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Catalysts 2017, 7(7), 212; doi:10.3390/catal7070212

In Silico Studies of Small Molecule Interactions with Enzymes Reveal Aspects of Catalytic Function

Department of Chemistry, McKinley Hall, Wichita State University, 1845 Fairmount, Wichita, KS 67260-0051, USA
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Received: 20 May 2017 / Revised: 7 July 2017 / Accepted: 10 July 2017 / Published: 14 July 2017
(This article belongs to the Special Issue Computational Methods and Their Application in Catalysis)
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Abstract

Small molecules, such as solvent, substrate, and cofactor molecules, are key players in enzyme catalysis. Computational methods are powerful tools for exploring the dynamics and thermodynamics of these small molecules as they participate in or contribute to enzymatic processes. In-depth knowledge of how small molecule interactions and dynamics influence protein conformational dynamics and function is critical for progress in the field of enzyme catalysis. Although numerous computational studies have focused on enzyme–substrate complexes to gain insight into catalytic mechanisms, transition states and reaction rates, the dynamics of solvents, substrates, and cofactors are generally less well studied. Also, solvent dynamics within the biomolecular solvation layer play an important part in enzyme catalysis, but a full understanding of its role is hampered by its complexity. Moreover, passive substrate transport has been identified in certain enzymes, and the underlying principles of molecular recognition are an area of active investigation. Enzymes are highly dynamic entities that undergo different conformational changes, which range from side chain rearrangement of a residue to larger-scale conformational dynamics involving domains. These events may happen nearby or far away from the catalytic site, and may occur on different time scales, yet many are related to biological and catalytic function. Computational studies, primarily molecular dynamics (MD) simulations, provide atomistic-level insight and site-specific information on small molecule interactions, and their role in conformational pre-reorganization and dynamics in enzyme catalysis. The review is focused on MD simulation studies of small molecule interactions and dynamics to characterize and comprehend protein dynamics and function in catalyzed reactions. Experimental and theoretical methods available to complement and expand insight from MD simulations are discussed briefly. View Full-Text
Keywords: molecular dynamics simulation; catalytic activity; protein conformational dynamics; ligand interactions; cofactor dynamics; substrate access channel; solvent interactions; hydration dynamics; enzyme-substrate complex; allosteric regulation molecular dynamics simulation; catalytic activity; protein conformational dynamics; ligand interactions; cofactor dynamics; substrate access channel; solvent interactions; hydration dynamics; enzyme-substrate complex; allosteric regulation
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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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Verma, R.; Mitchell-Koch, K. In Silico Studies of Small Molecule Interactions with Enzymes Reveal Aspects of Catalytic Function. Catalysts 2017, 7, 212.

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