Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 14, Problem 2P
Answers to all problems are at the end οΓthis book. Detailed solutions are available in the Student Solutions Manual. Study Guide, and Problems Book.
Using Site-Direcled Muta.nts to Understand an Enzyme Mechanism In this chapter, the exponent in which Craik and Rutter replaced Asp102 with Asn in trypsin (reducing activity 10,000 -fold) was discussed.
- On the basis of your knowledge of the catalytic triad structure in trypsin, suggest a structure for the “uncatalytic triad" of Asn-His-Ser in this mutant enzyme.
- Explain why the structure you have proposed explains the reduced activity of the mutant trypsin.
- See the original journal articles (Sprang, et al., 1987. Science 237:905-913) to Craik, et al., 1987. Scieence 237:909-913) to see Craik and Rutter's answer to this question.
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Biochemistry
Ch. 14 - Answers to all problems are at the end οΓthis...Ch. 14 - Answers to all problems are at the end οΓthis...Ch. 14 - Prob. 3PCh. 14 - Prob. 4PCh. 14 - Answers to all problems are at the end οΓthis...Ch. 14 - Prob. 6PCh. 14 - Prob. 7PCh. 14 - Answers to all problems are at the end οΓthis...Ch. 14 - Answers to all problems are at the end οf this...Ch. 14 - Answers to all problems are at the end οf this...
Ch. 14 - Answers to all problems are at the end of this...Ch. 14 - Answers to all problems are at the end οΓthis...Ch. 14 - Answers to all problems are at the end οΓthis...Ch. 14 - Prob. 14PCh. 14 - Prob. 15PCh. 14 - Prob. 16PCh. 14 - Prob. 17PCh. 14 - Prob. 18PCh. 14 - Answers to all problems are at the end οΓthis...Ch. 14 - Answers to all problems are at the end οΓthis...Ch. 14 - Answers to all problems are at the end οΓthis...Ch. 14 - Prob. 22PCh. 14 - Prob. 23PCh. 14 - Prob. 24PCh. 14 - Prob. 25PCh. 14 - Prob. 26P
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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. 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. General Controls Over Enzyme Activity List six general ways in which enzyme activity is controlled.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. Graphing the Results from Kinetics Experiments with Enzyme Inhibitors The following kinetic data were obtained for an enzyme in the absence of any inhibitor (1), and in the presence of two different inhibitors (2) and (3) at 5 mM concentration. Assume [ET] is the same in each experiment. Graph these data as Lineweaver-Burk plots and use your graph to find answers to a. and b. a. Determine Vmax and Km for the enzyme. b. Determine the type of inhibition and the K1 for each inhibitor.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. Characterizing a Covalent Enzyme Inhibitor Tosyl-L-phenylalanme cfaloromethyl ketone (TPCK) specifically inhibits chymotrypsin by covalently labeling His57 Propose a mechanism for the inactivation reaction, indicating the structure of the produce(s). State why this inhibitor is specific tor cJiymotrypsin. Propose a reagent based on the structure of TPCK that might be an effective inhibitor of trypsin.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. Describe the secondary structure of each subdomain of malonyl-CoA: ACP transferase Explain the difference between parallel and antiparallel beta sheets.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. Why zymogens Are Advantageous Why do you suppose proteolytic enzymes are- often synthesized as inactive zymogens?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. Using Graphical Methods to Derive the Kinetic Constants for an Ordered, Single-Displacement Reaction The general rate equation for an ordered, single-displacement reaction where A is the leading substrate is v=Vmax[ A ][ B ](KsAKmB+KmA[ B ]+KmB[ A ]+[ A ][ B ])Write the Lineweaver-Burk (double-reciprocal) equivalent of this equation and from it calculate algebraic expressions for the following: a. The slope b. The y-intercepts c. The horizontal and vertical coordinates of the point of intersection when 1/v is plotted versus 1/[B] at various fixed concentrations of Aarrow_forward
- Answers 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. Use examples from the ActiveModel for Human GaleLtin-1 to describe the hydrophobic effect.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. Examine the ActiveModle for N-myristoylt ranjsferase and explain the mechanism of N-myristolation.arrow_forward
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