Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
expand_more
expand_more
format_list_bulleted
Textbook Question
Chapter 15, Problem 10P
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.
One Way Negative Cooperatively Might Make
Allosteric enzymes that sit at branch, points leading to several essential products sometimes display negative cooperativity for feedback inhibition (allosteric inhibition) by one of the products. What might be the advantage of negative cooperativity instead of positive cooperativity in feedback inhibitor binding by such enzymes?
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionChapter 15 Solutions
Biochemistry
Ch. 15 - Answers to all problems are at the end of this...Ch. 15 - Answers to all problems are at the end of this...Ch. 15 - Answers to all problems are at the end of this...Ch. 15 - Answers to all problems are at the end of this...Ch. 15 - Prob. 5PCh. 15 - Prob. 6PCh. 15 - Prob. 7PCh. 15 - Prob. 8PCh. 15 - Answers to all problems are at the end of this...Ch. 15 - Answers to all problems are at the end of this...
Ch. 15 - Answers to all problems are at the end of this...Ch. 15 - Answers to all problems are at the end of this...Ch. 15 - Answers to all problems are at the end of this...Ch. 15 - Prob. 14PCh. 15 - Prob. 15PCh. 15 - Prob. 16PCh. 15 - Prob. 17PCh. 15 - Prob. 18PCh. 15 - Prob. 19PCh. 15 - Prob. 20PCh. 15 - Prob. 21PCh. 15 - Prob. 22PCh. 15 - Prob. 23PCh. 15 - Prob. 24P
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. 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 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. 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, Î’, X, and Y. Problems 12 through IS refer to these graphs.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. How Varying the Amount of Enzyme or the Addition of Inhibitors Affects v Versus [S] Plots Using Figure 13.7 as a model, draw curves that would be obtained in v versus [S] plots when a. twice as much enzyme is used. b. half as much enzyme is used. c. a competitive inhibitor is added. d. a pure noncompetitive inhibitor is added. e. an uncompetitive inhibitor is added. For each example, indicate how Vmax and Km change.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 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 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. 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. 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 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_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
Embryology | Fertilization, Cleavage, Blastulation; Author: Ninja Nerd;https://www.youtube.com/watch?v=8-KF0rnhKTU;License: Standard YouTube License, CC-BY