Biochemistry · Enzymes (Kinetics, Mechanism, Clinical Significance)

On a Lineweaver-Burk plot, an inhibitor produces lines that intersect to the LEFT of the y-axis, above the x-axis, with both the slope and the y-intercept increased compared with uninhibited lines. This pattern indicates:

  • A Pure competitive inhibition
  • B Uncompetitive inhibition
  • C Pure non-competitive inhibition
  • D Mixed inhibition with greater affinity for free enzyme than for the enzyme-substrate complex
Correct answer: D. Mixed inhibition with greater affinity for free enzyme than for the enzyme-substrate complex

Explanation

In mixed inhibition the inhibitor binds both free enzyme and the ES complex with different affinities, changing both slope and intercepts. When affinity for free enzyme exceeds affinity for ES, apparent Km rises and Vmax falls, producing lines intersecting above and left of the origin. Pure non-competitive inhibition is the special case where both affinities are equal, giving intersection exactly on the x-axis, which distinguishes option C from this plot.

Reference: Lehninger Principles of Biochemistry, 7th ed.

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