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nmdcat.online June 27, 2026

The catalytic efficiency of an enzyme is significantly reduced by a non-competitive inhibitor because it

A. Competes for the same active site as the substrate
B. Denatures the enzyme by breaking all peptide bonds
C. Binds to an allosteric site and changes the active site's conformation
✓
D. Removes the cofactor from the holoenzyme irreversibly

📝 Explanation

A non-competitive inhibitor binds to a site different from the active site (an allosteric site). This binding alters the three-dimensional shape of the enzyme, including the active site, so the substrate can no longer bind effectively, regardless of substrate concentration.

📖 Additional Information

  • Competes for the same active site as the substrate
  • Denatures the enzyme by breaking all peptide bonds
  • Binds to an allosteric site and changes the active site's conformation
  • Removes the cofactor from the holoenzyme irreversibly

A non-competitive inhibitor binds to a site different from the active site (an allosteric site). This binding alters the three-dimensional shape of the enzyme, including the active site, so the substrate can no longer bind effectively, regardless of substrate concentration.

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