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Biochemistry · Enzyme kinetics
Sample itemWhat happens to the apparent Km of an enzyme when a reversible competitive inhibitor is added?
Original practice item, not a recalled exam question. Nothing here is recorded.
The answer and the reasoning
C. It increases
A competitive inhibitor competes with substrate at the active site, so a higher substrate concentration is needed to reach half-maximal velocity; this increases apparent Km while Vmax can still be reached.
Option by option
A. It makes the enzyme irreversible
Competitive binding is reversible in the usual kinetic model.
B. It decreases to zero
Km does not fall to zero with competitive inhibition.
C. It increases (correct)
Correct: competitive inhibition raises apparent Km.
D. It remains unchanged with lower Vmax
Unchanged Km with reduced Vmax describes a noncompetitive pattern more closely.
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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