3D pH & Enzyme Activity

Adjust · bind · react · explain

Mode

Enzyme reaction chamber

Enzyme

Visual investigation

Solution pH7.0

Substrate concentration5.0 mM

Temperature37 °C

Enzyme amount1.0×

Simulation speed1×

Tap the enzyme, active site, ions, substrate, products, probe, or graph for a short explanation.

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Voice and language

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Narration volume100%

Embedded loudness-normalized narration can be captured by an external recorder using tab or system audio. No built-in recording controls are included.

Ready · 10 visual chapters.

Chapters

Learning objectives

Explain how pH changes active-site charge and shape.
Interpret an enzyme's bell-shaped activity–pH curve.
Distinguish reversible activity loss from denaturation.
Connect substrate saturation to V max and K m.
Compare pH optima of pepsin, amylase, and trypsin.

Key relationships

pH is logarithmic: each unit represents a tenfold hydrogen-ion change. Activity depends on the fraction of correctly protonated enzyme and on substrate saturation.

Suggested experiments

Sweep pH 1–14 for each enzyme.
Hold pH at optimum and increase substrate.
Compare optimum pH with extreme-pH denaturation.
Raise temperature while pH remains optimal.
Double enzyme amount and inspect V max.

Questions

Why do different enzymes have different pH optima? Why does rate plateau at high substrate? How can extreme pH alter protein structure?

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Ten independent pages. Works with touch, stylus, mouse, Android devices and interactive smart boards.