Kinetics Continued

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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?

Conversion of glucose to glucose-6-P Signup and view all the answers

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

Glucokinase Signup and view all the answers

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

Hexokinase Signup and view all the answers

What is the main role of the enzyme glucokinase?

Glycogenesis Signup and view all the answers

Which enzyme is found in the liver?

Glucokinase Signup and view all the answers

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

They lack the enzyme glucokinase Signup and view all the answers

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

Hexokinase 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?

Irreversible Enzyme Inhibition Signup and view all the answers

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

Reversible Enzyme Inhibition: Competitive Signup and view all the answers

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

Reversible Enzyme Inhibition: Competitive 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?

The affinity of the enzyme appears to go down Signup and view all the answers

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

Reversible Enzyme Inhibition: Noncompetitive Signup and view all the answers

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

The maximum velocity (Vmax) is lower 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?

The affinity of the enzyme appears to go down Signup and view all the answers

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

Reversible Enzyme Inhibition: Noncompetitive Signup and view all the answers

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

The maximum velocity (Vmax) remains unchanged 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?

The affinity of the enzyme remains unchanged Signup and view all the answers

Which of the following defines Km and Vmax?

The concentration of substrate at which the enzyme is working at half of its maximum velocity and the maximum velocity of the reaction Signup and view all the answers

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

A zero order reaction Signup and view all the answers

What is the difference between glucokinase and hexokinase?

Glucokinase has a higher Km value than hexokinase Signup and view all the answers

What does Kcat represent?

The ratio of the catalytic rate constant to the dissociation constant of the enzyme-substrate complex Signup and view all the answers

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

Glucokinase, which catalyzes the phosphorylation of glucose in the liver Signup and view all the answers

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

By measuring the initial reaction rate at different substrate concentrations and fitting the data to the Michaelis-Menten equation Signup and view all the answers

What is the difference between reversible and irreversible enzyme inhibition?

Reversible inhibition can be overcome by increasing the substrate concentration, while irreversible inhibition cannot Signup and view all the answers

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

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 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?

The graph in the presence of an inhibitor is shifted to the right, indicating a decrease in enzyme activity Signup and view all the answers

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

The concentration of substrate at which the reaction rate is half of Vmax Signup and view all the answers

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

The reaction rate is directly proportional to the concentration of the substrate Signup and view all the answers

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

The reaction rate is independent of the concentration of the substrate Signup and view all the answers

What can we use a Lineweaver-Burk plot for?

To determine the Km and Vmax of an enzyme Signup and view all the answers

Which of the following best defines Kcat?

The turnover number of the enzyme Signup and view all the answers

Which of the following best describes reversible enzyme inhibition?

The inhibitor binds to the enzyme or the enzyme-substrate complex Signup and view all the answers

Which of the following best describes irreversible enzyme inhibition?

The inhibitor permanently inactivates the enzyme Signup and view all the answers

Which of the following best describes allosteric inhibition?

The inhibitor binds to a site other than the active site of the enzyme Signup and view all the answers

Which of the following best describes competitive inhibition?

The inhibitor competes with the substrate for binding to the active site of the enzyme Signup and view all the answers

Which of the following best describes uncompetitive inhibition?

The inhibitor binds to the enzyme or the enzyme-substrate complex Signup and view all the answers

Kinetics Continued

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Questions and Answers

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

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

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

What same reaction do both hexokinase and glucokinase catalyze?

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

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

What is the main role of the enzyme glucokinase?

Which enzyme is found in the liver?

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

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

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

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

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

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

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

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

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

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

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

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

Which of the following defines Km and Vmax?

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

What is the difference between glucokinase and hexokinase?

What does Kcat represent?

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

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

What is the difference between reversible and irreversible enzyme inhibition?

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

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

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

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

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

What can we use a Lineweaver-Burk plot for?

Which of the following best defines Kcat?

Which of the following best describes reversible enzyme inhibition?

Which of the following best describes irreversible enzyme inhibition?

Which of the following best describes allosteric inhibition?

Which of the following best describes competitive inhibition?

Which of the following best describes uncompetitive inhibition?

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