An allosteric site on an enzyme is an section other than the active site, the site where the substrate actually binds. So, if an activator binds to the allosteric site, it makes conditions favorable for the substrate to bind to the enzyme thus "activating" the enzyme. The opposite happens when an inhibitor binds to the allosteric site because the inhibitor makes conditions unfavorable for the substrate to bind to the enzyme thus "inhibiting" the enzyme.
These conditions are changed due to complex associations and interactions between amino acids in the enzyme as well as the inhibitor or activator.
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An allosteric site on an enzyme is an section other than the active site, the site where the substrate actually binds. So, if an activator binds to the allosteric site, it makes conditions favorable for the substrate to bind to the enzyme thus "activating" the enzyme. The opposite happens when an inhibitor binds to the allosteric site because the inhibitor makes conditions unfavorable for the substrate to bind to the enzyme thus "inhibiting" the enzyme.
These conditions are changed due to complex associations and interactions between amino acids in the enzyme as well as the inhibitor or activator.