Allosteric inhibition is the progression by which a regulatory molecule attaches to an enzyme in a spot different from the active site for an additional particle, which causes a conformational alteration in the dynamic place for the second molecule, thwarting binding.
This progression is also known as noncompetitive inhibition. A similar method is used in allosteric activation, in which the modification of the binding site increases the binding of the second molecule, which is referred to as noncompetitive initiation.
In a method similar to allosteric inhibition, competitive inhibition is also used to prevent enzymatic activation. In competitive inhibition, the controlling molecule binds to the same site as the other molecule, which hinders binding from occurring.