Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Videos
Textbook Question
Chapter 3, Problem 16P
Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book.
- Analyzing the Energetics of Coupled Reactions What k the significance of (he magnitude of for ATP hydrolysis in the calculations in the Deeper Look box “ATP Changes the Keq by a Factor of 108�?
Repeat these calculations for the case of coupling of a reaction to 1,3-bisphosphoglycerate hydrolysis to sec what effect this reaction would have on the equilibrium ratio for emponents A and B under the conditions stated on this page.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Chapter 3 Solutions
Biochemistry
Ch. 3 - Answers to all problems are at the end of this...Ch. 3 - Answers to all problems are at the end of this...Ch. 3 - Answers to all problems are at the end of this...Ch. 3 - Answers to all problems are at (he end of this...Ch. 3 - Answers to all problems are at the end of this...Ch. 3 - Answers to all problems are at the end of this...Ch. 3 - Answers to all problems are at the end of this...Ch. 3 - Answers to all problems are at the end of this...Ch. 3 - Prob. 9PCh. 3 - Answers to all problems are at the end of this...
Ch. 3 - Answers to all problems are at the end of this...Ch. 3 - Answers to all problems are at the end of this...Ch. 3 - Answers to all problems are at the end of this...Ch. 3 - Answers to all problems are at the end of this...Ch. 3 - Answers to all problems are at the end of this...Ch. 3 - Answers to all problems are at the end of this...Ch. 3 - Answers to all problems are at the end of this...Ch. 3 - Answers to all problems are at the end of this...
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Graphical Analysis of MWC Allosteric Enzyme Kinetics (Integrates with Chapter 1.1) Draw both Line weaver-Burk plots and Hanes-Woolf plots for an MWC allosteric enzyme system, showing separate curves for the kinetic response in (a) the absence of any effectors, (b) the presence of allosteric activator Λ, and (c) the presence of allosteric inhibitor I.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Quantitative Relationships Between Rate Constants to Calculate Km, Kinetic Efficiency (kcat/Km) and Vmax - I Measurement of the rate constants for a simple enzymatic reaction obeying Michaelis-Menten kinetics gave the following results: k1=2108M1sec1k1=1103sec1k2=5103sec1a. What is Ks, the dissociation constant for the enzyme-substrate complex? b. What is Km, the Michaelis constant for this enzyme? c. What is kcat (the turnover number) for this enzyme? d. What is the catalytic efficiency (kcat/Km) for this enzyme? e. Does this enzyme approach kinetic perfection? (That is, does kcat/Km approach the diffusion-controlled rate of enzyme association with substrate?) f. If a kinetic measurement was made using 2 nanomoles of enzyme per mL and saturating amounts of substrate, what would Vmax equal? g. Again, using 2 nanomoles of enzyme per mL of reaction mixture, what concentration of substrate would give v = 0.75 Vmax? h. If a kinetic measurement was made using 4 nanomoles of enzyme per mL and saturating amounts of substrate, what would Vmax equal? What would Km equal under these conditions?arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. The enzyme alcohol dehydrogenase catalyzes the oxidation of ethyl alcohol by NAD+ to give acetaldehyde plus NADH and a proton: CHjCH3OH + NAD+ > C’H3CHO + NADH + H+ The rate of this reaction can be measured by following the change in pH. The reaction is run in 1-mL 10 m TRIS buffer at pH 8.6. If the pH of the reaction solution falls to 8.4 after 10 minutes, what is the rate of alcohol oxidation, expressed as nanomoles of ethanol oxidized per mL per sec of reaction mixture?arrow_forward
- Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Calculating and Keq for Coupled Reactions For the process A B. Keq (AB) is 0.02 at 370C. For the process B C. Keq (BC)=1000 at 370C. Determine Keq (AC), the equilibrium constant for the overall process A C, from Keq((AB) and (BC). Determine standard-state free energy changes for all three processes, and use G. (AC) to determine Keq (AC). Make sure that ibis value agrees with that determined m part a of this problem.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. The hydrolysis (if 1, 3-bisphoaphoglycerate is favorable, due in part to the increased resonance stabilization of the products of the reaction. Draw resonance structures for the reactant and the products cf this reaction to establish that this statement is true.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Assessing the Effect of pH on Metabolic Reactions The difference between Gand G' was discussed in Section 33. Consider the hydrolysis of acetyl phosphate (Figure T9) and determine the value of Gfor this reaction at pH 2,7, and 12. The value of Gfor the enolase reaction (Figure 3.10) is 1.8 kJ/mol. What is the value of Gfor enolase at pH 2, 7, and 12? Why is this case different from that (if acetyl phosphate?arrow_forward
- Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Quantitative Relationships Between Rate Constants to Calculate Km, Kinetic Efficiency (kcat/Km) and Vmax - III The citric acid cycle enzyme fumarase catalyzes the conversion of fumarate to form malate. Fumarate+H2OmalateThe turnover number, kcat, for fumarase is 800/sec. The Km of fumarase for its substrate fumarate is 5M. a. In an experiment using 2 nanomole/mL of fumarase, what is Vmax? b. The cellular concentration of fumarate is 47.5 M. What is v when [fumarate] = 47.5 M? c. What is the catalytic efficiency of fumarase? d. Does fumarase approach catalytic perfection?arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. CalculatingGandSfromH The equilibrium constant for some process AB 0.5 at 20°C and 10 at 30°C. Assuming that G is independent of temperature, calculate H for this reaction. GandSat20Candat30C Why- is it important in this problem to assume that H is independent of temperature?arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Quantitative Relationships Between Rate Constants to Calculate Km, Kinetic Efficiency (kcat/Km) and Vmax - VI The enzyme catalase catalyzes the decomposition of hydrogen peroxide: 2H2O22H2O+O2The turnover number (kcat) for catalase is 40,000,000 sec-1. The Km of catalase for its substrate H2O2 is 0.11 M. a. In an experiment using 3 nanomole/L of catalase, what is Vmax? b. What is v when [H2O2] = 0.75 M? c. What is the catalytic efficiency of catalase? d. Does catalase approach catalytic perfection?arrow_forward
- Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Graphical Analysis of Negative Gooperativity in KNF Allosteric Enzyme Kinetics The KNF model for allosteric transitions includes the possibility of negative cooperativity Draw Lineweaver-Burk and Hanes-Woolf plots for the case of negative cooperatively m substrate binding. (As a point of reference, include a line showing the classic Michaelis-Menten response of v to [S].)arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Quantitative Relationships Between Rale Constants to Calculate Km, Kinetic Efficiency (kcat/Km) and Vmax - II Triose phosphate isomerase catalyzes the conversion of glyceraldehyde-3-phosphate to dihydroxy-acetone phosphate. Glyceraldehyde3PdihydroxyacetonePThe Km of this enzyme tor its substrate glyceraldehyde-3-phosphate is 1.8 10-5 M. When [glyceraldehydes-3-phosphate] = 30 M, the rate of the reaction, v, was 82.5 mol mL-1 sec-1. a. What is Vmax for this enzyme? b. Assuming 3 nanomoles per mL of enzyme was used in this experiment ([Etotal]) = 3 nanomol/mL), what is kcat for this enzyme? c. What is the catalytic efficiency (kcat/Km) for triose phosphate isomerase? d. Does the value of kcat/Km reveal whether triose phosphate isomerase approaches catalytic perfection? e. What determines the ultimate speed limit of an enzyme-catalyzed reaction? That is, what is it that imposes the physical limit on kinetic perfection?arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Exploring the Michaelis-Menten Equation - III For a Miehaelis-Menten reaction, k1=7107/Msec, k-1=1103/secand k2=2104/sec. What are the values of Ks and Km? Does substrate binding approach equilibrium, or docs it behave more like a steady-stale system?arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Metabolism and ATP; Author: Professor Dave Explains;https://www.youtube.com/watch?v=-6VyMFQ7rRo;License: Standard YouTube License, CC-BY
Metabolic Diversity (photo-/chemo-, auto-/hetero-, litho-/organo-trophy) | GEO GIRL; Author: GEO GIRL;https://www.youtube.com/watch?v=vyLAm1CYIsI;License: Standard YouTube License, CC-BY