(i) Describe B-oxidation steps for an even chain saturated fatty acid. (ii) How many molecules of ATP could be produced from the complete oxidation of the 19 carbon saturated fatty acid, nonadecanoic acid (19:0)?
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- Acetyl-CoA, AG"=-7.7 kcal/mol COA Oxaloacetate Citrate AG" = ? AG"=-1.5 kcal/mol Isocitrate Krebs cycle is equilibrium at 25°C with coupled fatty acid biosynthesis. Calculate the free energy of the fatty acid biosynthesis (in kcal/mol), accounting for the concentrations of Oxaloacetate - 0.005 mM; Acetyl-CoA -0.03 mM; Citrate - 0.01 and Isocitrate - 0.0006 mM. Fatty acids64 Consider docosanoic acid, C2H43 CO₂H. a. Label the x and ß carbons. b. Draw the acyl CoA derived from this fatty acid. c. How many acetyl CoA molecules are formed by complete B-oxidation? d. How many cycles of ß-oxidation are needed for complete oxidation? e. How many molecules of ATP are formed from the complete catabolism of this fatty acid? Required:Acetyl-CoA AG" = -7.7 kcal/mol COA Fatty acids Oxaloacetate Citrate AG" = -1.5 kcal/mol Isocitrate Krebs cycle is equilibrium at 25°C with coupled fatty acid biosynthesis. Calculate the free energy of the fatty acid biosynthesis (in kcal/mol), accounting for the concentrations of Oxaloacetate – 0.005 mM; Acetyl-CoA - 0.03 mM; Citrate - 0.001mM and Isocitrate – 0.06 mM.
- (i) Consider a preparation that contains all the enzymes and cofactors necessary for fatty acid biosynthesis from acetyl-CoA and malonyl-CoA. If [2-H] acetyl-CoA labeled with deuterium, the heavy isotope of hydrogen and excess of unlabeled malonyl-CoA are added as substrates, where will you find these labeled deuterium atoms in a molecule of palmitate synthesized? Explain. S-COA (ii) Describe the steps involved in the synthesis of palmitic acid starting from acetyl-CoA and malonyl-CoA.25. The AG" values for the two reactions are given. 1. 2. oxaloacetate + acetyl-CoA + H₂O → citrate + COASH oxaloacetate + acetate → citrate Enzymes for reactions 1 and 2 are citrate synthase and citrate lyase, respectively. Determine the AG" for the hydrolysis of acetyl-CoA acetyl-CoA + H₂O acetate + COASH + H+ plane een isoimorfbold bns (94) opg Vp1903 9911 AG¹⁰ ? AGO = -32.2 kJ/mol AG"=-1.9 kJ/molConsider docosanoic acid C12H43CO2H a. Label the alpha and beta Carbons. Show the beta-oxidation in an EXPANDED structure. b. Draw each acyl CoA derived from this fatty acid. c. How many acetyl Co A molecules are formed by complete beta-oxidation? d. How many cycles of beta-oxidation are needed for complete oxidation? e. How many molecules of ATP are formed from the complete catabolism of this fatty acid? Show the complete computation. f. How many moles of ATP per gram of fatty acid is formed from the complete catabolism of the given fatty acid? g. What is the molar mass of the given fatty acid? Solution: Show here the complete computations, [from a to e]
- For myristic acid, C 13H 27CO 2H: (a) How many molecules of acetyl CoA are formed from complete β-oxidation? (b) How many cycles of β-oxidation are needed for complete oxidation?Considering the fatty acids: (a) Arachidic acid (C20H40O2); molar mass = 312.5 g/mol) (b) Palmitoleic acid (C16H30O2); molar mass = 256.4 g/mol). How many cycles of β -oxidation are needed for complete oxidation? How many molecules of acetyl CoA are formed from its complete catabolism? How can you calculate the number of molecules (moles) of ATP formed (net) by the complete catabolism of each fatty acid? and the number of moles of ATP formed per gram of each fatty acid metabolized??A. The inhibitor constants for three inhibitors of por- cine citrate synthase are summarized in the table on the right. The compounds were all determined to bind in the active site as competitive inhibitors of acetyl-CoA. Because they bind as competitive inhibitors, all three inhibitors must exhibit structural similarity to some part of acetyl-CoA. Look up in the textbook the structural formu- las for Coenzyme A, ATP, and NADH. What is the largest structural fragment of each inhibitor that is responsible for competitive inhibition? Draw the molecular fragment common to each inhibitor that competes with the binding of acetyl-CoA in the active site of citrate synthase. Bromoacetyl-CoA ATP NADH K₁ (μM) 25.7 6800 8300 B While the inhibitor constants listed in part (b) above were determined in vitro for purified citrate synthase, does their inhibitory action have any relevance to the flux of metabolites through the TCA cycle in vivo? If so, explain.
- (b) ☐ The exergonic reactions catalyzed by isocitrate dehydrogenase (ICDH) and α- ketoglutarate dehydroge-nase (aKGDH) are regu- lated by metabolites, in addition to the reaction catalyzed by citrate synthase. The diagram to the right illustrates the activity of ICDH (A,▲) and aKGDH (O,●) in the presence of 1.5 mM ADP (O,A) or 1.5 mM ATP (●,▲). In muscle tissue contraction of sarcomeres initiated by a nerve im- pulse results first in the release of Ca 2+ from the sarcoplasmic reticulum. As indicated by the chang- es in velocity of the two enzymes, what are the flux changes of the TCA cycle in muscle tissue upon release of Ca2+ under the influence of ADP viz. ATP and under the influence of NAD+ viz. NADH on cit- rate synthase? 100 75 Stimulation of activity (% of maximum) ŏ 25 1. -8 -7 -6 log {[Ca2+] (M)}Palmitoleic acid, 16:1Δ⁹ hexadecaenoic acid, (16 carbon FA with one double bond )is an important fatty acid component of TAGs and cell membranes. Briefly explain the process of beta oxidation of this fatty acid and the number (only) of FADH, NADH and acetyl CoA outcome. What is the total ATP (only number) generated from this fatty acid after beta oxidation.Page of 6 ZOOM + name: 3. In the last reaction of the citric acid cycle, malate is dehydrogenated to regenerate the oxaloacetate necessary for the entry of acetyl-CoA into the cycle: L-Malate + NAD+ → oxaloacetate + NADH + H* AG'° = 30.0 kJ/mol (a) Calculate the equilibrium constant for this reaction at 25 °C. (b) Because AG°' assumes a standard pH of 7, the equilibrium constant calculated in (a) corresponds to [oxaloacetate][NADH] Keq [L-malate][NAD*] The measured concentration of L-malate in rat liver mitochondria is about 0.20 mM when [NAD*]/[NADH] is 10. Calculate the concentration of oxaloacetate at pH 7 in these mitochondria. (c) To appreciate the magnitude of the mitochondrial oxaloacetate concentration, calculate the number of oxaloacetate molecules in a single rat liver mitochondrion. Assume the mitochondrion is a sphere of diameter 2.0 microns.