biology / Molecules of Life / free

Enzymes

Change substrate concentration and activation energy to see biological catalysis at work.

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A substrate meets a selective site. An enzyme's active site recognizes a substrate through shape, charge, and chemical complementarity. Binding positions the reactants without changing the reaction's overall destination.

enzyme catalysisproductive binding · velocity 46%

Focus the idea

site occupancy67.5%

velocity46%

activation barrier49

equilibrium50%

Substrate concentration 62%Enzyme amount 68%Inhibitor effect 18%Temperature 55%Reaction time 72%

At substrate 62, 67.5% of modeled active sites are occupied. More substrate raises encounter frequency until saturation; inhibitor effect 18% makes productive binding harder.

This is a normalized enzyme model. Real enzymes have specific active-site chemistry, multiple catalytic steps, pH optima, allostery, cooperativity, cofactors, and reaction-specific inhibition mechanisms.

04 / PRACTICE

Make the biology yours.

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Answer from the model, then use the explanation to connect the visual mechanism to the biological rule.

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Enzymes

Make the biology yours.

Why does velocity plateau at high substrate concentration?