Simultaneous engineering of an enzyme's entrance tunnel and active site: the case of monoamine oxidase MAO-N-Reference-Cited by-同舟云学术

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Simultaneous engineering of an enzyme's entrance tunnel and active site: the case of monoamine oxidase MAO-N

Published:2017 Issue:5 Volume:8 Page:4093-4099
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Li Guangyue¹²³⁴⁵,Yao Peiyuan⁶⁷⁸⁹¹⁰,Gong Rui⁶⁷⁸⁹¹⁰,Li Jinlong⁶⁷⁸⁹¹⁰,Liu Pi⁶⁷⁸⁹¹⁰,Lonsdale Richard¹²³⁴⁵,Wu Qiaqing⁶⁷⁸⁹¹⁰,Lin Jianping⁶⁷⁸⁹¹⁰,Zhu Dunming⁶⁷⁸⁹¹⁰^ORCID,Reetz Manfred T.¹²³⁴⁵^ORCID

Affiliation:

1. Max-Planck-Institut für Kohlenforschung

2. Mülheim an der Ruhr

3. Germany

4. Fachbereich Chemie

5. Philipps-Universität

6. National Engineering Laboratory for Industrial Enzymes

7. Tianjin Engineering Center for Biocatalytic Technology

8. Tianjin Institute of Industrial Biotechnology

9. Chinese Academy of Sciences

10. Tianjin 300308

Abstract

An efficient directed evolution strategy for enhancing activity and manipulating stereoselectivity of a monoamine oxidase is presented.

Funder

Max-Planck-Gesellschaft

Chinese Academy of Sciences

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2017/SC/C6SC05381E

Reference58 articles.

1. Biocatalysis: A Status Report

2. Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently

3. Improving and repurposing biocatalysts via directed evolution

4. E. M. J. Gillam , J. N.Copp and D. F.Ackerley, in Methods in Molecular Biology, Humana Press, Totowa, NJ, 2014, vol. 1179

5. Enzyme Engineering by Targeted Libraries

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