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Biochemistry · Enzyme kinetics: inhibition types
Sample itemIn a Lineweaver-Burk plot, an enzyme without inhibitor has Km 5 mM and Vmax 100. With an inhibitor, the line has double the y-intercept but the same x-intercept. Which inhibition type and values apply?
Original practice item, not a recalled exam question. Nothing here is recorded.
The answer and the reasoning
A. Noncompetitive; Vmax 50, Km 5 mM
The y-intercept is 1/Vmax, so doubling it halves Vmax to 50. The x-intercept is -1/Km, and since it is unchanged Km stays at 5 mM. Reduced Vmax with unchanged Km is the signature of pure noncompetitive inhibition, in which the inhibitor binds a site distinct from the active site.
Option by option
A. Noncompetitive; Vmax 50, Km 5 mM (correct)
Correct. Doubled 1/Vmax means Vmax 50, and an unchanged x-intercept means Km 5 mM.
B. Uncompetitive; Vmax 50, Km 2.5 mM
Uncompetitive inhibition gives parallel lines, with both Vmax and Km reduced.
C. Competitive; Vmax 100, Km 10 mM
Competitive inhibition shifts the x-intercept and leaves the y-intercept unchanged.
D. Noncompetitive; Vmax 200, Km 5 mM
A doubled y-intercept halves Vmax; it does not double it.
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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