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

doi:10.1021/acscatal.6b03056

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

Chemistry

Research output: Contribution to journal › Article › peer-review

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.

Original language	English
Pages (from-to)	1045-1048
Number of pages	4
Journal	ACS Catalysis
Volume	7
Issue number	2
Early online date	20 Dec 2016
DOIs	https://doi.org/10.1021/acscatal.6b03056
Publication status	Published - 2017

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.

Access to Document

10.1021/acscatal.6b03056

Frese et al. Accepted Manuscript
© 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.
Accepted author manuscript, 1.34 MB

http://dx.doi.org/10.1021/acscatal.6b03056

Cite this

@article{a63d20a251a742c9940ec6b4e50738a4,

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

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.",

author = "Amina Frese and Sutton, {Peter W.} and Turkenburg, {Johan P.} and Gideon Grogan",

note = "{\textcopyright} 2016 American Chemical Society. This is an author-produced version of the published paper. Uploaded in accordance with the publisher{\textquoteright}s self-archiving policy. Further copying may not be permitted; contact the publisher for details.",

year = "2017",

doi = "10.1021/acscatal.6b03056",

language = "English",

volume = "7",

pages = "1045--1048",

journal = "ACS Catalysis",

issn = "2155-5435",

publisher = "American Chemical Society",

number = "2",

}

TY - JOUR

T1 - Snapshots of the Catalytic Cycle of the Industrial Enzyme α-Amino-ε-Caprolactam Racemase (ACLR) observed using X-ray Crystallography

AU - Frese, Amina

AU - Sutton, Peter W.

AU - Turkenburg, Johan P.

AU - Grogan, Gideon

N1 - © 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.

PY - 2017

Y1 - 2017

N2 - 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.

AB - 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.

U2 - 10.1021/acscatal.6b03056

DO - 10.1021/acscatal.6b03056

M3 - Article

VL - 7

SP - 1045

EP - 1048

JO - ACS Catalysis

JF - ACS Catalysis

SN - 2155-5435

IS - 2

ER -