In the presence of saturating amounts of oxaloacetate, the activity of citrate synthase from pig heart tissue shows a sigmoid dependence on the concentration of acetyl-CoA. When succinyl-CoA is added, the curve shifts to the right and the sigmoid dependence is more pronounced. Choose the statements that are reasonable explanations for the right-ward shift of the velocity curve caused by succinyl-CoA. Succinyl-CoA binds at a regulatory site other than the active site. Succinyl-CoA competes with oxaloacetate for binding at the active site. Succinyl-CoA competes with dissociation of CoA as a product of the reaction. Succinyl-CoA binds covalently to the enzyme. ☐ Succinyl-CoA competes with acetyl-CoA for binding at the active site. Activity (% of Vmax) 100F No 80- 60- 40- 20- succinyl-CoA D Succinyl-CoA added 20 40 60 80 100 120 [Acetyl-CoA] (µM) Citrate synthase is regulated by another metabolite that has the opposite effect (i.e., stimulates citrate synthase). Choose the description of a condition where a positive regulator activates citrate synthase. High [citrate]. Citrate is a positive allosteric activator. High [NADH/NAD+] ratio. NADH is a positive allosteric activator. ☐ High [ATP/ADP] ratio. High ATP substrate levels favor product formation. Low [ATP/ADP] ratio. ADP is an allosteric activator of citrate synthase.
In the presence of saturating amounts of oxaloacetate, the activity of citrate synthase from pig heart tissue shows a sigmoid dependence on the concentration of acetyl-CoA. When succinyl-CoA is added, the curve shifts to the right and the sigmoid dependence is more pronounced. Choose the statements that are reasonable explanations for the right-ward shift of the velocity curve caused by succinyl-CoA. Succinyl-CoA binds at a regulatory site other than the active site. Succinyl-CoA competes with oxaloacetate for binding at the active site. Succinyl-CoA competes with dissociation of CoA as a product of the reaction. Succinyl-CoA binds covalently to the enzyme. ☐ Succinyl-CoA competes with acetyl-CoA for binding at the active site. Activity (% of Vmax) 100F No 80- 60- 40- 20- succinyl-CoA D Succinyl-CoA added 20 40 60 80 100 120 [Acetyl-CoA] (µM) Citrate synthase is regulated by another metabolite that has the opposite effect (i.e., stimulates citrate synthase). Choose the description of a condition where a positive regulator activates citrate synthase. High [citrate]. Citrate is a positive allosteric activator. High [NADH/NAD+] ratio. NADH is a positive allosteric activator. ☐ High [ATP/ADP] ratio. High ATP substrate levels favor product formation. Low [ATP/ADP] ratio. ADP is an allosteric activator of citrate synthase.
Chemistry
10th Edition
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Chapter1: Chemical Foundations
Section: Chapter Questions
Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...
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Question
![In the presence of saturating amounts of oxaloacetate, the
activity of citrate synthase from pig heart tissue shows a
sigmoid dependence on the concentration of acetyl-CoA.
When succinyl-CoA is added, the curve shifts to the right and
the sigmoid dependence is more pronounced.
Choose the statements that are reasonable explanations
for the right-ward shift of the velocity curve caused
by succinyl-CoA.
Succinyl-CoA binds at a regulatory site other than
the active site.
Succinyl-CoA competes with oxaloacetate for
binding at the active site.
Succinyl-CoA competes with dissociation of CoA as
a product of the reaction.
Succinyl-CoA binds covalently to the enzyme.
☐ Succinyl-CoA competes with acetyl-CoA for
binding at the active site.
Activity (% of Vmax)
100F No
80-
60-
40-
20-
succinyl-CoA
D
Succinyl-CoA
added
20 40 60 80 100 120
[Acetyl-CoA] (µM)](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fdc07c092-5f49-4d93-b501-b08294061775%2F86c60a95-08a6-45fb-bc2c-3778bff6eb27%2F3454229_processed.png&w=3840&q=75)
Transcribed Image Text:In the presence of saturating amounts of oxaloacetate, the
activity of citrate synthase from pig heart tissue shows a
sigmoid dependence on the concentration of acetyl-CoA.
When succinyl-CoA is added, the curve shifts to the right and
the sigmoid dependence is more pronounced.
Choose the statements that are reasonable explanations
for the right-ward shift of the velocity curve caused
by succinyl-CoA.
Succinyl-CoA binds at a regulatory site other than
the active site.
Succinyl-CoA competes with oxaloacetate for
binding at the active site.
Succinyl-CoA competes with dissociation of CoA as
a product of the reaction.
Succinyl-CoA binds covalently to the enzyme.
☐ Succinyl-CoA competes with acetyl-CoA for
binding at the active site.
Activity (% of Vmax)
100F No
80-
60-
40-
20-
succinyl-CoA
D
Succinyl-CoA
added
20 40 60 80 100 120
[Acetyl-CoA] (µM)
![Citrate synthase is regulated by another metabolite that has
the opposite effect (i.e., stimulates citrate synthase).
Choose the description of a condition where a positive
regulator activates citrate synthase.
High [citrate]. Citrate is a positive
allosteric activator.
High [NADH/NAD+] ratio. NADH is a positive
allosteric activator.
☐ High [ATP/ADP] ratio. High ATP substrate levels
favor product formation.
Low [ATP/ADP] ratio. ADP is an allosteric activator
of citrate synthase.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fdc07c092-5f49-4d93-b501-b08294061775%2F86c60a95-08a6-45fb-bc2c-3778bff6eb27%2F4w6ocut_processed.png&w=3840&q=75)
Transcribed Image Text:Citrate synthase is regulated by another metabolite that has
the opposite effect (i.e., stimulates citrate synthase).
Choose the description of a condition where a positive
regulator activates citrate synthase.
High [citrate]. Citrate is a positive
allosteric activator.
High [NADH/NAD+] ratio. NADH is a positive
allosteric activator.
☐ High [ATP/ADP] ratio. High ATP substrate levels
favor product formation.
Low [ATP/ADP] ratio. ADP is an allosteric activator
of citrate synthase.
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