6. The enzyme prostaglandin endoperoxide synthase (PTGS) catalyzes the conversion of arachidonicacid to PGG2, a precursor of prostaglandins. Ibuprofen is a potent inhibitor of PTGS. The followingdata were obtained for reactions catalyzed by PTGS in the absence and presence of ibuprofen ([Arachidonicacid] (mm)0.511.52.53.5Rate of formation ofPGG₂ (mm/min)23.532.236.941.844.0Rate of formation of PGG₂ with10 mg/ml ibuprofen (mm/min)16.6725.2530.4937.0438.91(a) Using Excel or an equivalent program, graph the data on a Lineweaver-Burk plot. Attach a graphof your work with properly labeled axes and equations for the linear regressions.(b) Determine the KM and Vmax of the reaction catalyzed by PTGS in the absence of ibuprofen as wellas the apparent KM and apparent Vmax of the reaction in the presence of ibuprofen.(c) What type of inhibition does ibuprofen exert on PTGS? Briefly explain your answer.

Parameters such as Km and Vmax are used for comparing enzyme activities. If we know the initial rate…

Answered: 6. The enzyme prostaglandin…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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The hexapeptide Ala-Met-Leu-Lys-Phe-Asp is digested in the same tube with both Cyanogen Bromide and Trypsin at the same time at pH=7. Draw the structure of the product(s) that would bind to a cation exchange column. (Relevant pKa values are 2.2, 3.9, 9.5 and 10.5. Assume pKa values for any newly generated a-amino and a-carboxyl groups are 9.5 and 2.2 respectively)
4. Below is a Michaelis-Menten plot for a wild-type (WT) and mutant (V105A) enzyme isolated from the bacterium Staphylococcus aureus. The enzyme is involved in carbohydrate metabolism and is a potential biocatalyst for the large-scale production of rare sugars. (8) mg V₂ μmol s1 1.50- 1.25- 1.00- 0.75- 0.50- 0.25- 0.00 0 100 200 300 [s], mM 400 500 WT (a) Estimate the KM and Vmax for the wild-type and mutant enzyme from the graph. V105A (b) Calculate the keat and keat/KM for the wild-type and mutant enzyme based on your estimated values in (a) if the total enzyme concentration is 0.5 µmol/mg. (c) Is the mutant enzyme a more or less efficient catalyst than the wild-type enzyme? Briefly explain.
For the following reaction: HNO3 H2SO4 NO2 NO2 NO2 10% 8% 82% 1. Write a reasonable mechanism, using curved arrow notation to show the flow of electrons, for the formation of all three products. Your answer should include all important resonance structures. 2. Using the mechanism and resonance structures, provide an explanation for the product ratios shown.
make a schematic diagram of BChE/AChE inhibitory determination Butyrylthiocholine iodide (BChI), as well as acetylthiocholine iodide(AChI) molecules were utilized as substrate compounds of the reaction. Inthis regard, 5,5′‐dithio‐bis(2‐nitro‐benzoic acid) compound (DTNB) wasused to estimate BChE/AChE activity. In summary, 100 μL Tris buffersolution (HCl, 1.0M, pH 8.0, Tris) and variety of concentrations of thesample solution (50‐200 mL) were added in deionized water and also20 μL of BChE/AChE enzymes solutions added. The mixture was thenincubated for 10 minutes at 20°C. Finally, 50 μL of DTNB (0.5 mM and25 mL) BChI/AChI were added to the incubator mixture. The reactionwas also started by adding 50 μL BChI/AChI. The activity of theseenzymes was evaluated using spectrophotometric spectra with awavelength of 412 nm.
can you explain what is happening in the attached graph? Figure 3: Lineweaver-Burke plot of alkaline phosphatase activity without inhibitor
The enzyme, fumarate, has the following kinetic constants: k 1 k 2 k -1 where k 1 = 10 9 M -1 s -1 k -1 =4.4 x 10 4 s -1 k 2 = 10 3 s -1 a. What is the value of the Michaelis constant for this enzyme? b. At an enzyme concentration of 10 -6 M, what will be the initial rate of product"
4.2
Write a balanced equation for cach of the following reactions or reaction sequences. (a) The reaction catalyzed by PFK-2 (b) The conversion of 2 moles of oxaloacetate to glucose (c) The conversion of glucose to UDP-Gle (d) The conversion of 2 moles of glycerol to glucose (e) The conversion of 2 moles of malate to glucose-6-phosphate
Chymotrypsin has the highest affinity for which of the following substrates: Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Chymotrypsin Ки (М) 4.4 x 10-1 8.8 x 10-2 6.6 x 104 Kcat (S-1) 5.1 x 10-2 1.7 x 10-1 1.9 x 102 Substrate N-acetylglycine ethyl ester N-acetylvaline ethyl ester N-acetyltyrosine ethyl ester Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 OA. N-acetylglycine ethyl ester OB. N-acetylvaline ethyl ester OC. N-acetyltyrosine ethyl ester D. Urea
Carboxylic acids, such as the one shown below, can be difficult to reduce Provide the name of a reductant A. Explain why this reductant is able to react with the carboxylic acid whereas others cannot (Hint: Draw and discuss the potential reactive intermediates/transition states).
Aspirin, C9H8O4, is produced from salicylic acid, C7H6O3, and acetic anhydride, C4H6O3, as shown below.C7H6O3 + C4 H603 C9H8O4 + HC2H3O2 What is the theoretical yield of aspirin if 175 kg of salicylic acid is allowed to react with excess of acetic anhydride?
None

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