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 6, Problem 67TQ
Summary Introduction
To review:
Information that can be determined by the turnover number (
Introduction:
Michaelis–Menten constant (
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The hexokinases are a class of enzymes that catalyze the ATP-dependent phosphorylation of hexoses (sugars with six carbons). The hexokinases will bind only D-hexose sugars and not their L-counterparts. In general terms, describe the features of enzyme structure that make this specificity possible.
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…
Chapter 6 Solutions
Biochemistry: The Molecular Basis of Life
Ch. 6 - Prob. 1QCh. 6 - Prob. 2QCh. 6 - Prob. 3QCh. 6 - Prob. 4QCh. 6 - Prob. 5QCh. 6 - Prob. 6QCh. 6 - Prob. 7QCh. 6 - Prob. 8QCh. 6 - Prob. 9QCh. 6 - Prob. 1RQ
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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 . 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.arrow_forwardIn order to function as an oxidative phosphorylation uncoupler, 2,4-dinitrophenol must act catalytically, not stoichiometrically. What does this mean? Identify and discuss an important implication of this conclusion.arrow_forwardThis is a picture of the catalysis of alcohol by ADH with an inhibitor binding as an aldehyde analog. I have two questions. First, what would the enzyme be classified as and why? Also, what would the steps of this mechanism be?arrow_forward
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