[Campbell Biology P.209] What is the fundamental difference in the effect of an allosteric a... | Practice Question

What is the fundamental difference in the effect of an allosteric activator versus an allosteric inhibitor on enzyme activity?

  • A: Activators bind to the active site, inhibitors bind elsewhere.
  • B: Activators stabilize the active enzyme conformation, while inhibitors stabilize the inactive enzyme conformation.
  • C: Inhibitors increase substrate affinity, activators decrease it.
  • D: Activators are always proteins, inhibitors are always small molecules.

Explanation

The text states that 'The binding of an activator to a regulatory site stabilizes the shape that has functional active sites, whereas the binding of an inhibitor stabilizes the inactive form of the enzyme.'