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nmdcat.online July 11, 2026

The activity of an allosteric enzyme is regulated by an effector molecule that binds to a site distinct from the active site. This binding typically results in

A. Irreversible denaturation of the enzyme protein
B. A conformational change that alters the affinity or activity of the active site
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C. Complete dissociation of the quaternary structure into inactive monomers
D. Competition with the substrate for the amino acid residues in the active site

📝 Explanation

Allosteric regulation involves binding to a regulatory site, which induces a conformational change transmitted to the active site, modifying its affinity or efficiency.

📖 Additional Information

  • Irreversible denaturation of the enzyme protein
  • A conformational change that alters the affinity or activity of the active site
  • Complete dissociation of the quaternary structure into inactive monomers
  • Competition with the substrate for the amino acid residues in the active site

Allosteric regulation involves binding to a regulatory site, which induces a conformational change transmitted to the active site, modifying its affinity or efficiency.

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