A competitive inhibitor resembles an enzyme's substrate and binds its active site. How does increasing inhibitor concentration affect measurable kinetics?

Question

Accepted Answer

B. Apparent Km increases while Vmax remains reachable, because enough substrate can eventually outcompete the inhibitor.

Answer

Vmax falls steadily while Km stays constant, because fewer functional enzyme molecules remain.

Answer

Apparent Km increases while Vmax remains reachable, because enough substrate can eventually outcompete the inhibitor.

Answer

Both Km and Vmax decrease because the inhibitor stabilizes the enzyme-substrate complex.

Answer

Neither parameter changes, because reversible binding cancels out over time.

A competitive inhibitor resembles an enzyme's substrate and binds its active site. How does increasing inhibitor concentration affect measurable kinetics?

Explanation

Core Concept

Correct Answer

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