This figure represents_inhibitor.
Correct answer: A. Non-competitive
- A. Non-competitive
- B. Irreversible
- C. Competitive
- D. Isosteric
Explanation
Non-competitive inhibitors bind to an allosteric site, causing a conformational change in the enzyme that reduces its activity regardless of the substrate concentration. This type of inhibition is distinct from competitive inhibition, where the inhibitor competes directly with the substrate for the active site. Irreversible inhibitors form permanent bonds with the enzyme, which is not characteristic of non-competitive inhibitors. Isosteric inhibitors are similar in structure to the substrate and compete for the active site, which does not apply to non-competitive inhibition.
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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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