Enzyme catalysis: the Michaelis–Menten curve
Plot the initial rate v of an enzyme reaction against substrate concentration and see why the curve saturates at Vmax.
Goal
Read and off the curve and connect them to enzyme–substrate affinity and enzyme amount.
Apparatus and reagents
Virtual bench: stock substrate solution, catalase-like enzyme, stopwatch and readout; the simulation supplies the full curve.
Procedure
- Start with the reference preset (Km = 1.0, Vmax = 1). Hover at [S] = Km and confirm that v = Vmax/2.
- Switch to Km = 4.0 (low affinity): how much substrate do you now need to reach half of Vmax?
- Compare Km = 1.0, Vmax = 0.5 with the reference: what stays the same and what shrinks? Link that to halving the enzyme.
- For each preset, estimate the apparent efficiency near [S] → 0: it approaches Vmax/Km.
What to observe
- At low [S] the curve is nearly linear with slope Vmax/Km; at high [S] it flattens because every enzyme active site is occupied.
- Doubling Km from 1.0 to 4.0 pushes the half-saturation point fourfold to the right without changing the plateau.
- Halving Vmax lowers the plateau but leaves Km — the half-saturation substrate level — unchanged.
Explanation
The enzyme E binds substrate S reversibly to form ES, which releases product: . When most active sites are empty, doubling [S] roughly doubles v. When [S] ≫ Km, every site is busy and the rate plateaus at : only adding more enzyme raises it. is the substrate level giving half that rate, so a small Km means productive binding even at low [S].
History of the experiment
Chemists behind it
Virtual experiment: a simplified model to build intuition. It does not replace real lab work or safety training; never repeat chemistry at home without supervision.