bibliographical note
© 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.
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