Evidence map›Paper›PMID 25210031›Full record

ReviewThe Journal of biological chemistry2014

Evolutionary aspects of enzyme dynamics.

Judith P Klinman, Amnon Kohen

Abstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Harnessing Conformational Plasticity to Generate Designer Enzymes.Journal of the American Chemical Society · 2020
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Conformational dynamics and enzyme evolution.Journal of the Royal Society, Interface · 2018
    Review
  17. Article
  18. Article
  19. Article
  20. Why the Energy Landscape of Barnase Is Hierarchical.Frontiers in molecular biosciences · 2018
    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

2 authors.

Judith P KlinmanDepartment of Chemistry, Department of Molecular and Cell Biology, and the California Institute for Quantitative Biosciences, University of California, Berkeley, Berkeley, California 94720 and. Electronic address: klinman@berkeley.edu.
Amnon KohenDepartment of Chemistry, The University of Iowa, Iowa City, Iowa 52242-1294. Electronic address: amnon-kohen@uiowa.edu.

Funding

Toward a Comprehensive Model for Enzyme CatalysisR01GM025765 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI KLINMAN, JUDITH P · 1985 to 2015
$7.1M
Tunneling and dynamic studies with DHFRR01GM065368 · NIGMS · UNIVERSITY OF IOWA · PI CHEATUM, CHRISTOPHER M · 2002 to 2017
$3.5M
DOPAMINE MONOOXYGENASE--MOLECULAR MECHANISMSR37GM025765 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI KLINMAN, JUDITH POLLOCK · 1990 to 1999
–
NIGMS NIH HHS GM025765NIGMS NIH HHS GM65368NIGMS NIH HHS R01 GM025765NIGMS NIH HHS R01 GM065368NIGMS NIH HHS R37 GM025765
6 · The paper itself

Abstract

The role of evolutionary pressure on the chemical step catalyzed by enzymes is somewhat enigmatic, in part because chemistry is not rate-limiting for many optimized systems. Herein, we present studies that examine various aspects of the evolutionary relationship between protein dynamics and the chemical step in two paradigmatic enzyme families, dihydrofolate reductases and alcohol dehydrogenases. Molecular details of both convergent and divergent evolution are beginning to emerge. The findings suggest that protein dynamics across an entire enzyme can play a role in adaptation to differing physiological conditions. The growing tool kit of kinetics, kinetic isotope effects, molecular biology, biophysics, and bioinformatics provides means to link evolutionary changes in structure-dynamics function to the vibrational and conformational states of each protein.

Indexed as

Evolution, MolecularAlcohol DehydrogenaseAnimalsBacterial ProteinsBiocatalysisCatalytic DomainHumansKineticsModels, ChemicalTetrahydrofolate DehydrogenaseAlcohol DehydrogenaseBacterial ProteinsTetrahydrofolate DehydrogenaseAlcohol Dehydrogenase (ADH)EnzymeEnzyme CatalysisEnzyme KineticsEnzyme MechanismEnzyme MutationEvolutionFolate MetabolismMolecular EvolutionProtein Evolution

Identifiers

PMID25210031
PMCPMC4215204

What OpenQuestion holds

Textmetadata
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.