EBK CAMPBELL BIOLOGY
EBK CAMPBELL BIOLOGY
10th Edition
ISBN: 9780136539414
Author: Reece
Publisher: VST
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Chapter 9, Problem 8TYU
Summary Introduction

To analyze: The allosteric regulation of the enzyme phosphofructokinase by ATP and related molecules during glycolysis and to find whether the ATP that is considered to be allosteric regulator inhibits or stimulates the activity of the enzyme phosphofructokinase.

Concept introduction:

The enzyme phosphofructokinase plays its role in the most important regulatory step (energy investment step) of glycolysis. It converts fructose-6 phosphate to fructose-1,6 bisphosphate. The regulation of phosphofructokinase is said to be allosteric due to the binding of an effector molecule other than the enzyme's active site. Adenosine triphosphate (ATP) is known as the allosteric regulator for this enzyme in this step of glycolysis.

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Back in 1962, Gerhart and Pardee developed a model for the regulation of the activity of the ATCase enzyme by CTP and ATP, using the pathway given in Figure 1. Describe that model, using information presented here as well as what you have learned about allosteric enzymes. Be sure to include a sentence explaining the physiological significance of your model.
Focusing on the mechanism linking complex I and ATP synthase depicted in figure 3 in the article, compare that hypothetical mechanism to the classical presentation described in textbooks. What are the major differences between this mechanism and Peter Mitchel’s original chemiosmotic theory? What are the similarities.
Focusing on the mechanism linking complex I and ATP synthase depicted in figure 3 in the article, compare that hypothetical mechanism to the classical presentation described in our textbook. What are the major differences between this mechanism and Peter Mitchel’s original chemiosmotic theory? What are the similarities.

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EBK CAMPBELL BIOLOGY

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