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प्रश्न
Which of the following statements is not true about enzyme inhibitors?
पर्याय
Inhibit the catalytic activity of the enzyme.
Prevent the binding of substrate.
Generally a strong covalent bond is formed between an inhibitor and an enzyme.
Inhibitors can be competitive or non-competitive.
उत्तर
Generally a strong covalent bond is formed between an inhibitor and an enzyme.
Explanation:
Inhibitors are chemical substances that tend to reduce the activity of a particular enzyme. Generally, a weak bond such as H-bonding, van der Waals interaction, etc. is formed between the enzyme and the inhibitor.
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संबंधित प्रश्न
Which of the following statements is correct?
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?
Explain the role of allosteric site in enzyme inhibition?
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: 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.
