How does non-competitive inhibition affect Vmax?

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Non-competitive inhibition refers to a mechanism by which an inhibitor can bind to an enzyme regardless of whether the substrate is present. This type of inhibition does not affect the binding of the substrate to the enzyme; however, it decreases the overall number of active enzyme molecules available to catalyze the reaction.

When a non-competitive inhibitor binds to the enzyme, it alters the enzyme's ability to convert substrate into product, effectively lowering the maximum rate of reaction—known as Vmax. Since the inhibitor reduces the amount of functional enzyme available for the reaction without changing the affinity of the enzyme for the substrate (which is represented by Km), the maximum velocity (Vmax) of the reaction is decreased.

It is important to note that while non-competitive inhibition decreases Vmax, the Km remains unchanged, meaning the concentration of substrate required to reach half of Vmax is the same. This property differentiates non-competitive inhibition from competitive inhibition, where Vmax remains the same while Km increases.

In summary, the presence of a non-competitive inhibitor leads to a decrease in Vmax due to fewer enzymatic active sites being available, which reflects the reduced capacity of the enzyme to catalyze the reaction at maximum efficiency.

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