FUNDAMENTALS OF BIOCHEMISTRY - LL FD
5th Edition
ISBN: 9781119598022
Author: Voet
Publisher: WILEY
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Chapter 11, Problem 27CQ
Summary Introduction
To explain: The reason behind chymotrypsin to catalyze the peptide bond formation.
Concept introduction: Enzymes are biocatalysts that speed up the reaction. Enzymes bind with chemical reactants called substrates. Chymotrypsin is a digestive enzyme that involves the breakdown of proteins in small proteins. Chymotrypsin is secreted by pancreas that converts into trypsin.
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Chapter 11 Solutions
FUNDAMENTALS OF BIOCHEMISTRY - LL FD
Ch. 11 - Prob. 1ECh. 11 - 2. What is the relationship between the rate of an...Ch. 11 - 3. Which type of enzyme (Table 11-2) catalyzes the...Ch. 11 - 4. Which type of enzyme (Table 11-2) catalyzes the...Ch. 11 - 5. On the free energy diagram shown, label the...Ch. 11 - Prob. 6ECh. 11 - 7. Approximately how much does staphylococcal...Ch. 11 - 8. Calculate the rate enhancement that could be...Ch. 11 - 9. Explain why enzyme activity varies with...Ch. 11 - 10. The covalent catalytic mechanism of an enzyme...
Ch. 11 - Prob. 11ECh. 11 - 12. Explain why RNase A cannot catalyze the...Ch. 11 - 13. Urease, the first enzyme to be crystallized,...Ch. 11 - 14. Wolfenden has stated that it is meaningless to...Ch. 11 - 15. Explain why lysozyme cleaves the artificial...Ch. 11 - 16. Would you expect lysozyme to hydrolyze...Ch. 11 - 17. Design a chloromethylketone inhibitor of...Ch. 11 - 18. Predict the effect of mutating Asp 102 of...Ch. 11 - 19. Diagram the hydrogen-bonding interactions of...Ch. 11 - Prob. 20ECh. 11 - 21. Using the reaction shown in Box 11-1 (the...Ch. 11 - Prob. 22CQCh. 11 - 23. What feature of RNA would allow it to function...Ch. 11 - 24. Suggest a transition state analog for proline...Ch. 11 - 25. Lysozyme residues Asp 101 and Arg 114 are...Ch. 11 - 26. Predict the effect on lysozyme’s activity of...Ch. 11 - Prob. 27CQCh. 11 - Prob. 28CQCh. 11 - Prob. 29CQCh. 11 - 30. Many of the cell’s hydrolytic enzymes are...Ch. 11 - Prob. 31CQCh. 11 - Prob. 32CQCh. 11 - Prob. 1MTE
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- Balance the following equation and list of coefficients in order from left to right. SF4+H2O+—-> H2SO3+HFarrow_forwardProblem 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_forward
- 1:30 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_forwardProblem 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_forward
- Problem 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_forwardProblem 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_forward
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