Advertisements
Advertisements
प्रश्न
What happens when the bond formed between an enzyme and an inhibitor is a strong covalent bond?
उत्तर
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.
APPEARS IN
संबंधित प्रश्न
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?
Explain the role of allosteric site in enzyme inhibition?
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.
