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nmdcat.online June 27, 2026

The allosteric regulation of an enzyme differs from competitive and non-competitive inhibition in that allosteric modulators

A. Always bind to the active site of the enzyme
B. Bind to a site distinct from the active site, leading to a conformational change
✓
C. Are always irreversible inhibitors of the enzyme
D. Compete with the substrate for binding at the catalytic site

📝 Explanation

Allosteric regulation is mediated by modulator molecules that bind to a site (allosteric site) physically distinct from the active site. This binding causes a conformational change that can either increase (allosteric activator) or decrease (allosteric inhibitor) the activity of the enzyme at its active site.

📖 Additional Information

  • Always bind to the active site of the enzyme
  • Bind to a site distinct from the active site, leading to a conformational change
  • Are always irreversible inhibitors of the enzyme
  • Compete with the substrate for binding at the catalytic site

Allosteric regulation is mediated by modulator molecules that bind to a site (allosteric site) physically distinct from the active site. This binding causes a conformational change that can either increase (allosteric activator) or decrease (allosteric inhibitor) the activity of the enzyme at its active site.

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