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Home/Biophysics, Fluids & Geoscience/Enzyme Inhibition Kinetics

Enzyme Inhibition Kinetics

This simulator compares ideal Michaelis-Menten inhibition mechanisms. Competitive inhibition increases apparent Km, noncompetitive inhibition lowers apparent Vmax, and uncompetitive inhibition lowers both Km and Vmax. The same parameters are shown on Michaelis-Menten and Lineweaver-Burk views so the intercept changes are visible.

Who it's for: Biochemistry, pharmacology, enzyme kinetics, and pre-medical biology courses.

Key terms

  • Michaelis-Menten
  • Competitive inhibition
  • Noncompetitive inhibition
  • Uncompetitive inhibition
  • Km
  • Vmax

The curves are idealized steady-state Michaelis-Menten kinetics. The Lineweaver-Burk panel is useful for seeing which intercept changes under each inhibition mechanism.

Live graphs

Inhibition mode

Kinetic parameters

1.2
0.45
0.55
0.35
0.7

Measured values

α2.571
v([S] probe)0.452
Apparent Vmax1.200
Apparent Km1.157

How it works

Compare competitive, noncompetitive, and uncompetitive enzyme inhibition on Michaelis-Menten and Lineweaver-Burk plots.

Key equations

v = Vmax [S] / (Km + [S]); α = 1 + [I]/Ki
Competitive: Km→αKm; noncompetitive: Vmax→Vmax/α; uncompetitive: Km,Vmax both scale down

Frequently asked questions

Why show Lineweaver-Burk plots?
They are not the best way to fit modern data, but they make changes in slope and intercept visually clear for teaching inhibition mechanisms.
Is this a full enzyme mechanism?
No. It is the steady-state textbook model with a single substrate and reversible inhibitor summarized by Ki.