Dr. Lim, Carmay
Emeritus Research Fellow
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Specialty:
- Computational Biophysics
- Computational Chemistry
- Bioinformatics
Education and Positions:
1984, Ph.D. in Chemical Physics, University of Minnesota, Minneapolis
1979, B.S. in Chemistry, Royal Holloway College, London University
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Efficient Binding of Flexible and Redox-Active Coenzymes by Oxidoreductases
Dr. Lim, Carmay
ACS Catalysis, Jun 03, 2016Although how an enzyme binds its substrate and rate-limiting transition state is well-studied, how it binds a flexible redox-active coenzyme, which may adopt different native solution conformations when oxidized/reduced, remains unclear. Using the coenzyme nicotinamide adenine dinucleotide (NAD) as an example, we show that redox enzymes bind oxidized NAD+and reduced NADH in similar conformations that are between folded NAD+ and extended NADH solution conformations. By preorganizing the coenzyme-binding site to bind such an “intermediate” conformation, a redox enzyme can efficiently bind oxidized and reduced NAD, whereas having to substantially reorganize the binding site to accommodate the NAD product might impede catalysis.