Dr. Lim, Carmay 林小喬 博士

Brand

HIGHLIGHT DETAIL
重要成果詳細內容


Efficient Binding of Flexible and Redox-Active Coenzymes by Oxidoreductases

ACS Catalysis, Jun 03, 2016

Although 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.

Journal Link 期刊連結

List of Highlights
文件紀錄

Top