Chemistry A. Corti 10/01/2024 Lecture 7: Enzymes Pt2
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Questions and Answers

What is the Michaelis Menten constant (Km) defined as?

  • The substrate concentration that gives 50% of the maximum velocity (correct)
  • The time required for the enzyme to catalyze a reaction
  • The concentration of the enzyme in a saturated solution
  • The maximum velocity of the enzyme-substrate reaction

    • What does Vmax represent in the Michaelis Menten model?

  • The amount of substrate required for the enzyme to catalyze a reaction
  • The maximum velocity that can be obtained when the enzyme is saturated by the substrate (correct)
  • The maximum enzyme concentration in a reaction
  • The time taken for the enzyme to reach its maximum activity

    • How is the Michaelis Menten Model different from the time course of an enzymatic reaction graph?

  • The MM graph includes time and product on the x and y axes, whereas the time course graph includes substrate concentration and reaction velocity (correct)
  • The MM graph represents the rate of an enzymatic reaction, whereas the time course graph represents enzyme concentration
  • The MM graph is used to calculate Km, whereas the time course graph is used to calculate Vmax
  • The MM graph shows the initial velocity, whereas the time course graph shows the final velocity

    • What can be inferred from a high Vmax in an enzyme-catalyzed reaction?

    <p>The enzyme has high catalytic activity</p> Signup and view all the answers

    In which scenario can Vmax be achieved in an enzyme-catalyzed reaction?

    <p>At excessively high concentration of substrates</p> Signup and view all the answers

    How is the Michaelis Menten graph used to understand enzyme kinetics?

    <p>It illustrates how the rate of an enzymatic reaction depends on the concentration of the enzyme and substrate</p> Signup and view all the answers

    What is the purpose of plotting the reciprocal of the MM graph?

    <p>To find the Vmax</p> Signup and view all the answers

    What information does the Michaelis Menten constant (Km) provide about the enzyme kinetics?

    <p>Affinity of the enzymes for the substrate</p> Signup and view all the answers

    What is the definition of turnover number/catalytic constant (Kcat)?

    <p>The number of substrate molecules converted into product in a unit time by one enzyme molecule</p> Signup and view all the answers

    What happens when the enzyme is totally saturated by the substrate, in relation to Kcat?

    <p>Kcat remains constant</p> Signup and view all the answers

    How can Vmax be found using the MM graph?

    <p>By finding the x-intercept of the MM graph</p> Signup and view all the answers

    What is the relationship between K2 and Kcat in the equilibrium equation?

    <p>They are equal in value</p> Signup and view all the answers

    What does the specificity constant describe?

    <p>The ratio between Kcat and Km</p> Signup and view all the answers

    Why is it difficult to evaluate the Michaelis Menten constant (Km) using the MM graph?

    <p>Vmax is an unknown asymptote</p> Signup and view all the answers

    What aspect of enzyme performance does a low Km indicate?

    <p>High affinity for substrate</p> Signup and view all the answers

    'Highly efficient enzymes have a high Kcat and a low Km' - What does this statement imply?

    <p>Km is inversely proportional to Kcat</p> Signup and view all the answers

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