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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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JournalACS Catalysis
DateAccepted/In press - 20 Dec 2016
DateE-pub ahead of print - 20 Dec 2016
DatePublished (current) - 2017
Issue number2
Volume7
Number of pages4
Pages (from-to)1045-1048
Early online date20/12/16
Original languageEnglish

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.

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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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