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Biochemistry · Enzyme kinetics
Sample itemWhich kinetic change is expected with a pure noncompetitive inhibitor?
Original practice item, not a recalled exam question. Nothing here is recorded.
The answer and the reasoning
A. Lower Vmax with unchanged Km
A pure noncompetitive inhibitor reduces the effective amount of active enzyme, lowering Vmax without altering substrate affinity, so adding more substrate cannot fully restore maximal reaction velocity.
Option by option
A. Lower Vmax with unchanged Km (correct)
Correct: pure noncompetitive inhibition lowers Vmax while Km stays unchanged.
B. Higher Km with unchanged Vmax
Higher Km with preserved Vmax is typical of competitive inhibition.
C. Higher Vmax with lower Km
Increasing Vmax is not the expected effect of inhibition.
D. No effect at any inhibitor concentration
A true inhibitor has a measurable kinetic effect.
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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