Draw the missing organic structures in the following multistep synthesis. Show the final product at physiological pH (pH = 7.4). Ignore any inorganic byproducts formed. + 0 O HN 1. NaOCH2CH3 2. CH3I Select to Draw
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- The overall adenylate kinase reaction (2 ADP = AMP + ATP) is a combination of 3 reactions: ATP hydrolysis, pyrophosphate hydrolysis, and ATP formation. Show each step and provide the standard free energy (ΔG°′) for each and the overall reaction. If the adenylate kinase reaction is at equilibrium and intracellular [ATP] = 5 mM and [ADP] = 0.5 mM, calculate the concentration of AMP at pH 7 and 25 °C. Show all work. ATP (ADP+P) = -30.5 kj/mol; ATP (AMP+PP) = -45.6 kj/mol; PP = -19.2 kj/molFrom Table 1.1 indicates, among other things, the melting points of various fatty acids. Analyze the trend that the melting points of saturated fatty acids follow, from n-dodecanoic (CH3-(CH2) 10-COOH) to n-tetracosanoic (CH3-(CH2)22-COOH), and answer both next questions. Briefly justify your answers. i) What value would you expect the melting point of triacontanoic acid (CH3-(CH2) 28-COOH) to have? Choose one of the following options:a) More than 200 ° Cb) About 94 ° Cc) Less than 86 ° Cd) Exactly 86.1 ° C ii) What value would you expect the melting point of octanoic acid (CH3-(CH2) 6-COOH) to have? Choose one of the following options:a) 43.5 ° Cb) -20 ° Cc) About 20 ° Cplease please help me to answer it >>> i have an exam Human xanthine oxidase catalyzes the oxidation of hypoxanthine to xanthine and can furthercatalyze the oxidation of xanthine to uric acid. For the treatment of hyperuricemia and gout,several medications are used to inhibit the activity of xanthine oxidase and reduce theproduction of uric acid. You are a biochemist and just discovered a chemical that can inhibitthe activity of the human xanthine oxidase. When analyzing its mode of inhibition, you foundthat the enzyme inhibitor complex requires 450 J.mol-1 to dissociate and that it displayskinetics somehow similar to noncompetitive inhibition. You sent your inhibitor to the ministryof health for approval as a medication for gout. Based on the data provided, are they going toauthorize it as a medication or not? Explain?
- 1. draw the product in the ff reactions 2. show the ring closure scheme for the glucose molecule3) 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?Which of the reactions are spontaneous (favorable)? 1)DHAP↽−−⇀glyceraldehyde-3-phosphateΔ?=3.8 kJ/mol 2)L-malate+NAD+⟶oxaloacetate+NADH+H+Δ?=29.7 kJ/mol- 3) glutamate+NAD++H2O⟶NH+4+α-ketoglutarate+NADH+H+Δ?=3.7 kcal/ 4) C6H13O9P+ATP⟶C6H14O12P2+ADPΔ?=−14.2KJ/mol 5) −Rh(I)C2H6Δ?=−150.97 kJ/molC2H4+H2→Rh(I)C2H6ΔG=−150.97 kJ/mol 6) C4H4O5⟶C4H2O4+H2OΔ?=3.1 kJ/mol
- In one of the steps in this pathway fructose 1,6-biphosphate (F1,6BP) is converted to gylceraldehyde-3-phosphate (G-3-p) and dihydroxyacetone phosphate (DHAP). This reaction is catalyzed by the enzyme aldolase. For this reaction at 25 celcuius and Ph7 we have: Keq= 10-4M and Delta G = +5456 cal/mol Calculate the following: The concentration of F1, 6BP, DHAP and G-3-P at equilibrium when the initial F1,6BP is (A) 1M, (b) 10-2 M, (c) 2 X 10*4 M and (d) 10-5 M. I been trying to solve this problem but I dont even know where to begin with. Atleast help me with problem A, I would be able to guide myself through.In step 7 of fatty-acid biosynthesis (Figure 29-5), dehydration of a -hydroxy thioester occurs to give trans-crotonyl ACP. Is the dehydration a syn elimination or an anti elimination?One of the steps in the metabolic degradation of guanine is hydrolysis to give xanthine. Propose a mechanism.
- Assume that acetyl CoA containing a 14C isotopic label in the carboxyl carbon atom is used as starting material for the biosynthesis of mevalonate, as shown in Figure 27-7. At what positions in mevalonate would the isotopic label appear?When some sugars dissolve in water they spontaneously undergo changes in optical rotation called mutarrotation. The Mutarrotation of D-glucopyranose is catalyzed by acid and bases. 2-Hydroxypyridine is a more effective catalyst than phenol and pyridine for this reaction because: a.Both oxygen and N in 2-hydroxypyridine act as bases increasing the rapid interconversion of sugar b. The OH of 2-hydroxypyridine serves as the base while the current N as the acid. c. 2-hydroxypyridine acts both as a base to remove the proton from the hydroxyl group in the hemiacetal and as an acid to provide a proton to the oxygen in the hemiacetal. d.Phenol and pyridine are very expensive.When in contact with the body, Methanol is oxidised to Methanal by ____________ . Select your answer. KMnO4 Aldehyde Dehydrogenase Chromic Acid Alcohol Dehydrogenase