Enzyme Activity & Kinetics

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About this simulation

Explore an enzyme’s active site and investigate substrate, temperature, pH and competitive inhibition with live rate curves.

What students can explore

At 37 °C and pH 7, how does a competitive inhibitor change the rate as substrate increases?
Illustrative Michaelis–Menten model: v = Vmax[S]/(Km(1+I)+[S]), Km=2. Activity peaks at 37 °C and pH 7 using smooth response factors. Units are relative; this is not a particular enzyme or a reversible denaturation experiment. Binding artwork is schematic.

Learning objectives

1At 37 °C and pH 7, how does a competitive inhibitor change the rate as substrate increases?

Questions teachers ask

At 37 °C and pH 7, how does a competitive inhibitor change the rate as substrate increases?

The inhibitor lowers the rate at a given substrate level. More substrate reduces its relative effect; both curves approach the same maximum.

About the model

Illustrative Michaelis–Menten model: v = Vmax[S]/(Km(1+I)+[S]), Km=2. Activity peaks at 37 °C and pH 7 using smooth response factors. Units are relative; this is not a particular enzyme or a reversible denaturation experiment. Binding artwork is schematic.

Embed this simulation

Drop it into your LMS, blog, or class site — free.

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