Q. How do allosteric activators affect enzyme kinetics?
-
A.
Increase Vmax
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B.
Decrease Km
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C.
Both A and B
-
D.
No effect on Vmax or Km
Solution
Allosteric activators can increase Vmax and decrease Km, enhancing enzyme activity.
Correct Answer:
C
— Both A and B
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Q. What effect does an allosteric activator have on enzyme activity?
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A.
Decreases enzyme activity
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B.
Increases enzyme activity
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C.
Has no effect
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D.
Inhibits substrate binding
Solution
An allosteric activator increases enzyme activity by enhancing the enzyme's affinity for its substrate.
Correct Answer:
B
— Increases enzyme activity
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Q. What is an allosteric site?
-
A.
A site where substrates bind
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B.
A site that regulates enzyme activity
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C.
A site for product release
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D.
A site for DNA binding
Solution
An allosteric site is a regulatory site on an enzyme that can bind molecules and influence the enzyme's activity.
Correct Answer:
B
— A site that regulates enzyme activity
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Q. What is the effect of allosteric inhibition on enzyme activity?
-
A.
Increases substrate affinity
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B.
Decreases enzyme activity
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C.
Increases product formation
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D.
Has no effect on enzyme structure
Solution
Allosteric inhibition decreases enzyme activity by altering the enzyme's conformation.
Correct Answer:
B
— Decreases enzyme activity
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Q. What is the primary role of allosteric enzymes in metabolic pathways?
-
A.
To catalyze irreversible reactions
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B.
To provide feedback inhibition
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C.
To enhance substrate binding
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D.
To stabilize the transition state
Solution
Allosteric enzymes often provide feedback inhibition, regulating metabolic pathways based on product concentration.
Correct Answer:
B
— To provide feedback inhibition
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Q. Which of the following best describes the effect of allosteric regulation?
-
A.
It is a permanent change in enzyme structure.
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B.
It involves binding at a site other than the active site.
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C.
It only occurs in competitive inhibition.
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D.
It is only relevant in prokaryotic organisms.
Solution
Allosteric regulation involves binding at a site other than the active site, leading to changes in enzyme activity.
Correct Answer:
B
— It involves binding at a site other than the active site.
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Q. Which of the following is a common allosteric effector in glycolysis?
-
A.
Fructose-1,6-bisphosphate
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B.
Glucose
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C.
NAD+
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D.
Citrate
Solution
Fructose-1,6-bisphosphate is a common allosteric effector that activates phosphofructokinase in glycolysis.
Correct Answer:
A
— Fructose-1,6-bisphosphate
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Q. Which of the following is an example of an allosteric inhibitor?
-
A.
ATP
-
B.
Citrate
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C.
ADP
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D.
NADH
Solution
Citrate acts as an allosteric inhibitor of phosphofructokinase, regulating glycolysis.
Correct Answer:
B
— Citrate
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Q. Which of the following is NOT a characteristic of allosteric enzymes?
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A.
Sigmoidal kinetics
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B.
Cooperativity
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C.
Michaelis-Menten kinetics
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D.
Regulation by effectors
Solution
Allosteric enzymes typically exhibit sigmoidal kinetics and do not follow Michaelis-Menten kinetics.
Correct Answer:
C
— Michaelis-Menten kinetics
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