Evidence map›Paper›PMID 28855956›Full record

ArticlePlant methods2017

Kinetic modelling: an integrated approach to analyze enzyme activity assays.

Jelena Boeckx, Maarten Hertog, Annemie Geeraerd, Bart Nicolai

Abstract read
In one paragraph

Article in Plant methods, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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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

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3 · Its place in the literature

Who cites it

8 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Protein scaffolds: A tool for multi-enzyme assembly.Biotechnology reports (Amsterdam, Netherlands) · 2021
    Review
  6. Article
  7. Enzyme Models-From Catalysis to Prodrugs.Molecules (Basel, Switzerland) · 2021
    Review
  8. A cost-effective enzyme kinetics and inhibition model for biochemistry education and research.Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology
    Article
4 · The record

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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

4 authors.

Jelena BoeckxBIOSYST-MeBioS, KU Leuven, Willem de Croylaan 42, 3001 Louvain, Belgium.
Maarten HertogBIOSYST-MeBioS, KU Leuven, Willem de Croylaan 42, 3001 Louvain, Belgium.
Annemie GeeraerdBIOSYST-MeBioS, KU Leuven, Willem de Croylaan 42, 3001 Louvain, Belgium.
Bart NicolaiBIOSYST-MeBioS, KU Leuven, Willem de Croylaan 42, 3001 Louvain, Belgium.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundIn general, enzyme activity is estimated from spectrophotometric data, by taking the slope of the linear part of the progress curve describing the rate of change in the substrate or product monitored. As long as the substrate concentrations are sufficiently high to saturate the enzyme and, the velocity of the catalyzed reaction is directly proportional to the enzyme concentration. Under these premises, this velocity can be taken as a measure of the amount of active enzyme present. Estimation of the enzyme activity through linear regression of the data should only be applied when linearity is true, which is often not the case or has not been checked.

resultsIn this paper, we propose a more elaborate method, based on a kinetic modelling approach, to estimate the in vitro specific enzyme activity from spectrophotometric assay data. As a case study, kinetic models were developed to estimate the activity of the enzymes pyruvate decarboxylase and alcohol dehydrogenase extracted from 'Jonagold' apple (

conclusionsIn contrast to the linear regression approach, the models can be used to estimate the enzyme activity regardless of whether linearity is achieved since they integrally take into account the complete progress curve. The use of kinetic models to estimate the enzyme activity can be applied to all other enzymes as long as the underlying reaction mechanism is known. The kinetic models can also be used as a tool to optimize the enzyme assays by systematically studying the effect of the various design parameters.

Indexed as

Alcohol dehydrogenaseEnzyme activityKinetic modelPyruvate decarboxylaseSpectrophotometric enzyme assay

Identifiers

PMID28855956
PMCPMC5574136

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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.