Evidence map›Paper›PMID 26087289›Full record

ArticleArchives of biochemistry and biophysics2015

Are there dynamical effects in enzyme catalysis? Some thoughts concerning the enzymatic chemical step.

Iñaki Tuñón, Damien Laage, James T Hynes

Abstract read
In one paragraph

Article in Archives of biochemistry and biophysics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Conformational dynamics and enzyme evolution.Journal of the Royal Society, Interface · 2018
    Review
  8. Review
  9. Quantifying the limits of transition state theory in enzymatic catalysis.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  10. Article
  11. Review
  12. Article
  13. Phase Space Bottlenecks in Enzymatic Reactions.The journal of physical chemistry. B · 2016
    Article
  14. Article
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

3 authors.

Iñaki TuñónDepartamento de Química Física, Universidad de Valencia, Spain. Electronic address: ignacio.tunon@uv.es.
Damien LaageEcole Normale Supérieure-PSL Research University, Chemistry Department, Sorbonne Universités-UPMC University Paris 06, CNRS UMR 8640 Pasteur, 24 rue Lhomond, 75005 Paris, France. Electronic address: damien.laage@ens.fr.
James T HynesEcole Normale Supérieure-PSL Research University, Chemistry Department, Sorbonne Universités-UPMC University Paris 06, CNRS UMR 8640 Pasteur, 24 rue Lhomond, 75005 Paris, France; Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO 80309-0215, USA. Electronic address: james.hynes@colorado.edu.

Funding

European Research Council 279977
6 · The paper itself

Abstract

We offer some thoughts on the much debated issue of dynamical effects in enzyme catalysis, and more specifically on their potential role in the acceleration of the chemical step. Since the term 'dynamics' has been used with different meanings, we find it useful to first return to the Transition State Theory rate constant, its assumptions and the choices it involves, and detail the various sources of deviations from it due to dynamics (or not). We suggest that much can be learned about the key current questions for enzyme catalysis from prior extensive studies of dynamical and other effects in the case of reactions in solution. We analyze dynamical effects both in the neighborhood of the transition state and far from it, together with the situation when quantum nuclear motion is central to the reaction, and we illustrate our discussion with various examples of enzymatic reactions.

Indexed as

BiocatalysisDiffusionEnzyme ActivationEnzymesEscherichia coliKineticsModels, BiologicalProtein ConformationProtonsQuantum TheoryTetrahydrofolate DehydrogenaseVibrationEnzymesProtonsTetrahydrofolate DehydrogenaseDynamical effectsEnzyme catalysisTransition State Theory

Identifiers

PMID26087289
PMCPMC4560206

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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.