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.
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.
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
Problem 1P
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![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 competes with oxaloacetate for
binding at the active site.
Succinyl-CoA competes with acetyl-CoA for
binding at the active site.
Succinyl-CoA binds at a regulatory site other than
the active site.
Succinyl-CoA binds covalently to the enzyme.
Succinyl-CoA competes with dissociation of CoA as
a product of the reaction.
Activity (% of Vmax)
100F No
80-
60-
40
succinyl-CoA
I
added
20
Succinyl-CoA
L
1
1
20 40 60 80 100 120
[Acetyl-CoA] (μm)](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F13a5a00a-4cb0-4c6a-93d2-f1168bf2c021%2Fd6d4cdd3-a33a-4b90-84f3-0ebe60810d59%2Fvglrsyv_processed.jpeg&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 competes with oxaloacetate for
binding at the active site.
Succinyl-CoA competes with acetyl-CoA for
binding at the active site.
Succinyl-CoA binds at a regulatory site other than
the active site.
Succinyl-CoA binds covalently to the enzyme.
Succinyl-CoA competes with dissociation of CoA as
a product of the reaction.
Activity (% of Vmax)
100F No
80-
60-
40
succinyl-CoA
I
added
20
Succinyl-CoA
L
1
1
20 40 60 80 100 120
[Acetyl-CoA] (μm)
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