Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 14, Problem 6P
Interpretation Introduction
To suggest:
The proteolytic enzymes that will help in carrying out the cleavage reactions in the question effectively.
Introduction:
Chymotrypsinogen and chymotrypsin both are vital enzymes which help in the catalysis of these reactions. And
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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 οΓthis book. Detailed solutions are available in the Student Solutions Manual. Study Guide, and Problems Book. Superbug infections are becoming more common around the world. Many of these infections arise from the action of -lactamases, of which there are several types with different mechanisms of action. Consult the end-of-chapter reference by von Nussbaum and Schiffer and write detailed mechanisms for the serine -lactamases and metallo- -lactamases.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. Solving the Sequence of an Oligopeptide From Sequence Analysis Data Amino acid analysis of ail oligopeptide seven residues long gave The following fads were observed: a. Trypsin treatment had no apparent effect. b. The phenylthiohydantoin released by Lid mini degradation was c. Brief chymotrypsin treatment yielded several products, including a dipeptide and a tetrapeptide. The amino acid composition of the tetrapeptide was Leu, Lyi. and Met. d. Cyanogen bromide treatment yielded a dipeptide, a tetrapeptide, and free Lys. What is the amino acid sequence of this heptapeptide?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. 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. Solving the Sequence of an Oligopeptide From Sequence Analysis Data Amino acid analysis of a decapeptide revealed the presence of the following products: The following facts were observed: Neither car boxy peptidase A nor B treatment of the- decapeptide had any effect. Trypsin treatment yielded two tetrapcptides and free Lys. Clostripain treatment yielded a tetrapcptide and a hexapeptidc. Cyanogen bromide treatment yielded an octapeptide and a dipeptide of sequence NP (using the one-letter codes). Chymotrypsin treatment yielded two tripeptides and a telrapeptide. The N-terminal chymotryptic peptide had a net charge of — 1 at neutral pi I and a net charge of —3 al pH 12. One cycle of Ed man degradation gave the PTH derivative What is the ammo acid sequence of this decapeptide?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. Evaluation of -Helices in Proteins The hem agglutinin protein in influenza virus contains a remarkably long -helix, with 53 residues. How long is this -helix (in nm)? How many turns does this helix have? The typical residue in an -helix is involved in two H bonds. How many H bonds are present in this helix?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 - 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 οΓthis book. Detailed solutions are available in the Student Solutions Manual. Study Guide, and Problems Book. Consult the following reference (Samanta U. and Bahnson. B. J., 2008. Crystal structure of human plasma platelet-activating factor acetylhydrolase. Journal of Biological Chemistry 283:31617-3U624). consider the active-site structure of this enzyme in the Light of material in this chapter, and write a detailed mechanism for the PAF acetylhydrolase.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_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 Effects on cAMP and Glycogen Levels in Cells Exposed to Cholera Toxin Cholera toxin is an enzyme that covalently modifies the G-subunit of G proteins. (Cholera toxin catalyzes the transfer of ADP-ribose from NAD+ to an arginine residue in Gan ADP-ribosylation reaction.) Covalent modification of G� inactivates its GTPase activity. Predict the consequences of cholera to.vin on cellular cAMP and glycogen levels.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. Review the mechanisms of the .serine and aspartic proteases, and compare these two mechanisms carefully. Are there steps m die mechanisms that are similar? How are they similar? How are they different? Suggest experiments that could support or refute your hypotheses.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. 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.arrow_forward
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