Enzyme Dynamics During Catalysis

Author:

Eisenmesser Elan Zohar1,Bosco Daryl A.1,Akke Mikael2,Kern Dorothee1

Affiliation:

1. Department of Biochemistry, Brandeis University, Waltham, MA 02454, USA.

2. Department of Biophysical Chemistry, Lund University, Post Office Box 124, SE-221 00 Lund, Sweden.

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference47 articles.

1. Chemical Basis for Enzyme Catalysis

2. A. Fersht Structure and Mechanism in Protein Science. A Guide to Enzyme Catalysis and Protein Folding (Freeman New York ed. 1 1999) pp. 44–51.

3. Protein NMR relaxation: theory, applications and outlook

4. A. G. Palmer 3rd Curr. Opin. Struct. Biol. 7 732 (1997).

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