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Which consequence results when enzymes reach saturation due to limiting Michaelis constant?

A)Decreased substrate-level phosphorylation rate
B)Enzyme kinetics approach zero-order
C)Increased transition state stabilization
D)Reduced effectiveness competitive inhibitors

💡 Explanation

The enzyme rate is limited by its concentration once saturated, because velocity becomes independent of substrate following Michaelis-Menten kinetics. Therefore, reaction rate plateaus and approaches zero-order kinetics rather than continuing to increase at a high rate.

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