Calculate the equilibrium constant (K'eg) for each of the three reactions at pH 7.0 and 25 °C, using the AGʻ° values given.(a)glucose 6-phosphataseglucose 6-phosphate + H,Oglucose + P;AG'° = –13.8 kJ/molK'eq=(b)B-galactosidaselactose + H,Oglucose + galactoseAG'O= -15.9 kJ/molK'eq= (c)fumarasemalatefumarate + H,0AG'° = 3.1 kJ/molK'eq=

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Answered: Calculate the equilibrium constant…

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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The Keq (25C) of the reaction below is 635.67. Fructose 1,6-biphosphate <-->fructose -6-phosphate + Pi. a) What is the standard Gibbs free energy change for this reaction? b) if the concentrationof fructose 1,6 biphosphate is adjusted to 0.85 M and that of fructose 6 phosphate and phosphate adjusted to 0.055 M, what is the actual free energy change
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 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
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
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.
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
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 equilibrium constant for the hydrolysis of the peptide alanylglycine (Gly-Ala in the reaction from Part B) by a peptidase is K = 9.0 × 10² at 310 K. Calculate AG for this reaction. Express the Gibbs free energy to three significant figures. AG = Submit ΠΑΠΙ ΑΣΦ Request Answer ? kJ/mol Keq [Gly] [Ala] [Gly-Ala]
The following initial-rate data were obtained on the rate of binding of glucose w ith the enzyme hexokinase (obtained from yeast) present at a concentration of 1.34 mmol dm-3. What is (a) the order of reaction with respect to glucose. (b) the rate constant?[C6H12O6]/(mmol dm-3) 1.00 1.54 3.12 4.02vo/(mol dm-3 s-1) 5.0 7.6 15.5 20.0
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.
Calculate the standard free energy for creatine-phosphate hydrolysis in a cell where [creatine-P]=3 mM, [creatine]=2 mM, and [Pi]= 12.1 mM. Is the reaction exergonic or endogonic?

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Calculate the equilibrium constant (K'eq) for each of the three reactions at pH 7.0 and 25 °C, using the AG'º values given.