How does an allosteric inhibitor regulate enzyme activity?
Answer and explanation
Correct answer: A. By binding to a regulatory site other than the active site and changing enzyme conformation
- Step 1: Define allosteric regulation.
- Step 2: An allosteric inhibitor binds to a non-active allosteric site, inducing a conformational change in the enzyme that lowers substrate affinity or catalytic efficiency at the active site.
Answer
By binding to a regulatory site other than the active site and changing enzyme conformation.
Why not the others: Competing for the active site is competitive inhibition; cleaving peptide bonds is irreversible proteolysis; destroying coenzymes is oxidative inactivation.
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