Linking Protein Motion to Enzyme Catalysis

Molecules

Priyanka Singh¹  Thelma Abeysinghe¹  Amnon Kohen¹ 

关键词: dihydrofolate reductase;    thymidylate synthase;    kinetic isotope effect;    protein motions;    dynamics;   

DOI  :  10.3390/molecules20011192

来源: mdpi

【 摘 要 】

Enzyme motions on a broad range of time scales can play an important role in various intra- and intermolecular events, including substrate binding, catalysis of the chemical conversion, and product release. The relationship between protein motions and catalytic activity is of contemporary interest in enzymology. To understand the factors influencing the rates of enzyme-catalyzed reactions, the dynamics of the protein-solvent-ligand complex must be considered. The current review presents two case studies of enzymes—dihydrofolate reductase (DHFR) and thymidylate synthase (TSase)—and discusses the role of protein motions in their catalyzed reactions. Specifically, we will discuss the utility of kinetic isotope effects (KIEs) and their temperature dependence as tools in probing such phenomena.

【 授权许可】

CC BY   
© 2015 by the authors; licensee MDPI, Basel, Switzerland.