Snapshots of the Catalytic Cycle of the Industrial Enzyme α-Amino-ε-Caprolactam Racemase (ACLR) observed using X-ray Crystallography

Amina Frese, Peter W. Sutton, Johan P. Turkenburg, Gideon Grogan

Research output: Contribution to journalArticlepeer-review


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.
Original languageEnglish
Pages (from-to)1045-1048
Number of pages4
JournalACS Catalysis
Issue number2
Early online date20 Dec 2016
Publication statusPublished - 2017

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© 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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