Evidence map›Paper›PMID 20099310›Full record

ReviewProteins2010

At the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis?

Shina C L Kamerlin, Arieh Warshel

Abstract readReview
In one paragraph

Review in Proteins, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 203 papers.

0numbers the graph read from it
0cells of the map it votes in
203citing papers in PubMed
10.6field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

203 citing papers in PubMed, 481 citations in OpenAlex.

  1. Review
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  7. Expose flexible conformations for intrinsically disordered protein.Current research in structural biology · 2025
    Article
  8. Article
  9. Article
  10. Review
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  13. A Foundational Shift in Models for Enzyme Function.Journal of the American Chemical Society · 2025
    Review
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  15. Review
  16. Article
  17. Article
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  19. Review
  20. Article

143 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Shina C L KamerlinDepartment of Chemistry, University of Southern California, Los Angeles, 90089, USA.
Arieh Warshel
University of Southern California · US

Funding

THEORETICAL STUDIES OF ENZYMATIC REACTIONSR01GM024492 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI WARSHEL, ARIEH · 1985 to 2017
$5.0M
NIGMS NIH HHS GM24492NIGMS NIH HHS R01 GM024492PHS HHS 1 U191050101-01PHS HHS 5U19A105010
6 · The paper itself

Abstract

Enzymes play a key role in almost all biological processes, accelerating a variety of metabolic reactions as well as controlling energy transduction, the transcription, and translation of genetic information, and signaling. They possess the remarkable capacity to accelerate reactions by many orders of magnitude compared to their uncatalyzed counterparts, making feasible crucial processes that would otherwise not occur on biologically relevant timescales. Thus, there is broad interest in understanding the catalytic power of enzymes on a molecular level. Several proposals have been put forward to try to explain this phenomenon, and one that has rapidly gained momentum in recent years is the idea that enzyme dynamics somehow contributes to catalysis. This review examines the dynamical proposal in a critical way, considering basically all reasonable definitions, including (but not limited to) such proposed effects as "coupling between conformational and chemical motions," "landscape searches" and "entropy funnels." It is shown that none of these proposed effects have been experimentally demonstrated to contribute to catalysis, nor are they supported by consistent theoretical studies. On the other hand, it is clarified that careful simulation studies have excluded most (if not all) dynamical proposals. This review places significant emphasis on clarifying the role of logical definitions of different catalytic proposals, and on the need for a clear formulation in terms of the assumed potential surface and reaction coordinate. Finally, it is pointed out that electrostatic preorganization actually accounts for the observed catalytic effects of enzymes, through the corresponding changes in the activation free energies.

Indexed as

BiocatalysisAnimalsBiochemistryComputer SimulationEnzymesHumansModels, BiologicalThermodynamicsEnzymes

Identifiers

PMID20099310
PMCPMC2841229
OpenAlexW2152572188

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.