What characterizes mixed inhibition in enzymatic reactions?

Mixed inhibition is characterized by an inhibitor that binds to both the free enzyme and the enzyme-substrate complex but with unequal affinity. This type of inhibition results in a decrease in the maximum velocity (Vmax) of the reaction because the presence of the inhibitor effectively reduces the overall number of active enzyme molecules available to catalyze the reaction.

In terms of Km, mixed inhibition can either increase or decrease this value depending on the specific binding affinities involved. Since the inhibitor can affect the enzyme and its substrate interaction differently based on its binding, the inhibition has a more complex effect compared to competitive or non-competitive inhibition.

Therefore, mixed inhibition ultimately leads to a reduction in Vmax and an alteration in Km, reflecting the nuanced interactions between the inhibitor and the enzyme-substrate dynamics. This is what makes the claimed answer about mixed inhibition accurate.