Calculate the overall ΔG° (report up to two decimal places) for the net reaction (see attached image).
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Calculate the overall ΔG° (report up to two decimal places) for the net reaction (see attached image).
Answer: _____ kcal/mol
Note: R = 1.98 x 10 -3 kcal/mol-K
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- The oxidation of 1 mol of glucose supplies enough metabolic energy to form 36 mol of ATP. Oxidation of 1 mol of a typical dietary fat like tristearin (C57H116O6) yields enough energy toform 458 mol of ATP. How many molecules of ATP can form per gram of (a) glucose; (b) tristearin?G6P(ag) F6P(aq) AG°=+1.7kJ/mol at 25 °C Consider the reaction: Estimate the fraction of F6P (Fructose 6 Phosphate) in equilibrium with G6P (Glucose 6 Phosphate) at 25 °C, where the fraction is defined as [F6P]/([F6P]+[G6P]). Show ALL your work.The enzyme aldolase catalyzes the reaction shown in the glycolytic pathway: Fructose 1,6-bisphosphate dihydroxyacetone phosphate + glyceraldehyde 3-phosphate The AG" for the reaction is +23.8 kJ mol¯¹ (+5.7 kcal mol−¹), whereas the AG in the cell is −1.3 kJ mol¯¹ (−0.3 kcal mol¯¹). Calculate the ratio of products to reactants under standard (equilibrium) conditions at 37°C. [products] [reactants] 7 x10-5 [products] [reactants] Incorrect Aldolase ===== Calculate the ratio of products to reactants under intracellular conditions at 37°C. 4 ×10-5 Incorrect Complete the statement using your results. under standard conditions under intracellular conditions A reaction that is endergonic under standard conditions can be converted into an exergonic reaction by maintaining the ratio of products to reactants below the equilibrium value.
- The dissociation of lactic acid to lactate is shown in the reaction. Lactic acid has a pKa of 3.86. OH Lactic acid OH OH Lactate + H+ A solution containing a mixture of lactic acid and lactate was found to have a pH of 5.10. Calculate the ratio of the lactic acid concentration to the lactate concentration in this solution. [lactic acid]/[lactate] =The protein catalase is an enzyme that catalyzes the decomposition of hydrogen peroxide:2 H2O2 (aq) → 2 H2O (l) + O2 (g)and has a Michaelis-Menten constant of 25 × 10-3 mol·dm-3 and a turnover number of 4.0×107s-1.The total enzyme concentration is 0.016×10-6 mol·dm-3 and the initial substrate concentration is4.32×10-6 mol·dm-3 Calculate the maximum reaction rate (????) for this enzyme, and the initial rateof this reaction. Note that catalase has a single active site.The hydrolysis of sucrose has the following data. Time (min) 0 30 60 90 130 180 [Sucrose] (M) 0.5011 0.4511 0.4038 0.3626 0.3148 0.2674 Sucrose + H₂O → glucose + fructose Unistanit. Determine the half-life. (Use the order from a.) You will need to take into account the order!
- The inilial reactions in the biosynthesis of the amino acid aspartate at 298 K are: Carbamoyphoephate Cartamoyi + phosphate ADP + phoaphate - ATP AO=-12,300 calmol AG-T800 calimol Which of the following statements is gorrect? A) The energy which is released fron the conversion of 1 mole of carbamoyphosphate to carbamoyl+ phosphate (P) in reaction I is sufficient to drive the synthesis of 1 mole of ATP in reaction II. B) AG for the reaction Carbamoyphosphate + Carbamoyl + phosphate is +123 kcalimol. c) AHP for reaction I cannot be detemined trom the information given. D) Al of the above. E) None of the above.fructose-6-phosphate + ATP fructose-1,6- biphosphate + ADP AG° = 30.5 and 16.3 respectively Standard Free Energy change: -14.2 kj/mol ATP: 3mM, ADP: 0.4mM, fructose-1,6-biphosphate: 7mM %3D At what concentration of fructose-1,6-biphosphate would the reaction proceed backwards at 35°C?Consider the fructose-1,6-bisphosphatase reaction. Calculate the free energy change if the ratio of the concentrations of the products to the concentrations of the reactants is 23.7, and the temperature is 37.0 °C? AG" for the reaction is -16.7 kJ/mol. The constant R = 8.3145 J/(mol-K) AG= Number kJ/mol
- 3. 1,3-bisphosphglycerate has a high energy bond that can be used to phosphorylate ADP to make ATP according to the equation below. The free energy of hydrolysis of 1,3- bisphophoglycerate and ATP under standard conditions are -49.4 kJ/mol and -30.5 kJ/mol, respectively. If the [ATP] to [ADP] is about 4 in the cell, how much 1,3-bisphophoglycerate is needed relative to 3-phosphoglycerate to keep this formation of ATP spontaneous? -203PO. H- -OH -OPO3-² + ADP H- -OH -OPO3-² + ATPIn the degradation of glycogen, the purpose of the debranching enzyme is to remove the last four glucose molecules from branches structure of glycogen. It does this by catalyzing three different reactions. Use the equations below to answer parts a-c. Synthesis of α(1,6) link ΔG = +7.1 kJ Hydrolysis of α(1,4) link ΔG = ─15.5 kJ a)What are the three chemical reactions performed during the removal of the last four glucose molecules of the branching structure of glycogen? b) Calculate ΔG for each of the three reactions described in part a. c) Now calculate the overall energy change for the net reaction carried out by this enzyme. d) Why is this reaction favorable?Given that the AG" values for the hydrolysis of glucose 1-phosphate and glucose 6-phosphate are approximately -21 kJ/mol and –14 kJ/mol, respectively, which statement is true regarding the isomerization shown? glucose 1-phosphate → glucose 6-phosphate O The reaction can likely proceed in either direction and will therefore depend on the concentrations of glucose 1-phosphate and glucose 6-phosphate. O Only the anabolic direction will occur because the free energy change is positive. O The reaction will proceed in both directions simultaneously. This reaction can only proceed in one direction and must be the rate limiting reaction for this point in metabolism.