Kinetics Continued
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Questions and Answers

Which enzyme, glucokinase or hexokinase, has a lower Vmax?

  • Both have the same Vmax
  • Glucokinase (correct)
  • It is not mentioned in the text
  • Hexokinase

Which enzyme, glucokinase or hexokinase, has a lower Km?

  • It is not mentioned in the text
  • Glucokinase
  • Both have the same Km
  • Hexokinase (correct)

Which enzyme, glucokinase or hexokinase, is turned off by high concentrations of glucose-6-P?

  • Hexokinase
  • It is not mentioned in the text
  • Glucokinase (correct)
  • Both enzymes are turned off by glucose-6-P

What same reaction do both hexokinase and glucokinase catalyze?

<p>Conversion of glucose to glucose-6-P (A)</p> Signup and view all the answers

Which enzyme, glucokinase or hexokinase, has a higher Km and is active even during fasting?

<p>Glucokinase (C)</p> Signup and view all the answers

Which enzyme, glucokinase or hexokinase, becomes active after a high-carbohydrate meal?

<p>Hexokinase (A)</p> Signup and view all the answers

What is the main role of the enzyme glucokinase?

<p>Glycogenesis (D)</p> Signup and view all the answers

Which enzyme is found in the liver?

<p>Glucokinase (A)</p> Signup and view all the answers

Why can't other tissues convert excess glucose to glycogen?

<p>They lack the enzyme glucokinase (D)</p> Signup and view all the answers

Which enzyme, glucokinase or hexokinase, is inhibited by glucose-6-P?

<p>Hexokinase (B)</p> Signup and view all the answers

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

<p>Irreversible Enzyme Inhibition (D)</p> Signup and view all the answers

Which type of enzyme inhibition competitively inhibits the enzyme that helps convert folate (B9) into its coenzyme form?

<p>Reversible Enzyme Inhibition: Competitive (D)</p> Signup and view all the answers

In reversible enzyme inhibition, which type of inhibition does not change the maximum velocity (Vmax) of the reaction?

<p>Reversible Enzyme Inhibition: Competitive (D)</p> Signup and view all the answers

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

<p>The affinity of the enzyme appears to go down (D)</p> Signup and view all the answers

Which type of enzyme inhibition results in no product formation even in the presence of substrate?

<p>Reversible Enzyme Inhibition: Noncompetitive (B)</p> Signup and view all the answers

In reversible enzyme inhibition, is the maximum velocity (Vmax) lower or higher in the presence of the inhibitor?

<p>The maximum velocity (Vmax) is lower (D)</p> Signup and view all the answers

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

<p>The affinity of the enzyme appears to go down (B)</p> Signup and view all the answers

Which type of enzyme inhibition occurs when the inhibitor binds to the enzyme or the enzyme-substrate complex?

<p>Reversible Enzyme Inhibition: Noncompetitive (D)</p> Signup and view all the answers

In reversible enzyme inhibition, does the maximum velocity (Vmax) change in the presence of the inhibitor?

<p>The maximum velocity (Vmax) remains unchanged (C)</p> Signup and view all the answers

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

<p>The affinity of the enzyme remains unchanged (B)</p> Signup and view all the answers

Which of the following defines Km and Vmax?

<p>The concentration of substrate at which the enzyme is working at half of its maximum velocity and the maximum velocity of the reaction (D)</p> Signup and view all the answers

Which of the following reactions conforms to Michaelis-Menten kinetics?

<p>A zero order reaction (B)</p> Signup and view all the answers

What is the difference between glucokinase and hexokinase?

<p>Glucokinase has a higher Km value than hexokinase (C)</p> Signup and view all the answers

What does Kcat represent?

<p>The ratio of the catalytic rate constant to the dissociation constant of the enzyme-substrate complex (B)</p> Signup and view all the answers

Which of the following is an example of a physiologically efficient enzyme and its role?

<p>Glucokinase, which catalyzes the phosphorylation of glucose in the liver (A)</p> Signup and view all the answers

How can we determine the Km and Vmax of an enzyme using Michaelis-Menten kinetics?

<p>By measuring the initial reaction rate at different substrate concentrations and fitting the data to the Michaelis-Menten equation (D)</p> Signup and view all the answers

What is the difference between reversible and irreversible enzyme inhibition?

<p>Reversible inhibition can be overcome by increasing the substrate concentration, while irreversible inhibition cannot (D)</p> Signup and view all the answers

What is the difference between competitive, uncompetitive, and non-competitive inhibition?

<p>Competitive inhibition occurs when the inhibitor binds to the active site of the enzyme, uncompetitive inhibition occurs when the inhibitor binds to the enzyme-substrate complex, and non-competitive inhibition occurs when the inhibitor binds to a site other than the active site (A)</p> Signup and view all the answers

How does the graph of an allosteric enzyme in the presence of an inhibitor differ from the graph in the absence of an inhibitor?

<p>The graph in the presence of an inhibitor is shifted to the right, indicating a decrease in enzyme activity (D)</p> Signup and view all the answers

Which of the following best defines Km in Michaelis-Menten kinetics?

<p>The concentration of substrate at which the reaction rate is half of Vmax (B)</p> Signup and view all the answers

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

<p>The reaction rate is directly proportional to the concentration of the substrate (B)</p> Signup and view all the answers

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

<p>The reaction rate is independent of the concentration of the substrate (D)</p> Signup and view all the answers

What can we use a Lineweaver-Burk plot for?

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

Which of the following best defines Kcat?

<p>The turnover number of the enzyme (A)</p> Signup and view all the answers

Which of the following best describes reversible enzyme inhibition?

<p>The inhibitor binds to the enzyme or the enzyme-substrate complex (A)</p> Signup and view all the answers

Which of the following best describes irreversible enzyme inhibition?

<p>The inhibitor permanently inactivates the enzyme (A)</p> Signup and view all the answers

Which of the following best describes allosteric inhibition?

<p>The inhibitor binds to a site other than the active site of the enzyme (B)</p> Signup and view all the answers

Which of the following best describes competitive inhibition?

<p>The inhibitor competes with the substrate for binding to the active site of the enzyme (C)</p> Signup and view all the answers

Which of the following best describes uncompetitive inhibition?

<p>The inhibitor binds to the enzyme or the enzyme-substrate complex (A)</p> Signup and view all the answers

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