Enzyme Kinetics – AP Biology | ShowMeClass

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Enzyme Kinetics

AP Biology · Unit 3: Cellular Energetics

Learning Objectives

Describe induced fit model and active site

Interpret Michaelis-Menten (V vs [S]) curve

Define Vmax and Km and their significance

Distinguish competitive and noncompetitive inhibition

Michaelis-Menten Equation

Inhibition Types

Competitive: blocks active site; ↑Km, Vmax unchanged

Noncompetitive: binds allosteric site; ↓Vmax, Km unchanged

EnzymeMichaelis-MentenAP Biology

Vmax (μmol/min) 10.0

Km (mM) 2.0

[S] highlight (mM) 2.0

Inhibitor type

Inhibitor [I] 1.0

Vmax—

Km—

V at [S]—

InhibitorNone

App. Vmax—

App. Km—

📝 Quick Quiz▼

1. At [S] = Km, the reaction rate V equals:

Vmax Vmax/4 Vmax/2 0

2. Competitive inhibition can be overcome by:

Adding more inhibitor Increasing substrate concentration Decreasing temperature Changing the inhibitor's structure

3. Which inhibitor type lowers Vmax but keeps Km unchanged?

Competitive Noncompetitive Uncompetitive Substrate analog