(a)
Interpretation:
The effect of arsenite the loss of citrate should be determined.
Concept introduction:
The citric acid cycle is a catabolic process. It is a series of
(b)
Interpretation:
Explanation for the modified action of arsenite due to the addition of more citrate.
Concept introduction:
The citric acid cycle is a catabolic process. It is a series of chemical reactions in which the stored energy of the body is released by the oxidation of acetyl-Coenzyme A. Oxaloacetate is an intermediate of the Krebs cycle which binds to the acetyl-CoA in the synthesis of citrate. Arsenite is a chemical compound that contains an arsenic oxo-anion in which the arsenic has oxidation state +3.
(c)
Interpretation:
Given data proposes about the place of action of arsenite.
Concept introduction:
The citric acid cycle is a catabolic process. It is a series of chemical reactions in which the stored energy of the body is released by the oxidation of acetyl-Coenzyme A. Oxaloacetate is an intermediate of the Krebs cycle which binds to the acetyl-CoA in the synthesis of citrate. Arsenite is a chemical compound that contains an arsenic oxo-anion in which the arsenic has oxidation state +3.
Want to see the full answer?
Check out a sample textbook solutionChapter 17 Solutions
Biochemistry
- Thank you for helping me. I have to questions. In solution B, if we choose two other points on the graph for calculating the slope, wouldnt the values for Km/Vmax be different than 6.1? Why did you choose exactly those points on the graph? Another thing, I understand the method you used to get to Km/Vmax= slope, but how did you then get the value for Vmax to be 10 mM/s??arrow_forwardEach plot has its own limitations. Match the plot with the correct statement on limitations. 1.Hanes-Woolf 2.Michaelis Menten 3.Lineweaver-Burk limitations: A. This plot appears to allow for more accurate calculation of these parameters, but is prone to error, as the y-axis takes the reciprocal of the rate of reaction –this increases any small errors in measurement at low substrate concentration, where they are most likely to occur. B.The advantage of this plot is that it does not not overemphasizing the data obtained at low [S]. The disadvantage is that any inaccurate measures of substrate concentration will be exaggerated as [S] is used on both axes. C.It is difficult to obtain a meaningful value of Km from this plot because of the high substrate concentrations needed to reach Vmax. Vmax has to be estimated by extrapolation- which is partly subjective and introduces error. D.The advantage of this plot is that it overcomes uneven spacing of points, and undue weight of a…arrow_forwardBased on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any inhibitor, (2) presence of 15 µM of a reversible inhibitor, or (3) presence of 20 µM of a second (distinct) reversible inhibitor. Purified enzyme concentration was 5 µM. The y-intercept of Lines (A) and (B) is 0.9 sec/uM; the y-intercept of Line (C) is 0.3 sec/uM. The slope of Line (A) is 1.8 sec; the slope of Lines (B) and (C) is 0.6 sec. Calculate the Km of the reaction represented by Line (B).arrow_forward
- Based on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any inhibitor, (2) presence of 15 µM of a reversible inhibitor, or (3) presence of 20 µM of a second (distinct) reversible inhibitor. Purified enzyme concentration was 5 µM. The y-intercept of Lines (A) and (B) is 0.9 sec/uM; the y-intercept of Line (C) is 0.3 sec/uM. The slope of Line (A) is 1.8 sec; the slope of Lines (B) and (C) is 0.6 sec. Calculate the catalytic efficiency of the reaction represented by Line (A).arrow_forwardBased on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any inhibitor, (2) presence of 15 µM of a reversible inhibitor, or (3) presence of 20 µM of a second (distinct) reversible inhibitor. Purified enzyme concentration was 5 µM. The y-intercept of Lines (A) and (B) is 0.9 sec/uM; the y-intercept of Line (C) is 0.3 sec/uM. The slope of Line (A) is 1.8 sec; the slope of Lines (B) and (C) is 0.6 sec. Line (B) represents ____________. A. an enzyme-catalyzed reaction in the absence of any inhibitor. B. an enzyme-catalyzed reaction in the presence of a competitive inhibitor. C. an enzyme-catalyzed reaction in the presence of an uncompetitive inhibitor. D. an enzyme-catalyzed reaction in the presence of a noncompetitive, or mixed, inhibitor.arrow_forwardBased on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any inhibitor, (2) presence of 15 µM of a reversible inhibitor, or (3) presence of 20 µM of a second (distinct) reversible inhibitor. Purified enzyme concentration was 5 µM. The y-intercept of Lines (A) and (B) is 0.9 sec/uM; the y-intercept of Line (C) is 0.3 sec/uM. The slope of Line (A) is 1.8 sec; the slope of Lines (B) and (C) is 0.6 sec. Calculate the Vmax of the reaction represented by Line (C). Show all mathematical work, please.arrow_forward
- Based on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any inhibitor, (2) presence of 15 µM of a reversible inhibitor, or (3) presence of 20 µM of a second (distinct) reversible inhibitor. Purified enzyme concentration was 5 µM. The y-intercept of Lines (A) and (B) is 0.9 sec/uM; the y-intercept of Line (C) is 0.3 sec/uM. The slope of Line (A) is 1.8 sec; the slope of Lines (B) and (C) is 0.6 sec. QUESTION: Line (A) represents ____________. A. an enzyme-catalyzed reaction in the absence of any inhibitor. B. an enzyme-catalyzed reaction in the presence of a competitive inhibitor. C. an enzyme-catalyzed reaction in the presence of an uncompetitive inhibitor. D. an enzyme-catalyzed reaction in the presence of a noncompetitive, or mixed, inhibitor.arrow_forwardBased on the Lineweaver-Burke plot attached. Kinetic data were generated in the (1) absence of any inhibitor, (2) presence of 15 µM of a reversible inhibitor, or (3) presence of 20 µM of a second (distinct) reversible inhibitor. Purified enzyme concentration was 5 µM. The y-intercept of Lines (A) and (B) is 0.9 sec/uM; the y-intercept of Line (C) is 0.3 sec/uM. The slope of Line (A) is 1.8 sec; the slope of Lines (B) and (C) is 0.6 sec. Which of the following statements is true? Select any/all answers that apply. A. Both types of inhibitor mediate a slope effect on the Lineweaver-Burke plot. B. Both types of inhibitor decrease the apparent Vmax for this enzyme-catalyzed reaction. C. Both types of inhibitor alter the apparent Km of this enzyme-catalyzed reaction. D. Lines (A) and (C) share the same X-intercept, indicating that the noncompetitive inhibitor decreases the apparent Km of this enzyme-catalyzed reaction. E. Lines (A) and (C)…arrow_forwardENZYME KINETICS ANALYSIS of 6 Xanthine oxidase (XO) is the enzyme that catalyzes the synthesis of uric acid, which in excess causes gouty arthritis. The inhibition of this enzyme is therefore critical in its treatment. A student researcher is investigating the inhibitory effects of kaempferol (Kmp) and chlorogenic acid (Cha) on XO which uses xanthine (Xan) as substrate. Table 1 below shows the enzyme kinetic data. Construct the Lineweaver-Burk plot complete with the linear regression analvsis. Fill in the needed information on Table 2 and paste a copy of your Lineweaver-Burk plot. submit the picture of your output in PNG or JPG format. Table 1. Enzyme Kinetic Data Velocity, mM/s [S], mM Хan Kmp Cha 0.492 0.0678 0.0351 0.0615 0.211 0.0531 0.0261 0.0451 0.087 0.0298 0.0157 0.0211 0.048 0.0195 0.0091 0.0142 0.029 0.0127 0.0067 0.0081 Table 2. Enzyme Kinetic Parameters Xanthine Kaempferol Chlorogenic acid Parameters Vmax Км Type of Inhibition Mode of Binding NA NA Lineweaver-Burk Plotarrow_forward
- Thin Layer chromatography (TLC). Explain the biochemical principle behind the separation of carbohydrates molecules by TLC as performed in practical 5. Explain which properties molecules must have to travel a short and large distance, respectively. Ketohexose sugars can form 8 different stereoisomers. How many of those isomers can be distinguished and resolved by TLC as performed in the practical and why? no more than 100 words totalarrow_forwardAnser in your own words. a. During pregnancy, do mother and child share the same blood? What if they have different blood types? b. If a patient takes a large dose of a drug that blocks calcium channels, what happens to the heart? c. The enzymes of the digestive system are classified as hydrolases. What does this mean? d. Explain in a scientific but simple manner the idiomatic expression “butterflies in my stomach”.arrow_forwardEnzyme Kinetics and Inhibition, Part 1 (worksheet for laboratory exercise 5) Suppose that you have isolated the enzyme sucrase (able to hydrolyze sucrose into glucose and fructose), and you wish to determine the nature of inhibitor A for this enzyme. You have prepared five different concentrations of substrate (sucrose), and five different concentrations of inhibitor A (plus the control, with zero mM of inhibitor A). The following Table lists the inhibitor A concentrations [I], substrate concentrations [S], and resulting enzyme velocities (V.) for all six of these experiments: 1/ V. (1) 0 mM O mM 0 mM 0 mM 0 mM [S] 0.1 mM 0.2 mM Vo 0.3333 0.50 1/[S] 33333 mM per minute 0.3 mM 0.4 mM 0.5 mM 0.60 0.666666666667 0.714285714286 0.1 mM 0.1 mM 0.20 0.2 mM 0.3 mM 0.1 mM 0.333333333333 0.428571428571 0.50 0.1 mM 0.1 mM 0.4 mM 0.5 mM 0.1 mM 0.1 mM 0.555555555556 0.20 mM 0.20 mM 0.20 mM 0.20 mM 0.20 mM 0.3 mM 0.142857142857 0.25 0.2 mM 0.3 mM 0.333333333333 0.40 0.454545454545 0.111111111111…arrow_forward
- BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. FreemanLehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. FreemanFundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
- BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningFundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON