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Biochemistry · Enzyme kinetics
Sample itemWhich pattern describes a competitive inhibitor?
Original practice item, not a recalled exam question. Nothing here is recorded.
The answer and the reasoning
A. Km increases and Vmax is unchanged
A competitive inhibitor binds the active site and competes with substrate. More substrate is needed to reach half-maximal velocity, so apparent Km rises, but a high enough substrate concentration overcomes it, so Vmax is unchanged. Non-competitive inhibitors lower Vmax with Km unchanged.
Option by option
A. Km increases and Vmax is unchanged (correct)
Correct. Substrate can outcompete the inhibitor, so Vmax is reached but at a higher Km.
B. Km is unchanged and Vmax decreases
This is the non-competitive pattern, where inhibitor reduces the amount of working enzyme.
C. Both Km and Vmax decrease
Both falling is the uncompetitive pattern.
D. Km decreases and Vmax is unchanged
A falling Km with unchanged Vmax does not describe a standard inhibitor pattern.
Source note: Original NextPrep sample item — pending expert review. This item is original practice material awaiting independent expert review, so confirm important facts in a standard textbook.
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