The inhibitors that bind tightly and permanently to enzymes and change their globular structure and catalytic activity are:
Correct answer: B. Irreversible inhibitors
- A. Reversible inhibitors
- B. Irreversible inhibitors
- C. Competitive inhibitors
- D. Non-competitive inhibitors
Explanation
Irreversible inhibitors are characterized by their ability to bind permanently to enzymes, often through covalent bonds, leading to an alteration in the enzyme's globular structure and a permanent loss of catalytic activity. Unlike reversible inhibitors, which can detach and allow the enzyme to regain function, irreversible inhibitors permanently inactivate the enzyme. This distinguishes them from both competitive and non-competitive inhibitors, which are types of reversible inhibitors that do not permanently change the enzyme's structure.
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About Enzymes
Enzymes are biological catalysts that lower activation energy without being consumed, and their specificity is explained by the lock and key and induced fit models. Work includes the effects of temperature, pH and substrate concentration on reaction rate, plus competitive and non-competitive inhibition and how these differ.
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