Snapshots of the Catalytic Cycle of the Industrial Enzyme α-Amino-Îμ -Caprolactam Racemase (ACLR) Observed Using X-ray Crystallography

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

Research output: Contribution to journalArticleResearchpeer-review

5 Citations (Scopus)

Abstract

© 2016 American Chemical Society. α-Amino-Îμ -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 they constitute a robust basis on which to engineer ACLRs for improved activity as industrial biocatalysts.
Original languageEnglish
Pages (from-to)1045-1048
JournalACS Catalysis
Volume7
Issue number2
DOIs
Publication statusPublished - 3 Feb 2017

Keywords

  • amino acids
  • biocatalysis
  • enzyme mechanism
  • PLP
  • racemase

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