Question:medium
Which one of the following shows allosteric inhibition ?
Which one of the following shows allosteric inhibition ?
Updated On: Jun 24, 2026
- Malonic acid & succinate
- 2, 3 BPG
- Amino acid alanine & pyruvate kinase
- Citrate
Show Solution
The Correct Option is B
Solution and Explanation
Step 1: Recall the concept. A true allosteric inhibitor docks at a regulatory site away from the catalytic site and reduces substrate binding affinity across the protein's subunits.
Step 2: Spot the classic example. 2,3-BPG is the standard illustration: it slots into a central pocket of hemoglobin and decreases oxygen affinity of every subunit, stabilizing the tense (deoxy) state. This is negative allosteric modulation in its purest form.
Step 3: Discard the others. Malonate versus succinate is a competitive inhibition pair at the succinate dehydrogenase active site, not an allosteric one. The remaining options do not give the clean classic allosteric picture that 2,3-BPG does.
The hemoglobin regulator is the textbook allosteric inhibitor.\[\boxed{\text{2,3 BPG}}\]
Step 2: Spot the classic example. 2,3-BPG is the standard illustration: it slots into a central pocket of hemoglobin and decreases oxygen affinity of every subunit, stabilizing the tense (deoxy) state. This is negative allosteric modulation in its purest form.
Step 3: Discard the others. Malonate versus succinate is a competitive inhibition pair at the succinate dehydrogenase active site, not an allosteric one. The remaining options do not give the clean classic allosteric picture that 2,3-BPG does.
The hemoglobin regulator is the textbook allosteric inhibitor.\[\boxed{\text{2,3 BPG}}\]
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