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Which outcome fundamentally alters reaction rate during enzyme inhibition?

A)Enzyme-substrate complex concentration greatly decreases
B)Reaction enthalpy increases towards endothermic
C)Product disassociation equilibrium favors reactants
D)Solvent viscosity prevents efficient diffusion

💡 Explanation

Enzyme inhibition reduces available enzyme, therefore the Michaelis-Menten kinetics show a decrease in the enzymatic saturation. This is because fewer enzyme-substrate complexes will form, rather than enthalpy changes or diffusion because binding affinity diminishes.

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