Where do drugs that act as allosteric inhibitors bind?

Allosteric inhibitors bind at the allosteric site of the enzyme, which is a specific region distinct from the active site. This binding induces a conformational change in the enzyme, which affects its activity. Unlike inhibitors that compete directly with substrates for the active site, allosteric inhibitors alter the enzyme's shape, thereby influencing how effectively the enzyme can catalyze a reaction.

This mechanism allows for more nuanced regulation of enzyme activity, enabling the cell to respond appropriately to changes in metabolic conditions. The allosteric site is designed to recognize and bind specific molecules, allowing for this regulatory effect without interfering directly with substrate binding. This mode of action is particularly important in controlling metabolic pathways and ensuring that enzymes function optimally under varying conditions.