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nmdcat.online June 27, 2026

The reason that an increase in the concentration of a competitive inhibitor does not change the maximum velocity (Vmax) of an enzymatic reaction is that

A. The inhibitor reduces the turnover number of the enzyme
B. The inhibitor permanently denatures a fraction of the enzyme population
C. The inhibitor's binding can be overcome by sufficiently increasing the substrate concentration
✓
D. The inhibitor binds only to the enzyme-substrate complex, not the free enzyme

📝 Explanation

The definition of competitive inhibition is a "competition" for the active site. At a high enough concentration, the substrate out-competes the inhibitor for the active site, so all enzyme molecules can still bind substrate and reach Vmax. The apparent Km is increased, but Vmax is ultimately unchanged.

📖 Additional Information

  • The inhibitor reduces the turnover number of the enzyme
  • The inhibitor permanently denatures a fraction of the enzyme population
  • The inhibitor's binding can be overcome by sufficiently increasing the substrate concentration
  • The inhibitor binds only to the enzyme-substrate complex, not the free enzyme

The definition of competitive inhibition is a "competition" for the active site. At a high enough concentration, the substrate out-competes the inhibitor for the active site, so all enzyme molecules can still bind substrate and reach Vmax. The apparent Km is increased, but Vmax is ultimately unchanged.

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