Changes in Active Site Loop Conformation Relate to the Transition toward a Novel Enzymatic Activity-Reference-Cited by-同舟云学术

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Changes in Active Site Loop Conformation Relate to the Transition toward a Novel Enzymatic Activity

Published:2024-04-25 Issue:5 Volume:4 Page:1941-1953
ISSN:2691-3704
Container-title:JACS Au
language:en
Short-container-title:JACS Au

Author:

Jacquet Pauline¹,Billot Raphaël¹^ORCID,Shimon Amir²,Hoekstra Nathan²,Bergonzi Céline¹²,Jenks Anthony³,Chabrière Eric¹⁴,Daudé David¹,Elias Mikael H.²³^ORCID

Affiliation:

1. Gene&GreenTK, 19-21 Bd Jean Moulin, Marseille 13005, France

2. Biotechnology Institute, University of Minnesota, St. Paul, Minnesota 55108, United States

3. Department of Biochemistry, Molecular Biology and Biophysics & Biotechnology Institute, University of Minnesota, St. Paul, Minnesota 55108, United States

4. Aix Marseille University, IRD, APHM, MEPHI, IHU Méditerranée Infection, Marseille 13005, France

Funder

Agence Nationale de la Recherche

University of Minnesota

National Institute of General Medical Sciences

Direction G?n?rale de l'Armement

MnDrive Initiative

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/jacsau.4c00179

Reference78 articles.

1. Enzyme Promiscuity: Engine of Evolutionary Innovation

2. Catalytic promiscuity and the evolution of new enzymatic activities

3. What makes an enzyme promiscuous?

4. The subtle benefits of being promiscuous: Adaptive evolution potentiated by enzyme promiscuity

5. The 'evolvability' of promiscuous protein functions

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2. Applications of Microbial Organophosphate-Degrading Enzymes to Detoxification of Organophosphorous Compounds for Medical Countermeasures against Poisoning and Environmental Remediation;International Journal of Molecular Sciences;2024-07-17

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