General Biology I · Module 5 · Energy, enzymes and metabolism

Energy and Enzymes Lab

Run an enzyme rate bench and watch the curve respond; train on free energy, energy diagrams, rate curves and inhibitors with animated worked solutions; sort the key terms; and read real experiments. Nothing here is graded.

Part 1: Enzyme Rate Bench

Enzymes bind substrate, make product and let go. The graph shows rate against substrate for the settings you choose.
Enzyme Substrate Product Competitive inhibitor (I) Noncompetitive inhibitor (N) Your curve Reference: no inhibitors, best conditions
Live readouts
MeasureValue

The rate follows the Michaelis-Menten equation, v = Vmax[S] ÷ (Km + [S]), with Km = 2 mM and Vmax = 10 µmol/min for 1 unit of enzyme at its best temperature and pH. A competitive inhibitor multiplies Km by (1 + [I]/Ki); a pure noncompetitive inhibitor divides Vmax by (1 + [N]/Ki). Temperature uses Q10 = 2 below the optimum and denaturation above it; pH uses a bell curve around the optimum. Denaturation here is shown as instant and reversible so you can explore; real heat denaturation is often permanent. Animation speed is exaggerated.