Fundamentals of Biochemistry: Life at the Molecular Level
5th Edition
ISBN: 9781118918401
Author: Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher: WILEY
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Chapter 20, Problem 14E
Summary Introduction
To determine: The number of ATP derived from the complete oxidation of butyrate.
Concept introduction: Butyrate is produced during the fermentation of the feedstuffs in the rumen. It is readily absorbed by the rumen wall. The epithelial cells in rumen possess high activity of the enzyme butyryl-CoA synthetase that can convert butyrate into butyryl-CoA.
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Chapter 20 Solutions
Fundamentals of Biochemistry: Life at the Molecular Level
Ch. 20 - Prob. 1ECh. 20 - 2. Identify die products generated by the action...Ch. 20 - 3. (a) What is. the charge of bile acids in the...Ch. 20 - 4. Bacteria that live in the large intestine...Ch. 20 - Prob. 5ECh. 20 - 6. Adipocytes store fat in phospholipid-coaled...Ch. 20 - Prob. 7ECh. 20 - Prob. 8ECh. 20 - 9. The first three steps of ? oxidation (Fig....Ch. 20 - Prob. 10E
Ch. 20 - Prob. 11ECh. 20 - Prob. 12ECh. 20 - Prob. 13ECh. 20 - 14. Short chain fatty acids such as butyrate are...Ch. 20 - 15. Why are unsaturated fats preferable to...Ch. 20 - 16. Calculate the ATP yield for the complete...Ch. 20 - 17. Explain why the degradation of odd-chain fatty...Ch. 20 - Prob. 18ECh. 20 - 19. Why is it important that liver cells lack...Ch. 20 - 20. An animal is fed palmitate with a 14C-labeled...Ch. 20 - 21. On what cartoon atoms docs the 14CO2 used to...Ch. 20 - Prob. 22ECh. 20 - 23. Explain why adipocytes need glucose as well as...Ch. 20 - Prob. 24ECh. 20 - 25. Pharmacological inhibition of acetyl-CoA...Ch. 20 - 26. Explain why inhibiting the activity of...Ch. 20 - Prob. 27ECh. 20 - 28. An animal is fed palmitate with a 14C-labeled...Ch. 20 - Prob. 29ECh. 20 - Prob. 30ECh. 20 - Prob. 31CQCh. 20 - Prob. 32CQCh. 20 - 33. Digestion of plant materials generates...Ch. 20 - Prob. 34CQCh. 20 - 35. The tricarboxylate transport system supplies...Ch. 20 - Prob. 36CQCh. 20 - 37. Compare the energy cost, in ATP equivalents,...Ch. 20 - Prob. 38CQCh. 20 - Prob. 39CQCh. 20 - Prob. 40CQCh. 20 - Prob. 41CQCh. 20 - Prob. 42CQCh. 20 - Prob. 43CQCh. 20 - Prob. 1MTE
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- Problem 15 of 15 Submit Using the following reaction data points, construct Lineweaver-Burk plots for an enzyme with and without an inhibitor by dragging the points to their relevant coordinates on the graph and drawing a line of best fit. Using the information from this plot, determine the type of inhibitor present. 1 mM-1 1 s mM -1 [S]' V' with 10 μg per 20 54 10 36 20 5 27 2.5 23 1.25 20 Answer: |||arrow_forward12:33 CO Problem 4 of 15 4G 54% Done On the following Lineweaver-Burk -1 plot, identify the by dragging the Km point to the appropriate value. 1/V 40 35- 30- 25 20 15 10- T Км -15 10 -5 0 5 ||| 10 15 №20 25 25 30 1/[S] Г powered by desmosarrow_forward1:30 5G 47% Problem 10 of 15 Submit Using the following reaction data points, construct a Lineweaver-Burk plot for an enzyme with and without a competitive inhibitor by dragging the points to their relevant coordinates on the graph and drawing a line of best fit. 1 -1 1 mM [S]' s mM¹ with 10 mg pe 20 V' 54 10 36 > ст 5 27 2.5 23 1.25 20 Answer: |||arrow_forward
- Problem 14 of 15 Submit Using the following reaction data points, construct Lineweaver-Burk plots for an enzyme with and without an inhibitor by dragging the points to their relevant coordinates on the graph and drawing a line of best fit. Using the information from this plot, determine the type of inhibitor present. 1 mM-1 1 s mM -1 [S]' V' with 10 μg per 20 54 10 36 20 5 27 2.5 23 1.25 20 Answer: |||arrow_forward12:36 CO Problem 9 of 15 4G. 53% Submit Using the following reaction data points, construct a Lineweaver-Burk plot by dragging the points to their relevant coordinates on the graph and drawing a line of best fit. Based on the plot, determine the value of the catalytic efficiency (specificity constant) given that the enzyme concentration in this experiment is 5.0 μ.Μ. 1 [S] ¨‚ μM-1 1 V sμM-1 100.0 0.100 75.0 0.080 50.0 0.060 15.0 0.030 10.0 0.025 5.0 0.020 Answer: ||| O Гarrow_forwardProblem 11 of 15 Submit Using the following reaction data points, construct a Lineweaver-Burk plot for an enzyme with and without a noncompetitive inhibitor by dragging the points to their relevant coordinates on the graph and drawing a line of best fit. 1 -1 1 mM [S]' 20 V' s mM¹ with 10 μg per 54 10 36 > ст 5 27 2.5 23 1.25 20 Answer: |||arrow_forward
- Problem 13 of 15 Submit Using the following reaction data points, construct Lineweaver-Burk plots for an enzyme with and without an inhibitor by dragging the points to their relevant coordinates on the graph and drawing a line of best fit. Using the information from this plot, determine the type of inhibitor present. 1 mM-1 1 s mM -1 [S]' V' with 10 μg per 20 54 10 36 20 5 27 2.5 23 1.25 20 Answer: |||arrow_forward12:33 CO Problem 8 of 15 4G. 53% Submit Using the following reaction data points, construct a Lineweaver-Burk plot by dragging the points to their relevant coordinates on the graph and drawing a line of best fit. Based on the plot, determine the value of kcat given that the enzyme concentration in this experiment is 5.0 μM. 1 [S] , мм -1 1 V₁ s μM 1 100.0 0.100 75.0 0.080 50.0 0.060 15.0 0.030 10.0 0.025 5.0 0.020 Answer: ||| Гarrow_forward1:33 5G. 46% Problem 12 of 15 Submit Using the following reaction data points, construct a Lineweaver-Burk plot for an enzyme with and without an uncompetitive inhibitor by dragging the points to their relevant coordinates on the graph and drawing a line of best fit. 1 -1 1 mM [S]' 20 V' s mM¹ with 10 μg per 54 10 36 > ст 5 27 2.5 23 1.25 20 Answer: |||arrow_forward
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