Imine reductases (IREDs)

Juan Mangas-Sanchez; Scott P France; Sarah L Montgomery; Godwin A Aleku; Henry Man; Mahima Sharma; Jeremy I Ramsden; Gideon Grogan; Nicholas J Turner

doi:10.1016/j.cbpa.2016.11.022

Imine reductases (IREDs)

Juan Mangas-Sanchez, Scott P France, Sarah L Montgomery, Godwin A Aleku, Henry Man, Mahima Sharma, Jeremy I Ramsden, Gideon Grogan, Nicholas J Turner

Chemistry

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

Abstract

Imine reductases (IREDs) have emerged as a valuable new set of biocatalysts for the asymmetric synthesis of optically active amines. The development of bioinformatics tools and searchable databases has led to the identification of a diverse range of new IRED biocatalysts that have been characterised and employed in different synthetic processes. This review describes the latest developments in the structural and mechanistic aspects of IREDs, together with synthetic applications of these enzymes, and identifies ongoing and future challenges in the field.

Original language	English
Pages (from-to)	19-25
Number of pages	7
Journal	Current Opinion in Chemical Biology
Volume	37
Early online date	27 Dec 2016
DOIs	https://doi.org/10.1016/j.cbpa.2016.11.022
Publication status	Published - Apr 2017

Bibliographical note

© 2016 Elsevier Ltd. All rights reserved. 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

10.1016/j.cbpa.2016.11.022

Mangas-Sanchez 2016 Accepted Manuscript
© 2016 Elsevier Ltd. All rights reserved. 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, 5.37 MB

Cite this

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abstract = "Imine reductases (IREDs) have emerged as a valuable new set of biocatalysts for the asymmetric synthesis of optically active amines. The development of bioinformatics tools and searchable databases has led to the identification of a diverse range of new IRED biocatalysts that have been characterised and employed in different synthetic processes. This review describes the latest developments in the structural and mechanistic aspects of IREDs, together with synthetic applications of these enzymes, and identifies ongoing and future challenges in the field.",

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AU - Mangas-Sanchez, Juan

AU - France, Scott P

AU - Montgomery, Sarah L

AU - Aleku, Godwin A

AU - Man, Henry

AU - Sharma, Mahima

AU - Ramsden, Jeremy I

AU - Grogan, Gideon

AU - Turner, Nicholas J

N1 - © 2016 Elsevier Ltd. All rights reserved. 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 - 2017/4

Y1 - 2017/4

N2 - Imine reductases (IREDs) have emerged as a valuable new set of biocatalysts for the asymmetric synthesis of optically active amines. The development of bioinformatics tools and searchable databases has led to the identification of a diverse range of new IRED biocatalysts that have been characterised and employed in different synthetic processes. This review describes the latest developments in the structural and mechanistic aspects of IREDs, together with synthetic applications of these enzymes, and identifies ongoing and future challenges in the field.

AB - Imine reductases (IREDs) have emerged as a valuable new set of biocatalysts for the asymmetric synthesis of optically active amines. The development of bioinformatics tools and searchable databases has led to the identification of a diverse range of new IRED biocatalysts that have been characterised and employed in different synthetic processes. This review describes the latest developments in the structural and mechanistic aspects of IREDs, together with synthetic applications of these enzymes, and identifies ongoing and future challenges in the field.

U2 - 10.1016/j.cbpa.2016.11.022

DO - 10.1016/j.cbpa.2016.11.022

M3 - Article

C2 - 28038349

SN - 1367-5931

VL - 37

SP - 19

EP - 25

JO - Current Opinion in Chemical Biology

JF - Current Opinion in Chemical Biology

ER -