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Molecules 2015, 20(1), 1192-1209;

Linking Protein Motion to Enzyme Catalysis

Department of Chemistry, University of Iowa, Iowa City, IA 52242, USA
These authors contributed equally to this work.
Author to whom correspondence should be addressed.
Academic Editor: Lajos Novak
Received: 29 November 2014 / Accepted: 7 January 2015 / Published: 13 January 2015
(This article belongs to the Special Issue Enzyme-Catalyzed Reactions)
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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. View Full-Text
Keywords: dihydrofolate reductase; thymidylate synthase; kinetic isotope effect; protein motions; dynamics dihydrofolate reductase; thymidylate synthase; kinetic isotope effect; protein motions; dynamics

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Singh, P.; Abeysinghe, T.; Kohen, A. Linking Protein Motion to Enzyme Catalysis. Molecules 2015, 20, 1192-1209.

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