Campbell Biology Custom Stony Brook 10 Th Edition
Campbell Biology Custom Stony Brook 10 Th Edition
10th Edition
ISBN: 9781269870818
Author: Reece Urry Cain Wasserman Minorsky Jackson
Publisher: PEARSON
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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.
. In another key reaction in glycolysis, dihydroxyacetone phosphate (DHAP) is isomerized into glyceraldehyde-3-phosphate (GAP) Because ∆G°′ is positive, the equilibrium lies to the left. (a) Calculate the equilibrium constant and the equilibrium fraction of GAP from the above, at 37 °C. (b) In the cell, depletion of GAP makes the reaction proceed. What will ∆G be if the concentration of GAP is always kept at 1/100 of the concentration of DHAP?
Predict the effect of each of the following mutations on the pace of glycolysis in liver cells: (a) Loss of the allosteric site for ATP in phosphofructokinase (b) Loss of the binding site for citrate in phosphofructokinase (c) Loss of the phosphatase domain of the bifunctional enzyme that controls the level of fructose 2,6-bisphosphate (d) Loss of the binding site for fructose 1,6-bisphosphate in pyruvate kinase

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Campbell Biology Custom Stony Brook 10 Th Edition

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