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Just want to add a little something to your answer bio_man. Basically with any
allosteric enzyme, inhibitors or activators, also known as effectors or regulator molecules, actually bind to a different site on the enzyme. This changes the structure of the enzyme, consequently altering its function. When an inhibitor binds to an allosteric enzyme, the enzyme is effectively turned off, and no longer able to function in the body. Activators, on the other hand, turn the enzyme on so that it can perform a function. The regulator molecules can detach as needed. Using this system, cells can regulate the activity of enzymes in response to changing situations, activating enzymes as needed and deactivating them when it does not want them to work. The binding site where a regulator molecule attaches is known is known as the allosteric site on the enzyme. Allosteric regulation of enzymes involves a number of different molecules which can fit on this site, much like keys fit into a lock. With inhibition, the enzyme is maintained so that it will be ready when needed, but won't function before it is required, and with activation, the allosteric enzyme is kicked into gear so that it can perform a desired metabolic function. The body balances the numbers of active and inactive enzymes to modulate a wide variety of biological processes.