Artificial Imine Reductases: Developments and Future Directions

Rosalind Booth; Gideon James Grogan; Keith Sanderson Wilson; Anne-Kathrin Duhme-Klair

doi:10.1039/D0CB00113A

Artificial Imine Reductases: Developments and Future Directions

Rosalind Booth, Gideon James Grogan, Keith Sanderson Wilson, Anne-Kathrin Duhme-Klair

Chemistry

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

Abstract

Biocatalytic imine reduction has been a topic of intense research by the artificial metalloenzyme community in recent years. Artificial constructs, together with natural enzymes, have been engineered to produce chiral amines with high enantioselectivity. This review examines the design of the main classes of artificial imine reductases reported thus far and summarises approaches to enhancing their catalytic performance using complementary methods. Examples of utilising these biocatalysts in vivo or in multi-enzyme cascades have demonstrated the potential that artIREDs can offer, however, at this time their use in biocatalysis remains limited. This review explores the current scope of artIREDs and the strategies used for catalyst improvement, and examines the potential for artIREDs in the future.

Original language	English
Pages (from-to)	1-10
Number of pages	10
Journal	RSC Chemical Biology
Early online date	16 Oct 2020
DOIs	https://doi.org/10.1039/D0CB00113A
Publication status	Published - 16 Oct 2020

Bibliographical note

Access to Document

10.1039/D0CB00113ALicence: CC BY

d0cb00113a
© 2020, The Author(s).
Final published version, 3.16 MBLicence: CC BY

1 Conference
1 Invited talk

Faraday Discussion Meeting Harnessing Non Covalent Interactions
Duhme-Klair, A.-K. (Committee member)
12 Apr 2023 → 14 Apr 2023
Activity: Participating in or organising an event › Conference
Exploiting siderophores in the development of antimicrobials and artificial enzymes
Duhme-Klair, A.-K. (Keynote/plenary speaker)
21 May 2021
Activity: Talk or presentation › Invited talk

2 Finished

Redox-reversible artificial metalloenzymes
Duhme-Klair, A.-K. (Principal investigator), Johnson, S. D. (Co-investigator) & Wilson, K. S. (Co-investigator)
27/01/20 → 31/10/23
Project: Research project (funded) › Research
Siderophores as anchors in artificial metalloenzymes
Duhme-Klair, A.-K. (Principal investigator) & Wilson, K. S. (Co-investigator)
EPSRC
31/12/14 → 30/12/17
Project: Research project (funded) › Research

Cite this

@article{3c9a5f981a3f4159859b7d4471170916,

title = "Artificial Imine Reductases: Developments and Future Directions",

abstract = "Biocatalytic imine reduction has been a topic of intense research by the artificial metalloenzyme community in recent years. Artificial constructs, together with natural enzymes, have been engineered to produce chiral amines with high enantioselectivity. This review examines the design of the main classes of artificial imine reductases reported thus far and summarises approaches to enhancing their catalytic performance using complementary methods. Examples of utilising these biocatalysts in vivo or in multi-enzyme cascades have demonstrated the potential that artIREDs can offer, however, at this time their use in biocatalysis remains limited. This review explores the current scope of artIREDs and the strategies used for catalyst improvement, and examines the potential for artIREDs in the future. ",

author = "Rosalind Booth and Grogan, {Gideon James} and Wilson, {Keith Sanderson} and Anne-Kathrin Duhme-Klair",

note = "{\textcopyright} 2020, The Author(s). ",

year = "2020",

month = oct,

day = "16",

doi = "10.1039/D0CB00113A",

language = "English",

pages = "1--10",

journal = "RSC Chemical Biology",

issn = "2633-0679",

publisher = "The Royal Society of Chemistry",

}

TY - JOUR

T1 - Artificial Imine Reductases: Developments and Future Directions

AU - Booth, Rosalind

AU - Grogan, Gideon James

AU - Wilson, Keith Sanderson

AU - Duhme-Klair, Anne-Kathrin

PY - 2020/10/16

Y1 - 2020/10/16

N2 - Biocatalytic imine reduction has been a topic of intense research by the artificial metalloenzyme community in recent years. Artificial constructs, together with natural enzymes, have been engineered to produce chiral amines with high enantioselectivity. This review examines the design of the main classes of artificial imine reductases reported thus far and summarises approaches to enhancing their catalytic performance using complementary methods. Examples of utilising these biocatalysts in vivo or in multi-enzyme cascades have demonstrated the potential that artIREDs can offer, however, at this time their use in biocatalysis remains limited. This review explores the current scope of artIREDs and the strategies used for catalyst improvement, and examines the potential for artIREDs in the future.

AB - Biocatalytic imine reduction has been a topic of intense research by the artificial metalloenzyme community in recent years. Artificial constructs, together with natural enzymes, have been engineered to produce chiral amines with high enantioselectivity. This review examines the design of the main classes of artificial imine reductases reported thus far and summarises approaches to enhancing their catalytic performance using complementary methods. Examples of utilising these biocatalysts in vivo or in multi-enzyme cascades have demonstrated the potential that artIREDs can offer, however, at this time their use in biocatalysis remains limited. This review explores the current scope of artIREDs and the strategies used for catalyst improvement, and examines the potential for artIREDs in the future.

U2 - 10.1039/D0CB00113A

DO - 10.1039/D0CB00113A

M3 - Article

SN - 2633-0679

SP - 1

EP - 10

JO - RSC Chemical Biology

JF - RSC Chemical Biology

ER -

Artificial Imine Reductases: Developments and Future Directions

Abstract

Bibliographical note

Access to Document

Activities

Faraday Discussion Meeting Harnessing Non Covalent Interactions

Exploiting siderophores in the development of antimicrobials and artificial enzymes

Projects

Redox-reversible artificial metalloenzymes

Siderophores as anchors in artificial metalloenzymes

Cite this