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- 6F. What conformational state is stabilized by y in ATP synthase? Why might achieving this state require energy input from the PMF?Calculate the ATP yield for the full catabolism of a phospholipid containing ethanolamine, C18:3 Δ9, 12, 15 and oleic acid. Include any ATP “expenses” or “income”. This will be a complex problem—neatly show your work and justify your choices.2B. Calculate the total number of ATP that will be generated from the complete B-oxidation of oncobic acid (CH:(CH,),CH=CH(CH,),COOH; 15:1 cis-A9) in an organism that has all the standard required enzymes for metabolism but which pumps only 2 H" in complex I, 0 H' in complex II, 2 H* in complex III and 4 H' in complex IV. The F,F, ATPase is composed of 3 a/ß subunits and 10 c subunits. Show all of your calculations. HO
- Is increasing the P; concentration a reasonable way to couple ATP hydrolysis and glucose phosphorylation? Yes. Increasing the concentration of P; would decrease K'eq and shift equilibrium to the right. No. The phosphate salts of divalent cations would be present in excess and precipitate out. No. The extra P; would give a negative AG", but would give a positive AG. Yes. The extra ATP hydrolysis would provide enough free energy to drive the phosphorylation reaction.The phosphorylation of glucose to glucose 6-phosphate is the initial step in the catabolism of glucose. The direct phosphorylation of glucose by P, is described by the equation Glucose + P→ glucose 6-phosphate + H₂O AG 13.8 kJ/mol = Coupling ATP hydrolysis to glucose phosphorylation makes thermodynamic sense, but consider how the coupling might take place. Given that coupling requires a common intermediate, one conceivable mechanism is to use ATP hydrolysis to raise the intracellular concentration of P₁. The increase in P; concentration would drive the unfavorable phosphorylation of glucose by P₁.6E. Draw a reaction coordinate diagram describing the different steps of ATP synthase catalysis, comparing the relative free energy of each state. What is the rate-limiting step in ATP synthase catalysis in the direction of ATP synthesis?
- CHO CHO CH,OH HO- H Phosphorogluco- isomerase Phosphofructo- kinase Hexokinase но H. но -H- но H- HO- АТР ADP H- HO- -HO- OH H- OH H- OH Via H- -HO- ATP ADP CH2OH CH,OPO,2 ČH,OPO,2 Но nin Glucose A B CH,OPO,2- CH2OPO, Fructose Fo D CH2OH Но H- biphosphate H- HO. HPO,2 / NAD+ / Triose aldolase OH Glyceraldehyde 3- phosphate dehydrogenase phosphate isomerase CH,OPO,2 Via OPO,2 сно HOH E CH,OPO, H- OH LOH CH,OPO, For CH,OPO,2 G COPO,2 он H3C HO. Pyruvic AcidWhy does ATP hydrolysis release so much energy? O Hydrolysis increases entropy through a gain in the possible resonance structures for Pi versus a terminal phosphate O Hydrolysis decreases entropy through a loss in the possible resonance structures for Pi versus a terminal phosphate O Hydrolysis decreases enthalpy through a loss in the possible resonance structures for Pi versus a terminal phosphate O Hydrolysis increases enthalpy through a gain in the possible resonance structures for Pi versus a terminal phosphateThis is the ATP accounting question. You are limited to the carbon in the following molecules: One xylulose 5-phosphate, One glyceraldehyde 3-phosphate, One sedoheptulose 7-phosphate, 1 Oxaloacetate, and 3 carbon dioxide A) Disregard regulation completely regarding pathway activity, using only the enzymes of glycolysis, pentose phosphate pathway, and citric acid cycle, what is the maximum ATP one can generate with these molecules? B) Disregard regulation completely regarding pathway activity, using only the enzymes of glycolysis, Calvin- Benson-Bassham cycle, and citric acid cycle, what is the maximum ATP one can generate with these molecules (in this instance only, you also are given 3 ATP and note that you do NOT need to regenerate substrates for rubisco once you get through this enzyme).
- (d) of glucose oxidation in diabetic human patients treated with Metformin (●) and in (nondiabetic) control human patients (0). At –150 min both groups of subjects were started on an intravenous feed of 3-(®H)-glucose, and at t = 0 min they were started on an oral glucose tolerance test whereby a measured amount of glucose in water (a syrupy mixture) was swallowed followed by measure- ment of blood glucose levels at 30 min intervals. The flux of glucose oxidation was measured by the appear- ance of 3H2O in the blood stream. While the information The diagram to the right compares the rate 8000 ORAL GLUCOSE 6000- 4000- 2000- -120 -60 60 120 180 240 300 Minutes cannot be directly extracted from the reaction mecha- nism diagrams in the textbook, the glycolytic step in which the tritium is first released into water is that catalyzed by TPI, as illustrated at the beginning of Question #3. Explain why this step is suitable for measuring the flux of glycolysis through the release of °H…3. Triose-phosphate isomerase (TPI) catalyzes the movement of a single proton to interconvert dihy- droxyacetone phosphate and glyceraldehyde 3-phosphate in glycolysis and gluconeogenesis. The enzyme, a dimer of identical subunits that are 248 amino acids in humans, has no cofactors, required metal ions, or cooperativity between subunits. The enzyme is found in all tissues. The value of Kcat/KM - 9.2 x 106 sec-'M-1 is close to the rate constant expected for a diffusion-limited reaction. The mechanism of the proton transfer is illustrated in the diagram below. Glu-165 Giu-165 Glu-165 ks HR H 20,PO HO, OH His-95 His-95 His-95 (a) ing structural formulas and naming enzymes and glycolytic intermediates, the reactions of the payoff phase. Consider only anerobic glycolysis. Remember that each glucose molecule yields two mole- cules of glyceraldehyde-3-phosphate (GAP). Indicate the net yield of ATP and NADH generated through anaerobic glycolysis per glucose molecule. The reaction catalyzed by…The glyceraldehyde-3-phosphate dehydrogenase reaction of glycolysis, (glyceraldehyde-3- phosphate → 1,3 bisphosphoglycerate) (Choose all that apply) O conserves energy by transfer of a proton H* to NAD+ forming NADH O has a high energy thioester intermediate on the enzyme/substrate complex O mechanistically uses covalent catalysis O conserves energy in the formation of a oxygen phosphoric ester O conserves energy in the formation of a carboxylic-phosphoric mixed anhydride O mechanistically requires the coenzyme thiamine pyrophosphate (TPP) to act as an electron sink