The role of dimer asymmetry and protomer dynamics in enzyme catalysis

Author:

Kim Tae Hun1,Mehrabi Pedram23,Ren Zhong45,Sljoka Adnan6,Ing Christopher78,Bezginov Alexandr2,Ye Libin1,Pomès Régis78,Prosser R. Scott17,Pai Emil F.2379

Affiliation:

1. Department of Chemistry, University of Toronto, Mississauga, Ontario L5L 1C6, Canada.

2. Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5G 1L7, Canada.

3. Ontario Cancer Institute/Princess Margaret Cancer Centre, Campbell Family Institute for Cancer Research, Toronto, Ontario M5G 1L7, Canada.

4. Department of Chemistry, University of Illinois, Chicago, IL 60607, USA.

5. Renz Research Inc., Westmont, IL 60559, USA.

6. CREST, Japan Science and Technology Agency (JST), Department of Informatics, School of Science and Technology, Kwansei Gakuin University, Japan.

7. Department of Biochemistry, University of Toronto, Toronto, Ontario M5S 1A8, Canada.

8. Program in Molecular Structure and Function, Research Institute, Hospital for Sick Children, Toronto, Ontario M5G 1X8, Canada.

9. Department of Molecular Genetics, University of Toronto, Toronto, Ontario M5S 1A8, Canada.

Abstract

Working as a pair Enzymes provide scaffolds that facilitate chemical reactions. Enzyme dynamics often enhance reactivity by allowing the enzyme to sample the transition state between reactants and products. Kim et al. explored the role of dynamics in the dimeric enzyme fluoroacetate dehalogenase (see the Perspective by Saleh and Kalodimos). They found that the two protomers are asymmetric, with only one being able to bind substrate at a time. The nonbinding protomer contributed to catalysis by becoming more dynamic to compensate for the entropy loss of its partner. Science , this issue p. 10.1126/science.aag2355 ; see also p. 247

Funder

Ontario Student Opportunity Trust Fund

Natural Sciences and Engineering Research Council of Canada

Canadian Institutes of Health Research

Canada Research Chairs Program

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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