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 15, Problem 11E
Summary Introduction
To explain: The reason for which ΔG values differ from the ΔG°ʹ in the given table in the text book.
Concept introduction: Gibb’s free energy explains the portion of the total energy of a system present for a
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Chapter 15 Solutions
Fundamentals of Biochemistry: Life at the Molecular Level
Ch. 15 - Prob. 1ECh. 15 - Prob. 2ECh. 15 - 3. The reversible reaction shown here is part of...Ch. 15 - 4. Step 4 of the pentose phosphate pathway...Ch. 15 - 5. The aldolase reaction can proceed in revere as...Ch. 15 - Prob. 6ECh. 15 - 7. Identify the intermediate in the...Ch. 15 - 8. The compound you identified in Problem 7 is a...Ch. 15 - 9. The pyruvate ? lactate reaction in animals is...Ch. 15 - Prob. 10E
Ch. 15 - 11. Why is it possible for the ?G values in Table...Ch. 15 - 12. If a reaction has a ?G0' value of at least...Ch. 15 - 13. Although it is not the primary flux-control...Ch. 15 - 14. What is the advantage of activating pyruvate...Ch. 15 - 15. Tumor cells, which tend to grow rapidly,...Ch. 15 - 16. The pyruvate kinase isozyme in cancerous cells...Ch. 15 - 17. Compare the ATP yield of three glucose...Ch. 15 - 18. If G6P is labeled at its C2 position, where...Ch. 15 - Prob. 19ECh. 15 - Prob. 20ECh. 15 - Prob. 21ECh. 15 - 22. Describe the products of the transketolase...Ch. 15 - Prob. 23CQCh. 15 - 24. The enzyme phosphoglucomutase interconverts...Ch. 15 - 25. You combine 0.2 g of yeast. 0.2 g of sucrose...Ch. 15 - 26. Nerve cells require a source of free energy to...Ch. 15 - Prob. 27CQCh. 15 - Prob. 28CQCh. 15 - 29. Consider the pathway for catabolizing...Ch. 15 - 30. Yeast take up and metabolize galactose, using...Ch. 15 - 31. (a) Describe how glycerol enters the...Ch. 15 - 32. Some organisms can anaerobically convert...Ch. 15 - 33. Explain why some tissues continue to produce...Ch. 15 - 34. Some bacteria catabolize glucose by the...Ch. 15 - Prob. 35CQCh. 15 - 36. For enzymes a–e in Problem 35, identify their...Ch. 15 - 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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