🧬 Enzyme Kinetics
🧬 Enzyme Kinetics
Kinetics
Michaelis-Menten
V = Vmax x [S] / (Km + [S]). Vmax is the maximum rate at saturating substrate. Km is the substrate concentration at half Vmax - lower Km = higher affinity. Competitive inhibitors raise Km, non-competitive lower Vmax.
Enzyme Kinetics Simulation: Rates, Substrates & Inhibition
This enzyme kinetics simulation models the Michaelis-Menten relationship between substrate concentration and reaction rate, letting students observe how enzymes bind substrates in their active sites and lower activation energy. Learners can investigate how temperature, pH, and inhibitor type — competitive or noncompetitive — alter enzyme activity and kinetic parameters like Vmax and Km. It is a powerful free tool for AP Biology, biochemistry, and physiology students studying enzyme function.
What you can do in this simulation
- Vary substrate concentration and plot the resulting reaction rate to visualize Michaelis-Menten kinetics
- Add competitive inhibitors and observe how they increase apparent Km without changing Vmax
- Add noncompetitive inhibitors and see Vmax decrease while Km remains unchanged
- Adjust temperature and pH to explore how enzyme conformation and activity change
- Examine enzyme-substrate binding at the active site and the role of induced fit
Concepts covered
enzyme kinetics · Michaelis-Menten · enzyme inhibition · active site · biochemistry · catalysis
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