A competitive inhibitor reduces the rate of an enzyme catalysed reaction by

Correct answer: C. occupying the active site because it resembles the substrate

  • 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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About Enzymes as Biocatalysts

Enzymes are protein or RNA biocatalysts that lower activation energy without being consumed, and their active sites bind specific substrates. The topic covers the lock and key and induced fit models, effects of temperature, pH and substrate concentration, cofactors, enzyme specificity, and competitive versus non-competitive inhibition.

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