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Which consequence results when an enzyme's active site becomes saturated in a metabolic pathway?

A)Enzyme reaction experiences zero-order kinetics
B)Product inhibition decreases pathway flux
C)Michaelis-Menten constant approximates substrate concentration
D)Transition state stabilization becomes rate-limiting

💡 Explanation

Saturation leads to zero-order kinetics because the enzyme's rate is independent of substrate concentration, therefore the reaction rate plateaus, rather than increasing despite further substrate boosts, deviating from first-order dependence.

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