Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 3, Problem 11P
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.
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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...
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- 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. Exploring the Michaelis-Menten Equation - II If Vmax=100mol/mLsecand Km=2mM, what is the velocity of the reaction when [S] = 20 mM?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 - 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 οΓthis book. Detailed solutions are available in the Student Solutions Manual. Study Guide, and Problems Book. Calculation of Rate Enhancement from Energies of Activation The relationships between the free energy terms defined in the solution to Problem 4 earlier are shown in the following figure. If the energy of the ES complex is 10 kJ/mol lower than the energy of E + S, the value of Ge:is 20 kJ/mol, and the value of Ge:is 90 kJ/mol what is the rate enhancement achieved by an enzyme in this case?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. 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 (he end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Understanding State Functions Define a slate function. Name three thermodynamic quantities that are state functions and three thatarrow_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_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 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. Interpreting Kinetics Experiments from Graphical Patterns The following graphical patterns obtained from kinetic experiments have several possible interpretations depending on the nature of the experiment and the variables being plotted. Give at least two possibilities for each.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. 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_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. General Controls Over Enzyme Activity List six general ways in which enzyme activity is controlled.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. 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_forward
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