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 L 20 40 60 80 100 120 [Acetyl-CoA] (μm)

Biochemistry
6th Edition
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Reginald H. Garrett, Charles M. Grisham
Chapter18: Glycolysis
Section: Chapter Questions
Problem 20P: Understanding the Mechanism of Hemolytic Anemia Genetic defects in glycolytic enzymes can have...
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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)
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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