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Question
What happens when the bond formed between an enzyme and an inhibitor is a strong covalent bond?
Solution
If the bond formed between an enzyme and an inhibitor is a strong covalent bond and cannot be broken easily, then the enzyme is blocked permanently, The body then degrades the enzyme-inhibitor complex and synthesises the new enzyme.
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RELATED QUESTIONS
Name the macromolecules that are chosen as drug targets.
Which forces are involved in holding the drugs to the active site of enzymes?
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?
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: Competitive inhibitors compete with natural substrate for their attachment on the active sites of enzymes.
Reason: In competitive inhibition, inhibitor binds to the allosteric site of the 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.
What are enzyme inhibitors? Classify them on the basis of their mode of attachments on the active site of enzymes. With the help of diagrams explain how do inhibitors inhibit the enzymatic activity.
