ReviewBiomolecules2025
Time-Dependent Kinetic Complexities in Enzyme Assays: A Review.
Review in Biomolecules, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Composition and activity of the proteasome in human iPSC-derived neuronal model of early-stage sporadic Alzheimer's disease.bioRxiv : the preprint server for biology · 2026Article
- Development of Cathepsin B‑Activatable Cell-Penetrating Peptides for Tumor Targeting.ACS pharmacology & translational science · 2026Article
- Development of Quantum dot-based enzyme biosensor for the detection of dopamine in urine.Scientific reports · 2026Article
- Free energy perturbations in enzyme kinetic models reveal cryptic epistasis.PLoS computational biology · 2026Article
- Differentiating the Substrate Profiles of Inflammatory Caspases Using Extended Förster Resonance Energy Transfer-Based Peptide Substrates.Chembiochem : a European journal of chemical biology · 2026Article
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the present review, the importance of analyzing full progress curves in enzyme assays is discussed. The atypical kinetic behavior that can be potentially displayed by enzymes in the performance of an activity assay, as well as the models explaining such behavior, are analyzed. These complex time-dependent kinetic patterns include hysteresis, damped oscillatory hysteresis, unstable product, and kinetic competence. The atypical time-dependent patterns are discussed with both real examples and In Silico simulations. When possible, the physiological implications of such kinetic behaviors are included. The importance of analyzing the derivative of the reaction rate of such atypical transitions as a method to distinguish them from the conventional non-atypical time progress curve is stressed.
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Registered trials
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