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Irreversible Enzyme Inhibition: Active Site Directed
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Irreversible Enzyme Inhibition: Active Site Directed

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Questions and Answers

What is the turnover number in enzyme kinetics?

  • The time it takes for an enzyme to saturate with substrate
  • The rate at which the product is converted to the substrate
  • The stability of the enzyme-substrate complex
  • The number of substrate molecules converted to product in a given unit of time on a single enzyme molecule (correct)

    • What happens if a competitive inhibitor is removed from the system?

  • The enzyme remains inactive
  • The action of the enzyme is fully restored (correct)
  • The Vmax of the reaction increases
  • The binding affinity between substrate and enzyme decreases

    • What is the impact of competitive inhibition on Km and Vmax?

  • Km increases, Vmax remains the same
  • Both Km and Vmax decrease
  • Km increases, Vmax decreases (correct)
  • Km decreases, Vmax remains the same

    • Which type of reversible inhibition involves the inhibitor binding covalently to the enzyme?

    <p>Suicide inhibition</p> Signup and view all the answers

    What distinguishes irreversible inhibitors from reversible inhibitors?

    <p>Irreversible inhibitors permanently inactivate enzymes</p> Signup and view all the answers

    Which statement is true regarding suicide inhibitors?

    <p>They form covalent bonds with the enzyme during catalysis</p> Signup and view all the answers

    What role do pharmacological agents like aspirin play in enzyme activity?

    <p>They inhibit enzymes by influencing binding or turnover number</p> Signup and view all the answers

    In reversible inhibition, what happens when an equilibrium is established between free inhibitor and enzyme-inhibitor complex?

    <p>'Vmax/2' is affected while 'Km' remains constant</p> Signup and view all the answers

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