Which outcome arises when an irreversible inhibitor permanently binds to an enzyme active site, affecting reaction kinetics?

💡 Explanation

When an irreversible inhibitor binds, the enzyme's effective concentration decreases because the inhibitor permanently blocks the active site, altering the maximal reaction rate constant. Therefore Vmax decreases proportionally to the amount of bound inhibitor, rather than Km inceasing, substrate overcoming, or shifting equilibrium; mechanisms that require reversible interactions.

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