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Question
Explain the role of allosteric site in enzyme inhibition?
Solution
Some drugs do not bind to the enzyme’s active site. These bind to a different site of enzyme which is called allosteric site. This bonding of inhibitor at allosteric site changes the shape of the active site in such a way that substrate cannot recognise it. As a result, the affinity of the substrate for the active site is reduced.
It may be noted that if the bond formed between enzyme and inhibitor is 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 enzymes.
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RELATED QUESTIONS
Name the macromolecules that are chosen as drug targets.
Which of the following statements is correct?
Which of the following statements is not true about enzyme inhibitors?
Which site of an enzyme is called allosteric site?
What type of forces are involved in binding of substrate to the active site of enzyme?
Why are certain drugs called enzyme inhibitors?
What happens when the bond formed between an enzyme and an inhibitor is a strong covalent bond?
Assertion: Enzymes have active sites that hold substrate molecule for a chemical reaction.
Reason: Drugs compete with natural substrate by attaching covalently to the active site of enzyme.
Assertion: Non-competitive inhibitor inhibits the catalyic activity of enzyme by binding with its active site.
Reason: Non-competitive inhibitor changes the shape of the active site in such a way that substrate can’t recognise it.
How do enzymes catalyse a chemical reaction in the living system? Explain drug target interaction taking the example of enzyme as target.
