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A: Dear student I have given answer to your question in the image format.
Q: Questions 31 - 33 concem the following compounds A. B. NH, C;H,NH2 CH,CONH, fle
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A: Identify the indicated hydrogens in the following molecules as pro-R or pro-S.,
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Q: NH2 OH NEN: `NH2 IZ IZ
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Q: но. но Br
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Q: Find out relationship between given both subpart along with explanation
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- You are called in as a consult for a patient who suffers from acidosis. Urine levels of both lactic acid and isocitric acid are elevated. Mitochondria isolated from the patient’s fibroblasts oxidize pyruvate very slowly whereas α-ketoglutarate and malate are oxidized normally. a. At what enzyme would you predict the patient has a defect? b. Why? What evidence do you have to choose that enzyme? c. How do you account for the increase in lactic acid?Explain, using Le Châtelier’s principle, why the equilibriumconstant for the formation of NO from N2 and O2increases with increasing temperature, whereas the equilibriumconstant for the formation of NO2 from NO and O2decreases with increasing temperature.From this activity, 1.) Which potato sample decomposed the most with hydrogen peroxide? 2.) Which one reacted the least? 3.) What is the function of Catalase in procedure?
- Suppose that the forward rate constant of a reaction is 10-4 and the reverse rate is 10-6. A. What is the equilibrium and deltaG of this reaction? B. Suppose you add a holoenzyme that enhances the reaction 100x. What is the rate constants, equilibrium constants and deltaG of the reaction?please explain why this happends, im having trouble in this section. Part A Chymotrypsin, an enzyme that hydrolyzes peptide bonds in proteins, functions in the small intestine at an optimum pH of 7.7 to 8.0. How is the rate of the chymotrypsin-catalyzed reaction affected by each of the following conditions?How would you find the initial [SCN-] and the Equilibrium [FeSCN2+]?
- The enzyme d-amino acid oxidase has avery high turnover number because the d-amino acids are potentially toxic. The KM for the enzyme is in the range of 1 to2 mM for the aromatic amino acids and in the range of 15 to20 mM for such amino acids as serine, alanine, and the acidicamino acids. Which of these amino acids are the preferred substrates for the enzyme?1 In relation to the redox below from electron transport chain (SuccinateDehydrogenase) Show calculations that proof how oxidation of FADH2 by ubuiqinone(Q) theroteically liberates enough enrgy to drive synthesis of ATP. △G°‘ or ATP synthesis from ADP and π is +30.5kj/mol. Explain calculation in terms of how the oxidation of FAD Hz by ubiquinone supplies sufficient energy for ATP synthesis from ADP and π.A person did estimation of blood glucose level by glucose oxidase method by referring the virtual lab procedure. But he forgot to add ortho - toluidine reagent during glucose oxidase reagent preparation. a) What is the observation of the result? b) Suggest three other chemicals used in place of ortho - toluidine?
- In this reaction, catalase functions as an: a. indicator in the detection of hydrogen peroxideb. emulsifier in the digestion of hydrogen peroxidec. enzyme in the synthesis of hydrogen peroxided. enzyme in the breakdown of hydrogen peroxide3) The enzyme aldolase catalyzes the conversion of fructose-1,6-diphosphate (FDP)to dihydroxyacetone phosphate (DHAP) and glyceraldehide-3-phosphate (G3P). Thereaction isFDP ⇄ DHAP + G3P , ∆rG0(298.15 K) = 23.8 kJ mol−1In red blood cells the concentration of these species are [FDP] = 35 µM, [DHAP] =130 µM, and [G3P] = 15 µM. (Remember that 1.0 µM = 1.0 × 10−6 mol L−1. Thestandard state for reactions in solution can be taken as c0 = 1.0 mol L−1).Calculate ∆rG in a red blood cell at 25 0C. Will the reaction occur spontaneouslyin the cell at this temperature?Explain Why and How Questions???Give the reasons and examples!!Add Structures too!!1- Lyase is similar and different from hydrolyase enzymes? 2- Lactate dehydrogenase is important?