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Enzyme Dynamics During Catalysis

Open access
Eisenmesser, Elan Zohar, Bosco, Daryl A., Akke, Mikael, Kern, Dorothee·2002·Science

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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Metadata

Authors
Eisenmesser, E. Z., Bosco, D. A., Akke, M., & Kern, D.
Venue
Science
Published
2002-02-22
Volume
295
Issue
5559
Pages
1520-1523
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2066961392
Cited by
731
References
1
FWCI
12.53
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Enzyme Dynamics During Catalysis. https://app.cochat.ai/papers/10.1126/science.1066176
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Eisenmesser, E. Z., Bosco, D. A., Akke, M., & Kern, D. (2002). Enzyme Dynamics During Catalysis. Science. https://doi.org/10.1126/science.1066176

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.