Biochem 7: Enzyme Kinetics
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Questions and Answers

Which enzyme is active even during fasting?

  • Hexokinase (correct)
  • Neither Glucokinase nor Hexokinase
  • Glucokinase
  • Both Glucokinase and Hexokinase
  • Which enzyme needs lots of glucose to be activated?

  • Neither Glucokinase nor Hexokinase
  • Glucokinase (correct)
  • Both Glucokinase and Hexokinase
  • Hexokinase
  • What is the main role of glucokinase and hexokinase?

  • Both Glycolysis and Glycogenesis (correct)
  • Neither Glycolysis nor Glycogenesis
  • Glycolysis
  • Glycogenesis
  • What pathway does hexokinase feed into if it can't do glycogenesis?

    <p>Glycolysis</p> Signup and view all the answers

    What does a low Km value indicate for an enzyme?

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

    Why is hexokinase inhibited by glucose-6-P, but glucokinase is not?

    <p>Glucokinase has a lower Km</p> Signup and view all the answers

    What is the general purpose of very efficient enzymes?

    <p>Catalyzing important physiological reactions</p> Signup and view all the answers

    What are some applications of enzyme inhibition?

    <p>Modulating enzyme activity</p> Signup and view all the answers

    What type of reversible enzyme inhibition is characterized by binding of the inhibitor to the active site of the enzyme?

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

    What does competitive inhibition do to the affinity of the enzyme for its substrate?

    <p>Decreases affinity</p> Signup and view all the answers

    Which type of reversible enzyme inhibition involves binding of the inhibitor to the enzyme-substrate complex (ES)?

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

    In uncompetitive inhibition, is the maximum reaction rate (Vmax) lower or higher in the presence of the inhibitor?

    <p>Lower</p> Signup and view all the answers

    Does the affinity of the enzyme appear to go up or down in the presence of an uncompetitive inhibitor?

    <p>Up</p> Signup and view all the answers

    Which type of reversible enzyme inhibition involves binding of the inhibitor to either the enzyme or the enzyme-substrate complex (ES)?

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

    In noncompetitive inhibition, is the maximum reaction rate (Vmax) lower or higher in the presence of the inhibitor?

    <p>Lower</p> Signup and view all the answers

    In noncompetitive inhibition, does the affinity of the enzyme appear to go up or down in the presence of the inhibitor?

    <p>Down</p> Signup and view all the answers

    Which type of reversible enzyme inhibition involves binding of the inhibitor to the enzyme but not at the active site?

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

    In mixed inhibition, is the maximum reaction rate (Vmax) lower or higher in the presence of the inhibitor?

    <p>Lower</p> Signup and view all the answers

    In mixed inhibition, does the affinity of the enzyme appear to go up or down in the presence of the inhibitor?

    <p>Down</p> Signup and view all the answers

    Which type of enzyme inhibition occurs when an inhibitor forms a covalent bond with the active site of the enzyme?

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

    Which of the following best describes a first-order reaction?

    <p>The rate of the reaction is directly proportional to the concentration of the reactant.</p> Signup and view all the answers

    What is the key difference between glucokinase and hexokinase?

    <p>Hexokinase has a lower Vmax and a lower Km compared to glucokinase.</p> Signup and view all the answers

    What is the purpose of a Lineweaver-Burk plot?

    <p>To determine the Km and Vmax of an enzyme.</p> Signup and view all the answers

    Which of the following best describes a zero-order reaction?

    <p>The rate of the reaction remains constant regardless of the concentration of the reactant.</p> Signup and view all the answers

    What is the definition of Km in Michaelis-Menten kinetics?

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

    What is the definition of Vmax in Michaelis-Menten kinetics?

    <p>The maximum velocity of the reaction.</p> Signup and view all the answers

    Which of the following best describes reversible inhibition?

    <p>The inhibitor binds reversibly to the enzyme.</p> Signup and view all the answers

    Which of the following best describes irreversible inhibition?

    <p>The inhibitor binds irreversibly to the enzyme.</p> Signup and view all the answers

    Which of the following best describes competitive inhibition?

    <p>The inhibitor binds to a different site on the enzyme.</p> Signup and view all the answers

    Which of the following best describes non-competitive inhibition?

    <p>The inhibitor does not affect the activity of the enzyme.</p> Signup and view all the answers

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