Final answer:
Allosteric regulation involves the binding of molecules to an allosteric site on an enzyme, causing a conformational change that can either inhibit or activate the enzyme.
Step-by-step explanation:
Allosteric regulation is a process where enzymes are regulated by the binding of a molecule at a site other than the active site. This can lead to either an increase or decrease in enzyme activity. Allosteric sites are specific locations on an enzyme where molecules known as effectors or modulators can bind, causing a change in the enzyme's conformation and affecting its function. Allosteric inhibitors bind to these sites and induce a conformational change that usually reduces the enzyme's affinity for its substrate, resulting in decreased enzyme activity. Conversely, allosteric activators bind to allosteric sites and cause a conformational change that increases the enzyme's affinity for its substrate, resulting in enhanced enzyme activity.