Evidence map›Paper›PMID 29208922›Full record

ArticleScientific reports2017

Beyond the Michaelis-Menten equation: Accurate and efficient estimation of enzyme kinetic parameters.

Boseung Choi, Grzegorz A Rempala, Jae Kyoung Kim

Abstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing 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

60 citing papers in PubMed.

  1. Article
  2. Fluorescent Analysis of KBiomolecules · 2026
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  6. Understanding low-pressure CONature chemistry · 2026
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  9. Introducing Quantitative Assessment of Michaelis Constant (KChembiochem : a European journal of chemical biology · 2025
    Article
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  11. Chemical Modification ofInternational journal of molecular sciences · 2025
    Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Building Localized NADP(H) Recycling Circuits to Advance Enzyme Cascadetronics.Angewandte Chemie (International ed. in English) · 2025
    Article
  18. Article
  19. Article
  20. From homogeneity to heterogeneity: Refining stochastic simulations of gene regulation.Computational and structural biotechnology journal · 2025
    Article
4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

3 authors.

Boseung ChoiKorea University Sejong campus, Division of Economics and Statistics, Department of National Statistics, Sejong, 30019, Korea.
Grzegorz A RempalaThe Ohio State University, Division of Biostatistics and Mathematical Biosciences Institute, Columbus, OH, 43210, USA.
Jae Kyoung KimKorea Advanced Institute of Science and Technology, Department of Mathematical Sciences, Daejeon, 34141, Korea. jaekkim@kaist.ac.kr.ORCID 0000-0001-7842-2172

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Examining enzyme kinetics is critical for understanding cellular systems and for using enzymes in industry. The Michaelis-Menten equation has been widely used for over a century to estimate the enzyme kinetic parameters from reaction progress curves of substrates, which is known as the progress curve assay. However, this canonical approach works in limited conditions, such as when there is a large excess of substrate over enzyme. Even when this condition is satisfied, the identifiability of parameters is not always guaranteed, and often not verifiable in practice. To overcome such limitations of the canonical approach for the progress curve assay, here we propose a Bayesian approach based on an equation derived with the total quasi-steady-state approximation. In contrast to the canonical approach, estimates obtained with this proposed approach exhibit little bias for any combination of enzyme and substrate concentrations. Importantly, unlike the canonical approach, an optimal experiment to identify parameters with certainty can be easily designed without any prior information. Indeed, with this proposed design, the kinetic parameters of diverse enzymes with disparate catalytic efficiencies, such as chymotrypsin, fumarase, and urease, can be accurately and precisely estimated from a minimal amount of timecourse data. A publicly accessible computational package performing such accurate and efficient Bayesian inference for enzyme kinetics is provided.

Indexed as

AlgorithmsBayes TheoremCatalysisChymotrypsinFumarate HydrataseHumansKineticsUreaseChymotrypsinFumarate HydrataseUrease

Identifiers

PMID29208922
PMCPMC5717222

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Registered trials

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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.