Allosteric regulation is the control of an enzyme's activity through sites distinct from its active site.When an effector molecule binds to such an allosteric site, it can induce a conformational change in the enzyme.This change may increase the affinity of the enzyme's active sites for its substrates, enhancing the enzyme's activity— a process known as allosteric activation.The reaction rates for many allosteric enzymes create a positive S-shaped curve when graphed against increasing substrate concentrations.When a positive effector is added, the allosteric activation shifts the graph to a nearly hyperbolic curve.On the other hand, if the binding of the effector causes a conformational change that decreases the affinity of the enzyme for its substrate, the process is referred to as allosteric inhibition.This decrease in enzyme function can result in a reduced rate of the chemical reaction compared to the activated state.