Which outcome occurs when an enzymatic reaction approaches its Michaelis constant?

💡 Explanation

When substrate concentration equals the Michaelis constant (Km), the reaction rate equals half the maximum velocity (Vmax) because the enzyme's active sites are filled at 50% capacity. Therefore the rate is half of Vmax, rather than enzyme denaturation, substrate limitation at saturation, or complete removal of product inhibition all of which depend on independent constraints.

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