FUNDAMENTALS OF BIOCHEMISTRY-ACCESS
5th Edition
ISBN: 9781119498742
Author: Voet
Publisher: WILEY
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Chapter 11, Problem 4E
(a)
Summary Introduction
To identify: The type of enzyme that catalyzes the given reaction.
Concept introduction: Enzymes are the biocatalysts that accelerate the
(b)
Summary Introduction
To identify: The type of enzyme that catalyzes the given reaction.
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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:
|||
12:36
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
Г
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:
|||
Chapter 11 Solutions
FUNDAMENTALS OF BIOCHEMISTRY-ACCESS
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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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
- 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
- 12:33 CO Problem 7 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 Vmax. Report your answer to three significant figures. 1 , mM-1 1 [S] 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: ||| Гarrow_forward12:33 CO Problem 5 of 15 4G 54% Done On the following Lineweaver-Burk 1 plot, identify the by dragging the Vmax point to the appropriate value on the line. NI 35 30- 25 20- 15- 10 5. 1 Vmax -15 10 -5 0 5 10 15 20 20 ||| で Г 25 30 1/[S]arrow_forward12:20 V 0.1- 0:09. 0.08 0:07 0.06 -0.05- 0:04- -0.03- -0.02- 4G 56% Problem 1 of 15 Done On the following Michaelis-Menten plot, estimate the value of - Vmax by 1 2 dragging the line to the appropriate value on the y-axis. 0.01 V max 0 0.5 ||| 1.5 2.5 3.5 4 ISLarrow_forward
- 12:33 CO 4G 54% Problem 6 of 15 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 Km. 1 mM-1 1 [S]' " s mM-1 V 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_forwardV 0.1- 0:09 0:08 0:07- -0.06 -0.05 0:04- 0:03 0:02 0:01- Problem 2 of 15 Done On the following Michaelis-Menten plot, estimate the value of Kм by dragging the point to the appropriate value on the x-axis. I T | 0 0.5 1.5 2 KM -0:01- ||| 25 2.5 3 3.5 4 Г [S] powered by desmosarrow_forward9. Sketch NMR of the following compound. Clearly label each H-atom in the molecule and where it appears in your NMR. Clearly label the splitting (coupling) pattern (singlet, doublet etc) for each set of equivalent protons. For each signal, clearly label the integration value or the number of protons represented by the signal. Brarrow_forward
- Please help with this Mass Spectrometry Question. Thank you For the mass spec. shown in the attached image, please determine and give the amino acid sequence of the pentapeptide. Show which end is the amino terminus and which is the carboxy terminus. How does one arrive at the solution?arrow_forwardDraw a tripeptide of your choosing at pH 7. Have the N-terminus on the left and the C-terminus on the right. Then: Draw a triangle around the α-carbons. Draw a box around the R-groups. Circle the atoms capable of hydrogen bonding. Highlight the atoms involved in the formation of the peptide bonds. What type of structure have you drawn? (primary, secondary, tertiary or quaternary protein structure).arrow_forward2. For the flow of fluid over a flat membrane of length 10cm, determine the length-average mass transfer coefficient. The relevant properties of the system are u=0.01cm²/s, D=5 x 106 cm²/s, and v = 5.0 cm/s.arrow_forward
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Enzyme Kinetics; Author: MIT OpenCourseWare;https://www.youtube.com/watch?v=FXWZr3mscUo;License: Standard Youtube License