Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 14, Problem 22P
Interpretation Introduction
To propose:
The experimental methods used and conclusions presented by Kern and her colleagues.
Introduction:
Kern and her colleagues have put forth some interesting regarding enzyme catalysis. Dorothee Kern and her colleagues examined and inspected microscopic steps which are included in the catalytic cycle of adenylate kinase.
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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 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. Assessing the-Metabolic Consequences of Life Without Enzymes The incredible catalytic power of enzymes can perhaps best be appreciated by imagining how challenging life would be without just one of the thousands of enzymes in the human body. For example, consider life without fnnctose-1,6-btsphosphatase, an enzyme in the gluconeogenesis pathway in Liver and kidneys (see Chapter 22). which helps product new glucose from the food we eat: Fructose-1.6-blsphosphate + H2O Fmrlose-6-P + Pi The human brain requires glucose as its only energy source, and the typical brain consumes about 120 g (or 480 kilocalories) of glucose dally. Ordinarily, two pieces of sausage pizza could provide more than enough potential glucose to feed the brain for a day. According to a national fast-food chain, two pieces of sausage pizza provide 1340 kilocalories. 48% of which is from fat. Fats cannot be converted to glucose in gluconeogenesis, so that leaves 697 kilocalories potentially available for glucose synthesis. The first-order rate constant for the hydrolysis of fructose-l.6-bispliosphate in the absence of enzyme is 2 10-20 /sec. Calculate how long it would take to provide enough glucose for one day of brain activity from two pieces of sausage pizza without the enzyme. The following graphs show the temperature and pH dependencies of four enzymes, A, Β, X, and Y. Problems 12 through IS refer to these graphs.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_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. Protein Kinase Specificity Via Consensus Target Sequences and Intrasteric Control Consult Table 15.2 and, a. Suggest a consensus amino acid sequence within, phosphorylase kinase that makes it a target of protein kinase A (the cAMP- dependent protein kinase). b. Suggest an effective amino acid sequence for a regulatory domain pseudosubstrate sequence that would exert intrasteric control on phosphorylase kinase by blocking its active site.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. 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_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_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_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. The Dimensions of Eukaryotic Cells and Their ConstituentsAssume that liver cells are cuboidal in shape, 20 m oil a side. (Section 1.5) How many liver cells laid end to end would fit across the diameter of a pinhead? (Assume a pinhead diameter of 0.5 mm) What is the volume of a liver cell? (Assume it is a cube.) What is the surface area of a liver cell? What is the surface-to- volume ratio of a liver cell? How does this compare to the surface-to-volume ratio of an E. coli cell (compare this answer with that of problem 3c)? What problems must cells with low surface-to-volume ratios confront that do not occur in cells with high surface-to-volume ratios? A human liver cell contains two sets of 23 chromosomes, each set being roughly equivalent in information content. The total mass of DNA contained in these 46 enormous DNA molecules is 4 1012 Because each nucleotide pair contributes 660 daltons to the mass of DNA and 0.34 run to the length of DNA, what is the total number of nucleotide pairs and the complete length of the DNA in a liver cell? How does this length compare with the overall dimensions of a liver cell? The maximal information in each set of liver cell chromosomes should be related to the number of nucleotide pairs in the chromosome set's DNA. This number can be obtained by dividing the total number of nucleotide pairs just calculated by 2. What is this value? If this information is expressed in proteins that average 400 amino acids in length and three nucleotide pairs encode one amino acid in a protein, how many different kinds of proteins might a liver cell be able to produce? (In reality, liver cell DNA encodes approximately 20,000 different proteins. Thus a large discrepancy exists between the theoretical information content of DNA in liver cells and the amount of information actually expressed.)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. Cells as Steady-State Systems Describe what is meant by the phrase "cells tire steady-state systems." (Section 1.4)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. Which statement is true concerning enzymes and Y? They could not possibly beat work in the same part of the body at the same time. They have different temperature ranges at which they work best. At a pH of 4.5, enzyme works slower than enzyme me Y. At their appropriate pH ranges, both enzymes work equally fast.arrow_forward
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