Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Enzyme dynamics during catalysis

Eisenmesser, Elan Zohar ; Bosco, Daryl A ; Akke, Mikael LU orcid and Kern, Dorothee (2002) In Science 295(5559). p.1520-1523
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.
Please use this url to cite or link to this publication:
author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Science
volume
295
issue
5559
pages
1520 - 1523
publisher
American Association for the Advancement of Science (AAAS)
external identifiers
  • pmid:11859194
  • wos:000173981300052
  • scopus:0037154884
ISSN
1095-9203
DOI
10.1126/science.1066176
language
English
LU publication?
yes
id
b174b3c5-63ac-4aa1-8305-c0d2deb4b5ab (old id 131424)
date added to LUP
2016-04-01 16:30:58
date last changed
2025-04-04 13:52:04
@article{b174b3c5-63ac-4aa1-8305-c0d2deb4b5ab,
  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.}},
  author       = {{Eisenmesser, Elan Zohar and Bosco, Daryl A and Akke, Mikael and Kern, Dorothee}},
  issn         = {{1095-9203}},
  language     = {{eng}},
  number       = {{5559}},
  pages        = {{1520--1523}},
  publisher    = {{American Association for the Advancement of Science (AAAS)}},
  series       = {{Science}},
  title        = {{Enzyme dynamics during catalysis}},
  url          = {{https://lup.lub.lu.se/search/files/4696301/624208.pdf}},
  doi          = {{10.1126/science.1066176}},
  volume       = {{295}},
  year         = {{2002}},
}