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 24RQ
Summary Introduction
To review:
Whether the stability of ATP (adenosine triphosphate) will be more, less, or the same in the absence of magnesium ions.
Introduction:
ATP is also known as the molecular currency of the cell. ATP is produced by three important pathways: glycolysis, citric acid cycle, and beta-oxidation of fatty acids. The main contributor of ATP in the cell is the citric acid cycle, which takes place in the mitochondrion of eukaryotic cells.
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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…
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 . Imidazol is a competitive inhibitor of carbonic anhydrase. It is effective at an alkaline (high) pH; in lower (more acidic) pH, it no longer inhibits the enzyme. Draw on a separate graph a Lineweaver-Burke plot for the effects of this compound at high pH and low pH. Be sure to label the axes and put in sample data points.
Chapter 4 Solutions
Biochemistry: The Molecular Basis of Life
Ch. 4 - Prob. 1QCh. 4 - Prob. 2QCh. 4 - Prob. 1RQCh. 4 - Prob. 2RQCh. 4 - Prob. 3RQCh. 4 - Prob. 4RQCh. 4 - Prob. 5RQCh. 4 - Prob. 6RQCh. 4 - Prob. 7RQCh. 4 - Prob. 8RQ
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