30 Questions
Which enzyme has a lower Vmax compared to glucokinase?
Hexokinase
Which enzyme has a lower Km compared to glucokinase?
Hexokinase
Which enzyme is turned off by high concentrations of glucose-6-P?
Glucokinase
What same reaction do both hexokinase and glucokinase catalyze?
Convert glucose to G-6P
What is the product of the reaction catalyzed by hexokinase and glucokinase used for?
Glycogenesis
Which line in the graph represents glucokinase?
Red
Which intercept represents Vmax?
A
Which intercept represents 1/2 Vmax?
C
Which intercept represents Km?
D
What does the higher Km of glucokinase tell you about its affinity for glucose compared to hexokinase?
Glucokinase has lower affinity for glucose
Which type of enzyme inhibition occurs when an inhibitor forms a covalent bond with the active site of the enzyme?
Irreversible inhibition
What type of inhibition occurs when an inhibitor binds to the active site of the enzyme and competes with the substrate for binding?
Competitive inhibition
In competitive inhibition, does the affinity of the enzyme appear to go up or down in the presence of the inhibitor?
Affinity remains the same
What type of inhibition occurs when an inhibitor binds to the enzyme-substrate complex and prevents the release of the product?
Uncompetitive inhibition
In uncompetitive inhibition, is Vmax lower or higher in the presence of the inhibitor?
Vmax is lower
What type of inhibition occurs when an inhibitor binds to the enzyme or the enzyme-substrate complex at a site other than the active site?
Noncompetitive inhibition
In noncompetitive inhibition, is Vmax lower or higher in the presence of the inhibitor?
Vmax is lower
What happens when an activator binds to a multi-subunit allosteric enzyme?
The enzyme becomes more active
What effect does an inhibitor have on the substrate graph of a multi-subunit allosteric enzyme?
The graph shifts to the right
What does the term 'allosteric inhibition' tell us about where an inhibitor binds when it is acting as an inhibitor?
It binds to an allosteric site
Which of the following is NOT an objective of the Kinetics section?
Determine the Km and Vmax of an enzyme
What is the main purpose of a Lineweaver-Burk plot?
To determine the Km and Vmax of an enzyme
Which of the following reactions conforms to Michaelis-Menten kinetics?
Pseudo-first order reaction
What is the difference between glucokinase and hexokinase?
All of the above
What does Kcat represent?
The maximum rate of the enzyme-catalyzed reaction
Which of the following is an example of physiologically efficient enzyme?
All of the above
What is the difference between competitive, uncompetitive, and non-competitive inhibition?
Competitive inhibition occurs when the inhibitor binds to the active site, 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
How does the graph of an allosteric enzyme change in the presence of an inhibitor?
The graph shifts to the right
What is happening in a first order reaction?
The rate of the reaction is directly proportional to the concentration of the reactant
What is happening in a zero-order reaction?
The rate of the reaction remains constant over time
Test your knowledge on enzymes kinetics and objectives in this quiz. Learn about Km, Vmax, first order reactions, pseudo-first order reactions, and zero order reactions.
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