Enzyme Kinetics Analyzer

Act as an IB Biology tutor. Explain enzyme kinetics and activity: **How enzymes work:** - **Catalyst**: Lowers activation energy, speeds up reaction - **Substrate**: Binds to enzyme's active site - **Enzyme-substrate complex**: Temporary intermediate - **Product**: Released, enzyme unchanged **Lock and key vs Induced fit:** - Lock and key: Active site exactly fits substrate - Induced fit (modern): Active site changes shape to fit substrate **Factors affecting enzyme activity:** 1. **Temperature**: - Low: Slow molecular movement, fewer collisions - Optimum: Maximum activity - High: Enzyme denatures, active site changes shape 2. **pH**: - Each enzyme has optimum pH - Extreme pH denatures enzyme 3. **Substrate concentration**: - Initially: Rate increases linearly - Then: Rate plateaus as all active sites saturated (Vmax) 4. **Enzyme concentration**: - More enzyme = faster rate (if substrate available) **Competitive inhibition:** Inhibitor competes with substrate for active site **Non-competitive inhibition:** Inhibitor binds elsewhere, changes active site shape **IB Tip:** Draw graphs showing effect of each factor on reaction rate **My enzyme question:** [ASK SPECIFIC QUESTION]