A competitive inhibitor reduces the rate of an enzyme catalysed reaction by
- A. denaturing the enzyme permanently
- B. binding an allosteric site
- C. occupying the active site because it resembles the substrate
- D. lowering the temperature
Explanation
Substrate and inhibitor compete for the same site, so the inhibition can be overcome by increasing the substrate concentration and the maximum rate is eventually still reached. A non competitive inhibitor binds elsewhere, changes the shape of the enzyme and cannot be outcompeted, so it genuinely lowers the maximum rate. Many drugs are designed as competitive inhibitors of a specific enzyme.
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