Biochemistry: The Molecular Basis of Life
6th Edition
ISBN: 9780190209896
Author: Trudy McKee, James R. McKee
Publisher: Oxford University Press
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Question
Chapter 6, Problem 8RQ
Summary Introduction
To review:
The regulation of enzymatic reactions by a cell.
Introduction:
Enzymes are macromolecules or proteins that catalyze the reactions. They are known as biological catalysts. Their activity can be regulated. Regulation is essential to maintain an ordered state in a cell and for conservation of energy.
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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
Ch. 6 - Prob. 2RQCh. 6 - Prob. 3RQCh. 6 - Prob. 4RQCh. 6 - Prob. 5RQCh. 6 - Prob. 6RQCh. 6 - Prob. 7RQCh. 6 - Prob. 8RQCh. 6 - Prob. 9RQCh. 6 - Prob. 10RQCh. 6 - Prob. 11RQCh. 6 - Prob. 12RQCh. 6 - Prob. 13RQCh. 6 - Prob. 14RQCh. 6 - Prob. 15RQCh. 6 - Prob. 16RQCh. 6 - Prob. 17RQCh. 6 - Prob. 18RQCh. 6 - Prob. 19RQCh. 6 - Prob. 20RQCh. 6 - Prob. 21RQCh. 6 - Prob. 22RQCh. 6 - Prob. 23RQCh. 6 - Prob. 24RQCh. 6 - Prob. 25RQCh. 6 - Prob. 26RQCh. 6 - Prob. 27RQCh. 6 - Prob. 28RQCh. 6 - Prob. 29RQCh. 6 - Prob. 30RQCh. 6 - Prob. 31RQCh. 6 - Prob. 32RQCh. 6 - Prob. 33RQCh. 6 - Prob. 34RQCh. 6 - Prob. 35RQCh. 6 - Prob. 36RQCh. 6 - Prob. 37RQCh. 6 - Prob. 38RQCh. 6 - Prob. 39RQCh. 6 - Prob. 40RQCh. 6 - Prob. 41RQCh. 6 - Prob. 42RQCh. 6 - Prob. 43FBCh. 6 - Prob. 44FBCh. 6 - Prob. 45FBCh. 6 - Prob. 46FBCh. 6 - Prob. 47FBCh. 6 - Prob. 48FBCh. 6 - Prob. 49FBCh. 6 - Prob. 50FBCh. 6 - Prob. 51FBCh. 6 - Prob. 52FBCh. 6 - Prob. 53SACh. 6 - Prob. 54SACh. 6 - Prob. 55SACh. 6 - Prob. 56SACh. 6 - Prob. 57SACh. 6 - Prob. 58TQCh. 6 - Prob. 59TQCh. 6 - Prob. 60TQCh. 6 - Prob. 61TQCh. 6 - Prob. 62TQCh. 6 - Prob. 63TQCh. 6 - Prob. 64TQCh. 6 - Prob. 65TQCh. 6 - Prob. 66TQCh. 6 - Prob. 67TQCh. 6 - Prob. 68TQCh. 6 - Prob. 69TQCh. 6 - Prob. 70TQCh. 6 - Prob. 71TQCh. 6 - Prob. 72TQCh. 6 - Prob. 73TQCh. 6 - Prob. 74TQCh. 6 - Prob. 75TQCh. 6 - Prob. 76TQCh. 6 - Prob. 77TQCh. 6 - Prob. 78TQCh. 6 - Prob. 79TQCh. 6 - Prob. 80TQCh. 6 - Prob. 81TQ
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- Hexokinase is an example of a general class of enzymeknown as the _____________________.arrow_forwardWhy does rubisco have such a low catalytic rate (that is, why is it so slow)?arrow_forwardThe primary structure of the enzyme lysozyme compared to its tertiary structure is an example of how _____________ is critical to _____________.arrow_forward
- The rate of enzyme activity can be affected by changes in ____________ and __________________.arrow_forwardThe 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…arrow_forwardThe 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…arrow_forward
- 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_forwardGlycogen phosphorylase, an enzyme that catalyzes the breakdown of glycogen to form glucose, is active when a phosphate group is added. This is an example of enzyme regulation by ____________________________.arrow_forward_____________ allosteric effects of enzymes involve ligands that are different from substrate molecules.arrow_forward
- Each type of enzyme contains a unique, intricately shaped binding surface called a(n) _____________.arrow_forwardThe term "dark reactions" was once used to describe the Calvin cycle. Explain why this term was used and suggest why this term is no longer used. Paragraph I U + v ...arrow_forwardThe uncatalyzed reaction rate for the conversion of substrate X to product Y is one year. The enzyme-catalyzedrate is one millisecond. Describe the features of theenzyme that are probably responsible for this ratedifference.arrow_forward
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