Which outcome arises when irreversible enzyme inhibitor molecules bind near an enzyme's active site, increasing Michaelis constant Km?

💡 Explanation

When an irreversible inhibitor increases Km, it reduces substrate binding affinity because the enzyme's active site geometry is perturbed, leading to slower reaction rates, especially at low substrate concentrations. Therefore, reduced product formation occurs at low substrate, rather than increased enzyme efficiency or substrate accumulation because inhibitor binding is irreversible.

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