Glucose 1-phosphate is converted into fructose 6-phosphate in two successive reactions.Reaction 1: Glucose 1-phosphate→ glucose 6-phosphateAG'° = -7.3 kJ/molReaction 2: Glucose 6-phosphate→ fructose 6-phosphateAGʻ° = +1.7 kJ/molUsing the values given, calculate the standard free-energy change, AGʻ°,,for the sum of the two reactions:sum >Sum:Glucose 1-phosphate→ fructose 6-phosphateAG'°,kJ/molsumCalculate the equilibrium constant, K',eq >for the sum of the two reactions.K'eeqII

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Answered: Glucose 1-phosphate is converted into…

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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Calculate 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.
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
The standard free energy change for the reaction catalyzed by phosphoglucomutase is -7.1 kJ/mol. Calculate the equilibrium constant for the reaction. Calculate AG at 37°C when the concentration of glucose-1-phosphate is 1-mM and the concentration of glucose-6-phosphate is 25-mM. Is the reaction spontaneous under these conditions? HOCH, -20;POCH, H H H H H H ОН Н НО ОН Н H НО ОН H ОН H. ОН Glucose-l-phosphate Glucose-6-phosphate
The ΔG°′ for hydrolytically removing a phosphoryl group from ATP is about twice as large as the ΔG°′ for hydrolytically removing a phosphoryl group from AMP (−14 kJ · mol−1). Explain the discrepancy.
What terms would best describe the above coupled reaction? (If the DGo for ATP hydrolysis into ADP + inorganic phosphate is -7.3 kcal/mole, and the DGo for maltose synthesis from glucose + glucose is +3.7 kcal/mole, calculate the standard free energy change for the combined reaction of ATP + glucose + glucose g ADP + maltose + inorganic phosphate.) it is non-spontaneous and endothermic (because the overall DGo is negative) it is spontaneous and exothermic (because the overall DGo is negative) it is non-spontaneous and endothermic (because the overall DGo is positive) it is spontaneous and exothermic (because the overall DGo is positive) it is non-spontaneous and exothermic (because the overall DGo is negative)
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 biochemistry
If a 0.1 M solution of glucose 1- phosphate at 25 °C is incubated with a catalytic amount of phosphoglucomutase, the glucose 1-phosphate is transformed to glucose 6-phosphate. At equilibrium, the concentrations of the reaction components are Calculate Keq and ΔG′° for this reaction.
The effect of temperature on the hydrolysis of lactose by a ß-galactosidase is shown below in Table 1. The temperature coefficient, Q10 is the factor by which the rate increases by raising the temperature 10°C. The universal gas constant, R is 8.314 J/mol.K. (a) (b) Table 1: Data of Vmax over temperature T (°C) 20 30 35 40 45 Vmax (umoles/min.mg protein) 4.50 8.65 11.80 15.96 21.36 Plot the graph of In Vm vs 1/T using any spreadsheet software (include all appropriate labels and equation). Calculate the activation energy Ea and temperature coefficient Q10.
Consider the following phosphoryl group transfer reaction which is the first step in glucose catabolism by glycolysis: Glucose + ATP + Glucose 6-phosphate + ADP The AG for the reaction is -16.7 kJ/mol. (R= 8.314 J/(K. mol) (a) Calculate Keq for the reaction at 25°C (b) What is the ratio of [Glucose 6-phosphate] to [Glucose] if the ratio of [ADP] to [ATP] is 10?
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.
ATP can be hydrolyzed into ADP + inorganic phosphate (P.) with a AG of -30500 J/mol. If, galactose-1-phosphate can be hydrolyzed into galactose + P, with a AG of -15.3 kJ/mol what is the Gibbs free energy change for the reaction of galactose + ATP = galactose-1-phospate + ADP? O a. -45.8 kJ/mol O b. 15.2 kJ/mol Oc. -30484.7 J/mol O d. -15.2 kJ/mol Oe. -1520 J/mol
A) Calculate the Gibbs free energy change for the following reaction: Fructose diphosphate If the reaction is performed at 27°C and AH is 1,246 calories and AS is 4 calories/K. Is this a spontaneous or non-spontaneous reaction. Why? Is the reaction endergonic or exergonic? DHAP+ Glyceraldehyde phosphate

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