10. Calculating AG in a Rat Liver Cell Calculate the free energy of hydrolysis of ATP in a rat liver cell in which the ATP, ADP, and P₁ concentrations are 3.4, 1.3, and 4.8 mM, respectively.
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- 23. Calculate the free energy of hydrolysis ATP in a rat liver cell in which the ATP, ADP, and Pi concentrations are 3.4, 1.3, and 4.8 mM, respectively. AG" for this hydrolysis -31.5 kJ/mol1. a. Calculate the physiological DG of the reaction shown below at 37°C, as it occurs in the cytosol ofneurons, with phosphocreatine at 4.7 mM, creatine at 1.0 mM, ADP at 0.73 mM, and ATP at 2.6mM. The standard free energy change for the overall reaction is –12.5 kJ/mol. Phosphocreatine + ADP ® creatine + ATP b. The enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose6-phosphate. Calculate the standard free energy change of this reaction if incubation of 20 mMglucose 1-phosphate (no glucose-6 phosphate initially present) yields a final equilibrium mixtureof 1.0 mM glucose 1-phosphate and 19 mM glucose 6-phosphate at 25°C and pH 7.0. c. If the rate of a nonenzymatic reaction is 1.2 x 10–2 μM s–1, what is the rate of the reaction at 37℃ inthe presence of an enzyme that reduces the activation energy by 30.5 kJ/mol?Explain the difference between ΔG°’ and ΔG and calculate the free energy (delta G) of hydrolysis of ATP in a rat liver cell in which the ATP, ADP, and Pi concentrations are 3.4, 1.3, and 4.8 mM.
- Calculate the actual, physiological AG for the reaction Phosphocreatine + ADP = creatine + ATP at 37 °C, as it occurs in the cytosol of neurons, where [phosphocreatine] = 4.7 mM, [creatine] = 1.0 mM, [ADP] = 0.73 mM, and [ATP] = 2.6 mM. Standard Free Energies of Hydrolysis of Some Phosphorylated Compounds Phosphorylated compound AGʻ° (kJ/mol) phosphoenolpyruvate -61.9 phosphocreatine -43.0 ADP (→ AMP + P;) -32.8 ATP (→ ADP + P;) -30.528. If 20 mM solution of Acetyl-phosphate is transformed to acetate by incubating with a catalytic amount of acetate kinase until equilibrium is reached. Acetyl-phosphate -> Acetate + Pi At equilibrium, the concentration of Acetyl-phosphate is 8 mM. Determine Keq and AG" for the hydrolysis of Acetyl-phosphate reaction. (R = 0.008314 kJ/mol K) .2. Calculate AG for the exchange of 3 Na* by 2 K* by Na*-K* ATPase (in kJ per mole of ATP) under the following conditions: 3 Na*(in) + 2 K*(out) + ATP + H2O → 3 Na*(out) + 2 K*(in) + ADP + Pi [K*]in [Na*]n [K*Jout [Na*Jout = 5 mM = 150 mM = 140 mM = 10 mM AY = Membrane Potential = -70mV Temperature = 37 °C Free Energy of Hydrolysis of ATP (ATP + H2O → ADP + P:): AG = -51.5 kJ/mol Hint: Since values of AG are additive, first calculate AG for transport of 1 mole of K* and for transport of 1 mole of Na* individually. These values can then be used, adjusted for the stoichiometry in the balanced equation, along with AG for hydrolysis of ATP to calculate AG for the overall reaction.
- 2.For question number 1 if a mixture was prepared containing 1 M Glucose 6-Phosphate and 0.001 M Glucose 1-Phosphate the ∆G for this reaction is: included question 1 however, need help with 2 and provided the option for the answer 1.What is the Keq for the conversion of Glucose 1-Phosphate to Glucose 6-Phosphate if the phosphate transfer potential for Glucose 1-Phosphate and Glucose 6-Phosphate are 20.9 kJ/mol and 13.8 kJ/mol respectively?Inside cells, the AG value for the hydrolysis of ATP to ADP + Pi is approximately -50 kJ/mol (-12 kcal/mol). Calculate the approximate ratio of [ATP] to [ADP][Pi ] in cells at 37°C. AG = AG + RT InKe R= 8.315 x 10³ kJ mol deg T= 298 K Table 15.1 Standard free energies of hydrolysis of some phosphorylated compounds Compound kJ mol- kcal mol- Phosphoenolpyruvate 1,3-Bisphosphoglycerate Creatine phosphate ATP (to ADP) -61.9 -14.8 -49.4 -11.8 -43.1 -10.3 -30.5 - 7.3 - 5.0 Glucose 1-phosphate Pyrophosphate Glucose 6-phosphate -20.9 -19.3 -4.6 -13.8 3.3 Glycerol 3-phosphate - 9.2 2.2 biochemistryCalculate the standard free-energy change of the reaction catalysed by the enzyme phosphoglucomutase Glucose- 1-P = Glucose-6-P, given that, starting with 28.29 mM Glucose-1-P and no Glucose-6-P, the final equilibrium mixture at 25°C and pH=7.0 contains 9.77 mM Glucose-6-P and the remaining Glucose- 1-P. Give the answer in J/mol.K to one decimal place.
- Substrate Concentration (mol L1) Velocity (mM min-1) 2.500 0.588 1.000 0.500 0.714 0.417 0.526 0.370 0.250 0.256 Determine the values of Km and Vmax for the decarboxylation of a 훃-keto acid given the followingdata. You have to plot the graph by using excel and please include the scope of graph5) In an experiment to investigate the inhibition of the enzyme-glucosidase the following data for the rates of reaction with glucopyranoside for various substrate concentrations was obtained. By constructing a Leaver-Burk plot, determine the value of the Michaelis constant. [S]/ (10-6 mol dm-3) v/ (10-3 mol dm-3 s-1) 1.00 2.00 3.00 4.00 16.7 33.3 41.1 49.8Determine the values of Km and Vmax for the decarboxylation of β-keto acid given the following data. Please show and label your plot. Show your calculations and box your final [S] in mol/l V in mM/ min 2.500 0.588 1.000 0.500 0.714 0.417 0.526 0.370 0.250 0.256