Evidence map›Paper›PMID 23373756›Full record

ArticleJournal of the American Chemical Society2013

Heavy-enzyme kinetic isotope effects on proton transfer in alanine racemase.

Michael D Toney, Joan Nieto Castro, Trevor A Addington

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

26 citing papers in PubMed, 46 citations in OpenAlex.

  1. Transitioning enzyme catalysis towards photocatalysis.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2025
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Heavy Enzymes and the Rational Redesign of Protein Catalysts.Chembiochem : a European journal of chemical biology · 2019
    Article
  7. Article
  8. Article
  9. Article
  10. Protein Mass Effects on Formate Dehydrogenase.Journal of the American Chemical Society · 2017
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Linking protein motion to enzyme catalysis.Molecules (Basel, Switzerland) · 2015
    Review
  20. 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 at 1 institution in 1 country.

Michael D ToneyDepartment of Chemistry, University of California-Davis, One Shields Avenue, Davis, California 95616, USA. mdtoney@ucdavis.edu
Joan Nieto Castro
Trevor A Addington
University of California, Davis · US

Funding

REACTION SPECIFICITY OF PYRIDOXAL PHOSPHATE ENZYMESR01GM054779 · NIGMS · YESHIVA UNIVERSITY · PI TONEY, MICHAEL · 1997 to 2011
$2.9M
Reaction Specificity of Pyridoxal Phosphate EnzymesR56GM054779 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI TONEY, MICHAEL · 2007 to 2007
$306k
NIGMS NIH HHS GM54779NIGMS NIH HHS R01 GM054779NIGMS NIH HHS R56 GM054779
6 · The paper itself

Abstract

The catalytic effects of perdeuterating the pyridoxal phosphate-dependent enzyme alanine racemase from Geobacillus stearothermophilus are reported. The mass of the heavy perdeuterated form is ~5.5% greater than that of the protiated form, causing kinetic isotope effects (KIEs) of ~1.3 on k(cat) and k(cat)/K(M) for both L- and D-alanine. These values increase when Cα-deuterated alanine is used as the substrate. The heavy-enzyme KIEs of ~3 on k(cat)/K(M) with deuterated substrates are greater than the product of the individual heavy-enzyme and primary substrate KIEs. This breakdown of the rule of the geometric mean is likely due to coupled motion between the protein and the proton-transfer reaction coordinate in the rate-limiting step. These data implicate a direct role for protein vibrational motions in barrier crossing for proton-transfer steps in alanine racemase.

Indexed as

DeuteriumProtonsAlanine RacemaseGeobacillus stearothermophilusKineticsMolecular StructureAlanine RacemaseDeuteriumProtons

Identifiers

PMID23373756
PMCPMC3579662
OpenAlexW2033717022

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.