Lesson Plan

• Describe the relationship between Vmax, Km, and substrate concentration.
• Explain how Vmax is determined from enzyme assay data.
• Apply the Michaelis–Menten equation to calculate Km.
• Compare enzyme affinities using Km values.
• Evaluate the effect of temperature, pH, and inhibitors on Vmax and Km.

• Projector and screen
• Whiteboard and markers
• Printed worksheets with substrate‑concentration tables
• Graph paper or digital graphing tool (e.g., Excel)
• Sample data set for enzyme assay
• Calculator

Begin with a quick demonstration of a reaction rate increasing as substrate is added, asking students what they notice. Recall prior learning on enzymes as catalysts and the concept of reaction velocity. State that by the end of the lesson they will be able to determine Vmax, calculate Km, and use Km to compare enzyme affinities.

1. Do‑now (5'): Students answer a short question on factors affecting enzyme rate on the board.
2. Mini‑lecture (10'): Review enzyme kinetics, introduce Vmax and Km, and display a Michaelis–Menten curve.
3. Guided practice (15'): Plot sample data to locate Vmax and calculate Km using a Lineweaver–Burk plot.
4. Collaborative activity (10'): Groups compare Km values from a provided table and discuss affinity implications.
5. Formative check (5'): Exit ticket – write one sentence explaining how Km reflects enzyme affinity.

Summarise that Vmax indicates the catalytic capacity when the enzyme is saturated, while Km provides a measure of substrate affinity. Ask students to complete a quick exit ticket describing the relationship between Km and affinity. For homework, assign problems requiring calculation of Km from given Vmax and substrate data.