A Levels Biology (9700)•9700/13/M/J/18

Explanation
Enzyme Inhibition by Structural and Binding Mechanisms
Steps:
- PHBA's structural similarity to catechol suggests it mimics the substrate, blocking the active site without changing what the enzyme recognizes.
- PTU binds directly to the copper cofactor in the active site, preventing normal catalysis while maintaining the enzyme's substrate preference.
- Option 1 describes a change in what the enzyme binds, but inhibitors here block activity without altering recognition.
- Neither inhibitor denatures or modifies the enzyme's inherent specificity; they reduce rate by occupancy.
Why B is correct:
- Both inhibitors reduce activity by altering effective specificity through competitive blockade, fitting definition of site-specific inhibition without broad changes (per enzyme kinetics).
Why the others are wrong:
- A includes irrelevant mechanisms like 2 and 3, as only 1 applies.
- C focuses solely on competition, ignoring specificity alteration by cofactor binding.
- D relies on undefined 3, which lacks evidence.
Final answer: B
Topic: Mode of action of enzymes
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