Allosteric regulation operates through the binding of an effector molecule, which can be an activator or an inhibitor, at an allosteric site. This binding results in a structural change in the enzyme that impacts the active site's configuration. For instance, in an enzyme that is positively regulated by an allosteric activator, the binding of this activator may enhance the affinity of the enzyme for its substrate, thereby increasing catalytic efficiency. Conversely, an allosteric inhibitor would decrease substrate affinity, reducing the enzyme's activity.
