Assume that you have a solution of 0.1 M glucose 6-phosphate. To this solution, you add the enzyme phosphoglucomutase,which catalyzes the reaction:Glucose 6-phosphateglucose 1-phosphateThe standard free-energy change (AGº') for the reaction is +7.5 kJ mol¯¹ (+1.8 kcal mol−¹).PhosphoglucomutaseWhat is the final concentration of glucose 6-phosphate (G6P)?[G6P] =What is the final concentration of glucose 1-phosphate (G1P)?[G1P] =MM Does the reaction proceed as written?Yes, because the standard free-energy change for the reaction is positive.No, because the equilibrium constant is less than 1, which favors the reactant.Yes, because the enzyme will shift the equilibrium point toward the product.Yes, because the reactant concentration is much higher than the product concentration at equilibrium.Under what cellular conditions could you produce G1P at a high rate?Supply G1P and G6P at a high rate.Supply G1P at a high rate and remove G6P at a high rate by other reactions.Supply G6P at a high rate and remove G1P at a high rate by other reactions.Remove G1P and G6P at a high rate by other reactions.

Standards free energy change calculated at biochemical standards is called biochemical standard free…

Answered: Assume that you have a solution of 0.1…

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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Assume that you have a solution of 0.1 M glucose 6-phosphate. To this solu- tion you add the enzyme phosphoglucomutase, which catalyzes the reaction: glucose-6-P = glucose-1-P AG' = +1.7 kJ/mol (a) Does this reaction proceed at all as written at 25 °C, and if so, what are the final concentrations of glucose 6-P and glucose 1-P? (b) What effect would omitting the enzyme have on the reaction. Be specific. (c) Under what cellular conditions, if any, would this reaction continuously produce glucose 1-P at a high rate?|
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
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.
Carbonic anhydrase catalyzes the hydration of CO. CO2 + H2O ¬ H½CO3 The Km of this enzyme for CO, is 1.20×104 µ.M. When [CO,] = 3.60×104 µM, the rate of reaction was 4.50 umol·mL! sec-1 a What is Vmax for this enzyme? umol·mL-!sec-!
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 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
[References) The AG" for the reaction ATP + H₂O ADP + P + H+ is -30.5 kJ mol'¹, Other organophosphate species also undergo hydrolysis of the phosphate moiety via a similar reaction. Determine the value of AG for the following reactions and indicate if the reaction will proceed spontaneously in the direction written if the reactants and products are initially in a 1:1 molar ratio. a. ATP + Glucose ADP+ Glucose-1-phosphate AG⁹¹ = kJ mol-1 The reaction is (The hydrolysis reaction for glucose-1-phosphate is Glucose-1-phosphate + H₂0 Glucose + P + H+; AG-20.9 kJ mol ¹.) b. ATP + Glutamate Carbamoyl phosphate + ADP AG The reaction is kJ mol-1 (The hydrolysis reaction for carbamoyl phosphate is Carbamoyl phosphate + H₂0 Glutamate + P, + H+ ; AG¹ = -51.4 kJ mol ¹.) Submit Answer Try Another Version 3 item attempts remaining
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.
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
Calculate the concentration of CuS in a solution in which [H3O+] is held constant at 2.0×10-4 M. (Cite the source of your thermodynamic constants)
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
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?

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