Fundamentals of General, Organic, and Biological Chemistry, Books a la Carte Plus Mastering Chemistry with Pearson eText -- Access Card Package (8th Edition)
8th Edition
ISBN: 9780134261256
Author: John McMurray, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher: PEARSON
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Chapter 25.6, Problem 25.6CIAP
Interpretation Introduction
Interpretation:
The essential amino called known as “nature’s Prozac” has to be determined with stating the symptoms in deficiencies of it.
Concept introduction:
Amino acids are nutritionally classified into three groups,
- Nonessential amino acids
- Conditional amino acids
- Essential amino acids.
Essential amino acids are those in which our body cannot produce them through the biochemical machinery we possess therefore it must be consumed through the food we eat.
Tryptophan is an essential amino acid used as a mild antidepressant.
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Balance the following equation and list of coefficients in order from left to right. SF4+H2O+—-> H2SO3+HF
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:
|||
12:33
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
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Chapter 25 Solutions
Fundamentals of General, Organic, and Biological Chemistry, Books a la Carte Plus Mastering Chemistry with Pearson eText -- Access Card Package (8th Edition)
Ch. 25.2 - Prob. 25.1PCh. 25.2 - Prob. 25.2KCPCh. 25.3 - Prob. 25.3PCh. 25.3 - Prob. 25.4PCh. 25.3 - Prob. 25.5PCh. 25.3 - Prob. 25.6PCh. 25.4 - Prob. 25.1CIAPCh. 25.4 - Prob. 25.2CIAPCh. 25.4 - Prob. 25.3CIAPCh. 25.4 - Prob. 25.7P
Ch. 25.4 - Prob. 25.8KCPCh. 25.6 - Prob. 25.9PCh. 25.6 - Prob. 25.10KCPCh. 25.6 - What is meant by a conditional amino acid?Ch. 25.6 - Prob. 25.5CIAPCh. 25.6 - Prob. 25.6CIAPCh. 25 - In the diagram shown here, fill in the sources for...Ch. 25 - Prob. 25.12UKCCh. 25 - Prob. 25.13UKCCh. 25 - Prob. 25.14UKCCh. 25 - Prob. 25.15UKCCh. 25 - Prob. 25.16UKCCh. 25 - Prob. 25.17APCh. 25 - Prob. 25.18APCh. 25 - Prob. 25.19APCh. 25 - Prob. 25.20APCh. 25 - Prob. 25.21APCh. 25 - Prob. 25.22APCh. 25 - What is the structure of the -keto acid formed...Ch. 25 - Prob. 25.24APCh. 25 - In general, how does oxidative deamination differ...Ch. 25 - Prob. 25.26APCh. 25 - Prob. 25.27APCh. 25 - Prob. 25.28APCh. 25 - Prob. 25.29APCh. 25 - Prob. 25.30APCh. 25 - Prob. 25.31APCh. 25 - Prob. 25.32APCh. 25 - Prob. 25.33APCh. 25 - Prob. 25.34APCh. 25 - How do essential and nonessential amino acids...Ch. 25 - Prob. 25.36APCh. 25 - Prob. 25.37APCh. 25 - How is tyrosine biosynthesized in the body? What...Ch. 25 - Prob. 25.39APCh. 25 - Prob. 25.40APCh. 25 - Prob. 25.41APCh. 25 - What energy source is used in the formation of...Ch. 25 - Write the equation for the transamination reaction...Ch. 25 - Prob. 25.44CPCh. 25 - Prob. 25.45CPCh. 25 - Prob. 25.46CPCh. 25 - Prob. 25.47CPCh. 25 - Prob. 25.48CPCh. 25 - Prob. 25.49CPCh. 25 - Prob. 25.50CPCh. 25 - Prob. 25.51CPCh. 25 - Prob. 25.52CPCh. 25 - Why might it be a bad idea to take large...Ch. 25 - Prob. 25.54GPCh. 25 - Prob. 25.55GPCh. 25 - Prob. 25.56GP
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- 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
- 1:33 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_forward12:33 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_forward
- 12:20 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_forward12:33 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_forward
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