Enzyme dynamics during catalysis
Eisenmesser, Elan Zohar ; Bosco, Daryl A ; Akke, Mikael LU
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:
https://lup.lub.lu.se/record/131424
- author
- Eisenmesser, Elan Zohar
; Bosco, Daryl A
; Akke, Mikael
LU
and Kern, Dorothee
- organization
- publishing date
- 2002
- 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
- 2022-03-15 01:01:37
@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}},
}