Acetyl-CoAAG" = -7.7 kcal/molCOAFatty acidsOxaloacetateCitrateAG" = -1.5 kcal/molIsocitrateKrebs 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.

The free energy change (∆Gº) of a chemical reaction is the amount of energy released in the…

Answered: Acetyl-CoA AG" = -7.7 kcal/mol COA…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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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 acids
Acetyl CoA + 2H* + 2e = pyruvate + COASH E = -0.48 V Ubiquinone + 2H* + 2e = Ubiquinol E" = +0.04 V Consider the redox rxn wherein a pair of e passes from pyruvate to ubiquinone. Calculate the change in standard Gibbs free energy (kJ/mol). Report answer to two decimal places.
Given the following data, calculate Keq for the denaturation reaction of the protein β-lactoglobin at 25oC: ΔH° = –88 kJ/mol ΔS° = 0.3 kJ/mol. The free energy of hydrolysis of ATP in systems free of Mg2+ is −35.7 kJ/mol. When the concentration of this ion is 5 mM, ΔG°observed is approximately −31 kJ/mol at pH 7 and 38°C. Suggest a possible reason for this effect.
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;) -30.5
Pyruvate carboxylase catalyzes the first step of gluconeogenesis. ATP + HCO3─ + pyruvate → oxaloacetate + ADP + Pi ∆G0’ = ─2.1 kJ mol-1 a) Calculate ΔG for this reaction under the following physiological conditions: 370C, pH 7 [pyruvate] = [HCO3─] = 4.0 mM [oxaloacetate]= 2.0 mM [ATP] = 3.5 mM [Pi] = 5.0 mM [ADP] = 1.8 mM
Calculate what the intracellular glucose concentration should be if to transport glucose in active form from the external medium (c1 = 5 mM) at 37 ºC, a energy input of + 2970 J / mol.
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.
Determine the values of KM and Vmax for the decar-boxylation of a β-keto acid given the following data. You have to plot the graph by using excel. Please include slope Substrate Concentration (mol L1) Velocity (mM min1)2.500 0.5881.000 0.5000.714 0.4170.526 0.3700.250 0.256
The glucose/glucose-6-phosphate substrate cycle involves distinct reactions of glycolysis and gluconeogenesis that interconvert these two metabolites. Assume that under physiological conditions, [ATP] = [ADP]; [P;] = 1 mM. Consider the glycolytic reaction catalyzed by hexokinase: ATP + glucose ADP + glucose-6-phosphate AG = - 16.7 kJ/mol (a) Calculate the equilibrium constant (K) for this reaction at 298°K, and from that, calculate the maximum [glucose-6-phosphate]/ Iglucose] ratio that would exist under conditions where the reaction is still thermodynamically favorable. (b) Reversal of this interconversion in gluconeogenesis is catalyzed by glucose-6-phosphatase: glucose-6-phosphate + H20 = glucose + P AG" = -13.8 kJ/mol
Consider the following equilibrium at 25ºC :Glucose-1-Phosphate Glucose-6-PhophateUsing the equilibrium concentrations of [Glucose-1-Phosphate] = 0.35 M and [Glucose-6-Phosphate] = 1.65 M, calculate BOTH K′eqand Gº′ for this reaction. Is this reaction exergonicor endergonic? R = 8.314 J/K·mol
In working skeletal muscle under anaerobic conditions, glyceraldehyde 3-phosphate is converted to pyruvate (the payoff phase of glycolysis), and the pyruvate is reduced to lactate. Write balanced biochemical equations for all the reactions in this process, with the standard free-energy change for eachreaction. Then write the overall or net equation for the payoff phase of glycolysis (with lactate as the end product), including the net standard free-energy change.
Calculcate Kcat for PNP substrate for both enzyme concentrations. enzyme volume: 20 ul Bovine Intensince Alkaline phosphatase molecular weight: 140,000 Bovine intenstine Alkaline phosphatase activity: 300 units/ml and 14 units/mg extinction coefficient PNP: 18.5 abs (mM-1 cm-1) Vmax: 0.332 moles/sec a) enzyme 1 concentration: undiluted b) enzyme 2 concentration: 1:1 dilution

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