#1 / Describe how an allosteric inhibitor operates and use an example to explain how it works. #2 / Describe a competitive inhibitor and use an example to explain how it works.

Allosteric control, in enzymology, inhibition or activation of an enzyme by a small regulatory molecule that interacts at a site (allosteric site) other than the active site (at which catalytic activity occurs). The interaction changes the shape of the enzyme so as to affect the formation at the active site of the usual complex between the enzyme and its substrate (the compound upon which it acts to form a product). As a result, the ability of the enzyme to catalyze a reaction is modified. This is the basis of the so-called induced-fit theory, which states that the binding of a substrate or some other molecule to an enzyme causes a change in the shape of the enzyme so as to enhance or inhibit its activity.