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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 18RQ
Summary Introduction
Introduction:
The free energy (also called Gibbs free energy) is represented by delta G and is a state function that affects the
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_____________ are molecules used in enzyme studies that resemble the structure of a substrate’s transition state.
_________________ is the general term for molecules that enzymes modify to produce reaction products.
The rate of enzyme activity can be affected by changes in ____________ and __________________.
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
Ch. 4 - Prob. 9RQCh. 4 - Prob. 10RQCh. 4 - Prob. 11RQCh. 4 - Prob. 12RQCh. 4 - Prob. 13RQCh. 4 - Prob. 14RQCh. 4 - Prob. 15RQCh. 4 - Prob. 16RQCh. 4 - Prob. 17RQCh. 4 - Prob. 18RQCh. 4 - Prob. 19RQCh. 4 - Prob. 20RQCh. 4 - Prob. 21RQCh. 4 - Prob. 22RQCh. 4 - Prob. 23RQCh. 4 - Prob. 24RQCh. 4 - Prob. 25RQCh. 4 - Prob. 26RQCh. 4 - Prob. 27RQCh. 4 - Prob. 28RQCh. 4 - Prob. 29RQCh. 4 - Prob. 30FBCh. 4 - Prob. 31FBCh. 4 - Prob. 32FBCh. 4 - Prob. 33FBCh. 4 - Prob. 34FBCh. 4 - Prob. 35FBCh. 4 - Prob. 36FBCh. 4 - Prob. 37FBCh. 4 - Prob. 38FBCh. 4 - Prob. 39FBCh. 4 - Prob. 40SACh. 4 - Prob. 41SACh. 4 - Prob. 42SACh. 4 - Prob. 43SACh. 4 - Prob. 44SACh. 4 - Prob. 45TQCh. 4 - Prob. 46TQCh. 4 - Prob. 47TQCh. 4 - Prob. 48TQCh. 4 - Prob. 49TQCh. 4 - Prob. 50TQCh. 4 - Prob. 51TQCh. 4 - Prob. 52TQCh. 4 - Prob. 53TQCh. 4 - Prob. 54TQCh. 4 - Prob. 55TQCh. 4 - Prob. 56TQCh. 4 - Prob. 57TQCh. 4 - Prob. 58TQCh. 4 - Prob. 59TQCh. 4 - Prob. 60TQCh. 4 - Prob. 61TQCh. 4 - Prob. 62TQ
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- The first and second laws of thermodynamics are useful for biochemists who investigate chemical reactions in living organisms. Explain why the third law is not useful.arrow_forwardA patient had severe acid reflux symptoms and decided to take the antacid, Amphojel (aluminum hydroxide). Answer both parts. If this is an oxidation-reduction (redox) and/or precipitation reaction, then show work to support your answer. If this is not an oxidation-reduction (redox) and/or precipitation reaction, then show work to support your answer. Assume that Calcium Iodide and Sodium Oxalate are the starting substances (reactants) in the reaction: What type of reaction(s) is/are being represented by the chemical reaction?arrow_forwardIn enzyme kinetics, why are measurements made at the start of a reaction?arrow_forward
- Allosteric enzymes allow the rate of reactions to control the activity. For example, the production of Product (P) can stop or limit the activity of enzyme 1 via _____________________________.arrow_forwardIn addition to having 6 major classes that display different reactions, enzymes are specific and diverse, and are highly sensitive to ______________ 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 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 . 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 . 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_forwardQuestion 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?)arrow_forward
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