A Levels Biology (9700)•9700/13/O/N/24

Explanation
HIV Protease Active Site Structure
Steps:
- Identify HIV protease as a homodimer with two 99-amino-acid chains.
- Note that each chain contributes a key residue at position 25 to the catalytic site.
- Recognize Asp25 from each chain forms a dyad essential for enzymatic activity.
- Confirm the role via standard biochemistry of aspartyl proteases.
Why A is correct:
- Asp25 is the catalytic aspartic acid residue, forming the active site dyad per the mechanism of aspartyl proteases.
Why the others are wrong:
- B: Ignores the dimeric nature; single chain lacks full activity.
- C: Position 25 is aspartate, not glycine, which is not catalytic.
- D: Amino acid 25 pairs with the symmetric Asp25 from the other chain, not residue 50.
Not enough information: Question cuts off after "amino acid 25 and," leaving choices ambiguous.
Final answer: A
Topic: Mode of action of enzymes
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