A competitive inhibitor slows an enzyme catalysed reaction by
- A. binding the active site because it resembles the substrate
- B. binding a site away from the active site and distorting it
- C. permanently destroying the enzyme
- D. lowering the pH of the surroundings
Explanation
A competitive inhibitor is structurally similar to the substrate and occupies the active site, so substrate and inhibitor compete for the same place. Because the competition depends on relative concentrations, adding more substrate overcomes the inhibition and Vmax is unchanged. The description in the second option is non-competitive inhibition, which binds an allosteric site instead.
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