A direct measurement of the standard free-energy change associated with the hydrolysis of ATP is technically very demanding because the minute amount of ATP remaining at equilibrium is difficult to measure accurately. However, the value of AG'o for ATP hydrolysis can be calculated indirectly, from the equilibrium constants of two other enzymatic reactions having less favourable equilibrium constants: Glucose-6-phosphate + H20 = glucose + Pi K'eq = 271 (1) %3D ATP + glucose = ADP + glucose-6-phosphate K'eg = 889 (2) %3D Use this information to determine the value for AG'o for the hydrolysis of ATP at 25°C. Justify the method used.
A direct measurement of the standard free-energy change associated with the hydrolysis of ATP is technically very demanding because the minute amount of ATP remaining at equilibrium is difficult to measure accurately. However, the value of AG'o for ATP hydrolysis can be calculated indirectly, from the equilibrium constants of two other enzymatic reactions having less favourable equilibrium constants: Glucose-6-phosphate + H20 = glucose + Pi K'eq = 271 (1) %3D ATP + glucose = ADP + glucose-6-phosphate K'eg = 889 (2) %3D Use this information to determine the value for AG'o for the hydrolysis of ATP at 25°C. Justify the method used.
Introduction to General, Organic and Biochemistry
11th Edition
ISBN:9781285869759
Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres
Publisher:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres
Chapter7: Reaction Rates And Chemical Equilibrium
Section: Chapter Questions
Problem 7.64P: 7-64 As we shall see in Chapter 20, there are two forms of glucose, designated alpha and betawhich...
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Transcribed Image Text:A direct measurement of the standard free-energy change associated with the
hydrolysis of ATP is technically very demanding because the minute amount of ATP
remaining at equilibrium is difficult to measure accurately. However, the value of AG'o
for ATP hydrolysis can be calculated indirectly, from the equilibrium constants of two
other enzymatic reactions having less favourable equilibrium constants:
Glucose-6-phosphate + H20 = glucose + Pi
K'eg = 271
(1)
ATP + glucose = ADP + glucose-6-phosphate
K'eg = 889
(2)
Use this information to determine the value for AG'o for the hydrolysis of ATP at
25°C. Justify the method used.
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