Which of the following statements best describes the role of an uncompetitive inhibitor?

An uncompetitive inhibitor specifically binds to the enzyme-substrate complex, which directly affects the conversion of substrate to product. This type of inhibition leads to a decrease in the overall rate of the reaction by stabilizing the enzyme-substrate complex, effectively restricting the formation of products. Consequently, the presence of the uncompetitive inhibitor reduces the maximum rate of reaction (Vmax) without changing the binding affinity for the substrate (Km). As a result, the situation creates a scenario where, despite the substrate being available, the enzyme cannot efficiently convert it into a product due to the inhibited enzyme-substrate complex.

The correct understanding of uncompetitive inhibition highlights that it does not interfere with the initial binding of the substrate to the enzyme; rather, it only affects the subsequent step of product formation. This distinguishes it from competitive inhibitors, which compete for the active site and can be overcome by increasing substrate concentration, making uncompetitive inhibition unique in its mechanism of action.