⚗ Enzyme Kinetics Lab

Mission: control reaction speed

Watch substrates fit active sites, transform, and leave as products. Change one factor and connect particle events to the measured rate.
Bind
→
React
→
Release
SubstrateEnzymeProductInhibitorActive site
1×

Reaction conditions

5.0 mM
1.0 µM
37 °C
7.0
0.0 mM
0.0µM product/s
0bound enzymes
0products

Rate curve

Blue: current conditions · Orange point: current substrate concentration

Tracked object

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TipTap an enzyme, substrate, product, or inhibitor

Camera

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Teacher tools

Teacher-guided complete lecture

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What to watch: each spoken idea is spotlighted in the reaction chamber.
Choose a language and voice, then begin. The canvas will automatically demonstrate every chapter.
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Chapters

Learning objectives

  • Describe how enzymes lower activation barriers without being consumed.
  • Connect active-site binding to product formation.
  • Interpret substrate saturation and the maximum rate.
  • Compare competitive and noncompetitive inhibition.
  • Predict temperature and pH effects on activity.

Key concepts

Specific binding

A substrate must collide with an active site in a compatible orientation.

Catalytic cycle

Binding, conversion, and release repeat while the enzyme remains available.

Saturation

At high substrate concentration, most active sites are occupied and rate approaches a maximum.

Environmental shape

Temperature and pH affect molecular motion and the enzyme’s folded active-site shape.

Scientific model

The live rate uses an educational Michaelis–Menten model: rate = maximum rate × substrate concentration ÷ (Km + substrate concentration). Enzyme concentration changes maximum rate. Competitive inhibition increases apparent Km; noncompetitive inhibition lowers maximum rate. Temperature and pH use smooth activity factors around an optimum. Particle count, scale, and collision timing are conceptual visualizations.

Try these experiments

  • Raise substrate from low to high and watch the curve flatten.
  • Double enzyme concentration and compare maximum rate.
  • Add competitive inhibitor, then increase substrate.
  • Heat beyond the optimum and observe active-site distortion.

Common misconceptions

  • Enzymes speed both directions toward equilibrium; they do not change the equilibrium position.
  • Enzymes are not used up in one reaction.
  • More substrate cannot raise rate forever when enzyme is limited.
  • Very high temperature may denature an enzyme rather than continually speeding it up.
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