Enzyme Inhibitors and Lineweaver-Burk Plots
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Questions and Answers

What is the effect of a competitive inhibitor on the apparent Km of an enzyme?

  • It is increased (correct)
  • It is decreased
  • It is unchanged
  • It becomes zero

    • What happens to the reaction velocity when the concentration of substrate is increased in the presence of a competitive inhibitor?

  • It decreases
  • It reaches Vmax (correct)
  • It becomes zero
  • It remains unaffected

    • What is the effect of non-competitive inhibitors on the binding of substrate to enzyme?

  • They bind to the active site of the enzyme
  • They have no effect on the binding of substrate to enzyme (correct)
  • They increase the binding of substrate to enzyme
  • They decrease the binding of substrate to enzyme

    • What is the point of intersection between the plots of inhibited and uninhibited reactions in a Lineweaver-Burk plot?

    <p>The y-axis at 1/Vmax</p> Signup and view all the answers

    What is the result of increasing the substrate concentration in the presence of uncompetitive inhibitors?

    <p>The inhibition is increased</p> Signup and view all the answers

    What is a potential limitation of enzyme activity measurements?

    <p>All of the above</p> Signup and view all the answers

    What is the purpose of maintaining a constant pH during enzyme concentration measurements?

    <p>To ensure accurate enzyme activity measurements</p> Signup and view all the answers

    What is the effect of non-competitive inhibitors on Vmax?

    <p>It is decreased</p> Signup and view all the answers

    What is the effect of non-competitive inhibitors on Km?

    <p>It is unchanged</p> Signup and view all the answers

    What is the principle of the fixed-time assay method?

    <p>Reactants are combined, reaction proceeds for a designated time, and then the reaction is stopped</p> Signup and view all the answers

    How do uncompetitive inhibitors differ from competitive inhibitors?

    <p>Uncompetitive inhibitors are not overcome by increasing substrate concentration, while competitive inhibitors are</p> Signup and view all the answers

    What is the advantage of continuous-monitoring or kinetic assays?

    <p>They can be used to measure substrate depletion</p> Signup and view all the answers

    What is the effect of increasing substrate concentration on competitive inhibition?

    <p>Inhibition is partially reversed</p> Signup and view all the answers

    What type of bond is formed between a reversible inhibitor and an enzyme?

    <p>Noncovalent bond</p> Signup and view all the answers

    What happens when the concentration of substrate is significantly higher than the concentration of a competitive inhibitor?

    <p>Inhibition is partially reversed</p> Signup and view all the answers

    What is the characteristic of non-competitive inhibitors?

    <p>They bind to an allosteric site</p> Signup and view all the answers

    What is the effect of increasing substrate concentration on uncompetitive inhibition?

    <p>Inhibition is increased</p> Signup and view all the answers

    What is the characteristic of mixed inhibitors?

    <p>They bind to either E or ES complex</p> Signup and view all the answers

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