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PubMed · 11859194

Enzyme dynamics during catalysis.

Elan Zohar Eisenmesser·Daryl A Bosco·Mikael Akke·Dorothee Kern
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Abstract

Internal protein dynamics are intimately connected to enzymatic catalysis. However, enzyme motions linked to substrate turnover remain largely unknown. We have studied dynamics of an enzyme during catalysis at atomic resolution using nuclear magnetic resonance relaxation methods. During catalytic action of the enzyme cyclophilin A, we detect conformational fluctuations of the active site that occur on a time scale of hundreds of microseconds. The rates of conformational dynamics of the enzyme strongly correlate with the microscopic rates of substrate turnover. The present results, together with available structural data, allow a prediction of the reaction trajectory.

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Binding SitesCatalysisCyclophilin AHydrogen BondingIsomerismKineticsMathematicsModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein BindingProtein ConformationJournal ArticleResearch Support, Non-U.S. Gov'tResearch Support, U.S. Gov't, Non-P.H.S.Research Support, U.S. Gov't, P.H.S.

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Elan Zohar Eisenmesser, Daryl A Bosco, Mikael Akke, Dorothee Kern. 2002-02-22. Enzyme dynamics during catalysis.. https://doi.org/10.1126/science.1066176

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