ArticleNature communications2023
Optimal enzyme utilization suggests that concentrations and thermodynamics determine binding mechanisms and enzyme saturations.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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.
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.
Who cites it
15 citing papers in PubMed.
- Microbial drought resistance is achieved at the expense of soil carbon loss.Nature communications · 2026Article
- How far can you go? Extrapolating values of catalytic activity from known protein landscapes in natural and directed evolution.Chemical Society reviews · 2026Review
- XomicsToModel: omics data integration and generation of thermodynamically consistent metabolic models.Nature protocols · 2026Article
- Neuroprotective Nanoplatform Integrating Antioxidant MXene Nanozymes and Ferroptosis Inhibitors for Targeted Therapy of Cerebral Ischemia-Reperfusion Injury.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Complete genome sequencing ofFrontiers in microbiology · 2026Article
- Galactose Oxidase and Horseradish Peroxidase Hybrid Nanoflowers for Biosynthesis of 1-Tetralone.Applied biochemistry and biotechnology · 2025Article
- Kinetic Dissection of the Reaction of Human GDP-l-Fucose Synthase.ACS catalysis · 2025Article
- Effect and mechanism of chlorogenic acid inhibition of starch enzymatic hydrolysis: Comparison of different processing methods.Food chemistry: X · 2025Article
- Jaxkineticmodel: Neural ordinary differential equations inspired parameterization of kinetic models.PLoS computational biology · 2025Article
- Exploration and heterologous expression of laccase genes and pesticide degradation ability of laccases from Cerrena unicolor GC.u01.World journal of microbiology & biotechnology · 2025Article
- Sustainable Bioconversion of Methanol: A Renewable Employing Novel Alcohol Oxidase and Pyruvate Aldolase.Journal of agricultural and food chemistry · 2025Article
- Graphene-based FETs for advanced biocatalytic profiling: investigating heme peroxidase activity with machine learning insights.Mikrochimica acta · 2025Article
- Free-energy transduction mechanisms shape the flux space of metabolic networks.Biophysical journal · 2024Article
- Omics data analysis reveals the system-level constraint on cellular amino acid composition.Synthetic and systems biotechnology · 2024Article
- Optimal enzyme utilization suggests that concentrations and thermodynamics determine binding mechanisms and enzyme saturations.Nature communications · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Deciphering the metabolic functions of organisms requires understanding the dynamic responses of living cells upon genetic and environmental perturbations, which in turn can be inferred from enzymatic activity. In this work, we investigate the optimal modes of operation for enzymes in terms of the evolutionary pressure driving them toward increased catalytic efficiency. We develop a framework using a mixed-integer formulation to assess the distribution of thermodynamic forces and enzyme states, providing detailed insights into the enzymatic mode of operation. We use this framework to explore Michaelis-Menten and random-ordered multi-substrate mechanisms. We show that optimal enzyme utilization is achieved by unique or alternative operating modes dependent on reactant concentrations. We find that in a bimolecular enzyme reaction, the random mechanism is optimal over any other ordered mechanism under physiological conditions. Our framework can investigate the optimal catalytic properties of complex enzyme mechanisms. It can further guide the directed evolution of enzymes and fill in the knowledge gaps in enzyme kinetics.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.