Kinetics Analysis App

• Fit data to a Michaelis–Menten model

• View transformations such as Lineweaver–Burk plots

• Estimate key parameters (Km, Vmax)

• Compare how different representations affect interpretation

• Load or enter a dataset

• Observe how reaction rate varies with substrate concentration

• Apply a model fit and inspect the curve

• Switch between plot types to compare representations

• The transition from approximately linear behaviour at low substrate concentration to saturation at higher concentrations

• Where the reaction rate begins to level off and approach a maximum

• How different plot types emphasise different features of the same data

• Km is the substrate concentration at which the reaction rate reaches half of Vmax, and is often used as an indicator of substrate affinity

• Vmax represents the maximum rate achieved when enzyme active sites are fully occupied

• At low substrate concentration, reaction rate is approximately proportional to substrate concentration

• At high substrate concentration, the enzyme becomes saturated and the reaction rate approaches a limiting value

The analysis is based on standard enzyme kinetics assumptions:

• Formation of an enzyme–substrate complex

• A steady-state approximation

• A single-substrate reaction system

Under these conditions, reaction rate follows Michaelis–Menten behaviour, producing a characteristic saturation curve.

• What features of the data make Km easier or harder to estimate?

• How does changing the graphical representation affect interpretation?

• In what situations might one plot be preferred over another?

This type of analysis is widely used in:

• Biochemistry and enzymology teaching

• Drug and inhibitor studies

• Interpretation of experimental rate data

• Assumes simple Michaelis–Menten kinetics (no cooperativity or allosteric effects)

• Linear transformations (e.g. Lineweaver–Burk) can overweight error at low substrate concentration

• Parameter estimates are sensitive to experimental noise and data quality

This tool is available for reuse and adaptation in teaching and research contexts.

• Download a local copy

If you use the tool in teaching or academic work, please cite:

Price, C. L., Noble, J. G., & Seeley, A. (2025). Kinetic Analysis App. Zenodo. https://doi.org/10.5281/zenodo.15622263

This tool allows you to explore how enzyme kinetics data can be analysed, how key parameters are estimated, and how different representations influence interpretation.