Biochemistry: The Molecular Basis of Life
Biochemistry: The Molecular Basis of Life
6th Edition
ISBN: 9780190209896
Author: Trudy McKee, James R. McKee
Publisher: Oxford University Press
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Chapter 4, Problem 6RQ
Summary Introduction

Introduction:

The spontaneity of any reaction can be determined by looking at the value of Gibbs free energychange (delta G). The overall negative value indicates that the reaction is spontaneous whereas a positive value indicates that the reaction cannot occur in those conditions. Non- spontaneous reactions can be made to occur by coupling them with other reactions such as ATP hydrolysis(delta G = –30.5 kilojoules per mole) so that the overall value of Gibbs free energy turns out to be negative.

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The following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menten plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3. CO2 + H20 > H+ + HCO3 There are many different isoforms of this enzyme. (see for instance http://en.wikipedia.org/wiki/Carbonic_anhydrase . Assume that one variant has a Km of 10 µM and a different variant has a Km of 100 µM. Draw on the same graph a typical Michaelis-Menton plot showing the alteration in the rate of carbonic anhydrase as the CO2 level is varied for the two different variants of enzyme, assuming the concentration of the enzyme (10 mM) in the test tube is kept constant. Assume that you have equal amounts of the two different variants of carbonic anhydrase in a number of test tubes and that the Vmax for both enzymes are the same. Be sure to label the axes. For the same conditions as above, draw a…
The following question focuses on how the parameters regulating enzyme function might change, and how these might appear graphically on a Michaelis-Menten plot and a Lineweaver-Burke plot. Carbonic anhydrase is an enzyme that will convert CO2 and water into HCO3. CO2 + H20 > H+ + HCO3 There are many different isoforms of this enzyme. (see for instance http://en.wikipedia.org/wiki/Carbonic_anhydrase 1 Assume that one variant has a Km of 10 µM and a different variant has a Km of 100 µM. Draw on the same graph a typical Michaelis-Menton plot showing the alteration in the rate of carbonic anhydrase as the CO2 level is varied for the two different variants of enzyme, assuming the concentration of the enzyme (10 mM) in the test tube is kept constant. Assume that you have equal amounts of the two different variants of carbonic anhydrase in a number of test tubes and that the Vmax for both enzymes are the same. Be sure to label the axes. For the same conditions as above, draw a…
Question 1: Part a:  Assume that the standard free energy of ATP hydrolysis is -31 kJ/mol. Assume the following values for the standard free energy changes of the four reactions: HK -16.7 kJ/mol; PFK -14.2 kJ/mol; PGK -18.9 kJ/mol; PK -31.7 kJ/mol. (from bio.libretexts.org). Use these values to compute the standard free energy of hydrolysis (releasing Pi) of i. glucose 6-P ii. fructose 1,6-bis-P iii. 1,3-bisphosphoglycerate iv. phosphoenolpyruvate Part b: Which of these four compounds is the strongest phosphoryl donor?______________ Which is the weakest?__________________ Part c: The phosphoglycerate kinase reaction is favorable by -18.9 kJ/mol in the glycolytic direction, as stated above. In gluconeogenesis, this step is simply reversed; i.e. it is not one of the three steps in gluconeogenesis that is driven by using different chemistry than that of glycolysis. How can this be? (Be specific: what specific factors could enable reversal of this step?)
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