Enzyme Kinetics Simulator | mysimulator.uk

Enzyme Kinetics

Substrate [S] 70

Temperature 37 °C

Competitive inhibitor 0%

Active sites (enzyme) 6

Rate v (products/s)

–

Sites occupied

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Product formed

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v / Vmax

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How it works

Free substrate molecules (blue) diffuse randomly through the cell volume. When one drifts close to an unoccupied active site on an enzyme, it binds — the enzyme changes colour and holds the substrate for a short catalytic delay, then releases it as product (orange), freeing the site for the next collision. A translucent inhibitor (magenta), when present, competes for the same active sites without ever converting: it occupies a site, blocks substrate binding for a while, then lets go unchanged. Reaction rate is measured directly as products formed per second, exactly as Michaelis–Menten kinetics predicts:

v = Vmax · [S] / (Km + [S])
Km = [S] at which v = Vmax / 2
competitive inhibitor → raises apparent Km, Vmax unchanged

Substrate [S] — how many substrate molecules are diffusing in the volume; more collisions per second means a higher reaction rate, until active sites saturate near Vmax.
Temperature — raises diffusion speed and catalytic turnover up to an optimum, then represents thermal denaturation: too hot and some active sites stop working, cutting Vmax.
Competitive inhibitor — a molecule that occupies active sites without reacting, directly competing with substrate; raising it forces [S] higher to reach the same rate (apparent Km rises).
Active sites — number of catalytic centres available; more sites raise Vmax, the ceiling the rate approaches as [S] grows.

This sense-bind-convert-release loop is the same one behind every enzyme in a living cell — from digestive proteases to the polymerases that copy DNA — and it is exactly what pharmacology exploits when a drug is designed as a competitive inhibitor of a disease-relevant enzyme.

Substrate Product Inhibitor Enzyme (free)

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