How does a noncompetitive enzyme inhibitor affect the kinetic parameters Km and Vmax?
Answer and explanation
Correct answer: C. Decreases Vmax while leaving Km unchanged
A pure noncompetitive inhibitor binds to an allosteric site with equal affinity for free enzyme and enzyme-substrate complex, reducing catalytic turnover (lowering Vmax) without altering substrate binding affinity (Km unchanged).
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