Explain the rote of allosteric site in enzyme inhibition?
Some drugs do not bind to the active site of enzymes to inhibit their activities. The site different from the active site of an enzyme where a drug molecule can bind is called the allosteric site. This binding of inhibitor (drug) changes the shape of the active site in such a way that substrate cannot recognize it. As a result, the affinity of the substrate for the active site is reduced.
Non-competitive inhibitor changes the active site of the enzyme after binding at the allosteric site.
It may be noted that if the bond formed between the enzyme and inhibitor is a strong covalent bond and therefore cannot be broken easily, then the enzyme gets blocked permanently. The body then degrades the enzyme-inhibitor complex and synthesizes new enzyme.