Enzyme Kinetics Lineweaver-Burk Plot
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Questions and Answers

What is the relationship between the substrate concentration and the reaction rate when the enzyme is saturated with substrate?

  • The reaction rate is inversely proportional to the substrate concentration.
  • The reaction rate is independent of the substrate concentration. (correct)
  • The reaction rate increases exponentially with the substrate concentration.
  • The reaction rate is directly proportional to the substrate concentration.
  • What is the purpose of the Lineweaver-Burk plot?

  • To determine the maximum reaction velocity (Vmax) and the Michaelis constant (Km) of an enzyme. (correct)
  • To determine the affinity of the enzyme for the substrate.
  • To determine the rate-limiting step in the enzymatic reaction.
  • To determine the order of the reaction with respect to the substrate concentration.
  • What is the significance of the x-intercept in the Lineweaver-Burk plot?

  • It represents the value of Km.
  • It represents the value of the substrate concentration at which the reaction velocity is half of the maximum.
  • It represents the value of -1/Km. (correct)
  • It represents the value of 1/Vmax.
  • Why is it not always possible to determine the maximum reaction velocity (Vmax) from a plot of reaction velocity (vo) against substrate concentration ([S])?

    <p>Because the plot has a gradual upward slope at high substrate concentrations.</p> Signup and view all the answers

    What information can be obtained from the slope of the Lineweaver-Burk plot?

    <p>The ratio of Km to Vmax.</p> Signup and view all the answers

    What is the relationship between the Michaelis constant (Km) and the affinity of an enzyme for its substrate?

    <p>The lower the Km, the higher the affinity of the enzyme for the substrate.</p> Signup and view all the answers

    What happens to the reaction rate when the substrate concentration is increased, while keeping the enzyme concentration constant?

    <p>The reaction rate increases until a saturation point is reached, after which it remains constant</p> Signup and view all the answers

    What is the relationship between the reaction velocity and substrate concentration at low substrate concentrations?

    <p>The reaction velocity is directly proportional to the substrate concentration</p> Signup and view all the answers

    What does the saturation point in the enzyme kinetics curve represent?

    <p>The point where all active sites on the enzyme are occupied by the substrate</p> Signup and view all the answers

    What information can be obtained from a Lineweaver-Burk plot for an enzyme-catalyzed reaction?

    <p>The maximum reaction velocity ($V_{max}$) and the Michaelis constant ($K_m$)</p> Signup and view all the answers

    What does a high value of the Michaelis constant ($K_m$) indicate about an enzyme?

    <p>The enzyme has a low affinity for the substrate</p> Signup and view all the answers

    What is the order of the enzyme-catalyzed reaction with respect to the substrate concentration at low substrate concentrations?

    <p>First order</p> Signup and view all the answers

    What does Km represent in the context of the Michaelis-Menten equation?

    <p>The substrate concentration at which the reaction velocity is half of the maximum velocity</p> Signup and view all the answers

    How does an increase in substrate concentration affect the enzyme's reaction velocity according to the Michaelis-Menten equation?

    <p>Increases until it reaches Vmax, then decreases</p> Signup and view all the answers

    In the context of enzyme kinetics, what does Vmax represent?

    <p>The maximum velocity the enzyme can reach in a reaction</p> Signup and view all the answers

    What does the Lineweaver-Burk plot analyze in enzyme kinetics?

    <p>Reaction velocity at different substrate concentrations</p> Signup and view all the answers

    What assumption is made about the rate of back reaction from product to substrate when deriving the Michaelis-Menten rate equation?

    <p>It is negligible because k-2 is approximately 0</p> Signup and view all the answers

    What does Michaelis constant Km calculate in enzyme kinetics?

    <p>Substrate concentration at half of the maximum velocity</p> Signup and view all the answers

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