There are multiple options for answers to click on. In the presence of saturating amounts of oxaloacetate, theactivity of citrate synthase from pig heart tissue shows asigmoid dependence on the concentration of acetyl-CoA.When succinyl-CoA is added, the curve shifts to the right andthe sigmoid dependence is more pronounced.Choose the statements that are reasonable explanationsfor the right-ward shift of the velocity curve causedby succinyl-CoA.Succinyl-CoA competes with oxaloacetate forbinding at the active site.Succinyl-CoA competes with acetyl-CoA forbinding at the active site.Succinyl-CoA binds at a regulatory site other thanthe active site.Succinyl-CoA binds covalently to the enzyme.Succinyl-CoA competes with dissociation of CoA asa product of the reaction.Activity (% of Vmax)100F No80-60-40succinyl-CoAIadded20Succinyl-CoAL1120 40 60 80 100 120[Acetyl-CoA] (μm)

Citrate synthase is an enzyme of the citric acid cycle , also called the Tricarboxylic acid cycle…

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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