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nmdcat.online June 27, 2026

A competitive inhibitor reduces the rate of an enzyme-catalyzed reaction by

A. Binding to the allosteric site and altering the enzyme's shape
B. Binding to the enzyme-substrate complex irreversibly
C. Mimicking the substrate and occupying the active site
D. Denaturing the enzyme protein at its active site

📝 Explanation

A competitive inhibitor structurally resembles the substrate and competes for binding at the enzyme's active site. This effect can be overcome by increasing substrate concentration. It does not bind to the allosteric site or permanently alter the enzyme.

📖 Additional Information

  • Binding to the allosteric site and altering the enzyme's shape
  • Binding to the enzyme-substrate complex irreversibly
  • Mimicking the substrate and occupying the active site
  • Denaturing the enzyme protein at its active site

A competitive inhibitor structurally resembles the substrate and competes for binding at the enzyme's active site. This effect can be overcome by increasing substrate concentration. It does not bind to the allosteric site or permanently alter the enzyme.

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