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

Amina Frese | Zendy; Peter W. Sutton | Zendy; J.P. Turkenburg | Zendy; Gideon Grogan | Zendy

Open Access

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

Author(s) -

Amina Frese,

Peter W. Sutton,

J.P. Turkenburg,

Gideon Grogan

Publication year - 2016

Publication title -

acs catalysis

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 4.898

H-Index - 198

ISSN - 2155-5435

DOI - 10.1021/acscatal.6b03056

Subject(s) - racemization , chemistry , catalysis , catalytic cycle , amino acid , enzyme , stereochemistry , caprolactam , combinatorial chemistry , organic chemistry , biochemistry

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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