In competitive inhibition, where does the inhibitor bind?

In competitive inhibition, the inhibitor binds directly at the active site of the enzyme. This occurs because the structure of the inhibitor is similar to that of the substrate, allowing it to compete with the substrate for access to the active site. When the inhibitor is bound to the active site, it prevents the substrate from binding, which means that the enzyme is unable to catalyze the reaction. The extent of inhibition can generally be overcome by increasing the concentration of the substrate, leading to the classic feature of competitive inhibition that it can be reversed by higher substrate levels. This mechanism is critical in understanding how enzyme activity can be regulated in metabolic pathways.