Evidence map›Paper›PMID 30472832›Full record

ArticleBiochemistry2018

Linear Eyring Plots Conceal a Change in the Rate-Limiting Step in an Enzyme Reaction.

Teresa F G Machado, Tracey M Gloster, Rafael G da Silva

Abstract read
In one paragraph

Article in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Degradation pathway of (R)-1,3-butanediol inApplied and environmental microbiology · 2026
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Why Do Empirical Valence Bond Simulations Yield Accurate Arrhenius Plots?Journal of chemical theory and computation · 2024
    Article
  12. Article
  13. Article
  14. Efficient Empirical Valence Bond Simulations with GROMACS.Journal of chemical theory and computation · 2023
    Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Dissecting the Mechanism of (ACS catalysis · 2020
    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.

Teresa F G Machado
Tracey M Gloster
Rafael G da SilvaORCID 0000-0002-1308-8190

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The temperature dependence of psychrophilic and mesophilic ( R)-3-hydroxybutyrate dehydrogenase steady-state rates yields nonlinear and linear Eyring plots, respectively. Solvent viscosity effects and multiple- and single-turnover pre-steady-state kinetics demonstrate that while product release is rate-limiting at high temperatures for the psychrophilic enzyme, either interconversion between enzyme-substrate and enzyme-product complexes or a step prior to it limits the rate at low temperatures. Unexpectedly, a similar change in the rate-limiting step is observed with the mesophilic enzyme, where a step prior to chemistry becomes rate-limiting at low temperatures. This observation may have implications for past and future interpretations of temperature-rate profiles.

Indexed as

AcetoacetatesAcinetobacter baumanniiBacterial ProteinsBiocatalysisHydroxybutyrate DehydrogenaseKineticsLinear ModelsModels, BiologicalPsychrobacterRecombinant ProteinsSolventsSubstrate SpecificityTemperatureValeratesViscosityAcetoacetatesacetoacetic acidBacterial ProteinsHydroxybutyrate DehydrogenaseRecombinant ProteinsSolventsValerates

Identifiers

PMID30472832
PMCPMC6300308

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.