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Which outcome reduces catalytic efficiency when reactant concentration saturates enzymatic active sites?

A)Michaelis-Menten kinetics plateaus
B)Catalyst denaturation accelerates rapidly
C)Equilibrium favors product reversal
D)Enzyme confirms negative enantioselectivity

💡 Explanation

The kinetics plateau because the enzyme active sites are fully occupied, such that increasing substrate no longer accelerates the rate due to enzymatic saturation, rather than changes in enzyme structure or reversal of equilibrium.

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