How does a non-competitive (allosteric) enzyme inhibitor affect enzyme kinetics?
Answer and explanation
Correct answer: C. It binds to an allosteric site, reducing Vmax without altering the substrate affinity Km
Pure non-competitive inhibitors bind with equal affinity to both the free enzyme and the enzyme-substrate complex at an allosteric site distinct from the active site. Because the substrate can still bind but catalysis is impaired, substrate affinity is unchanged (Km remains constant), while the overall catalytic capacity is reduced (Vmax decreases). Uncompetitive inhibitors reduce both Km and Vmax.
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