The degradation of glycogen is catalyzed by the enzyme phosphorylase and has AGO" equal to +3.1 kJ · mol1. The equation for thisreaction is shown below.glycogen (n residues) + P;→ glycogen (n-1 residues) + G1PWhat is the ratio of [P;]/[G1P] under standard conditions? Use 2 significant figures.[P;] : [G1P] = i:1What is the value of AG under cellular conditions when the [P;/[G1P] ratio is 50/1? Use 2 significant figures.AG =ikJ. mol-1

Glucose is stored in liver and muscle cells in form of glycogen. At the time of glucose requirement,…

Answered: he degradation of glycogen is catalyzed…

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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Similar questions

The isomerization of dihydroxyacetone phosphate (DHAP) to glyceraldehyde 3-phosphate (GAP) is catalyzed by triose phosphate isomerase. In the cell, the concentration ratio of DHAP/GAP = 5.5. Calculate [DHAP] (in M) when [GAP] = 0.00002
Glycogen phosphorylase catalyzes the inorganic phosphate-mediated removal of glucose from glycogen (glycogen, to glycogenn-1), allowing the production of glucose 1- phopshate. The DG° for this reaction is +1.6 kJ/mol and R=8.31 J.mol1.K1 (Hint: The removal of glucose units from glycogen does not change the glycogen concentration at equilibrium or physiological conditions). 1- Write down the net equation of the reaction. 2- Calculate the [Pi]/[glucose 1-phosphate] ratio at the equilibrium at 25°C. 3- The ratio [Pi]/[glucose 1-phosphate] of this reaction is equal to 100 in the skeletal muscle under physiological conditions. 3a- Calculate the DG' of the reaction under physiological conditions at 25°C. 3b- What is the direction of this reaction under physiological conditions in the skeletal muscle?.
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
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.
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.
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.
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.
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 final step in the pathway for the synthesis of glucose from lactate (gluconeogenesis) is: Glucose-6-phosphate + H20 5 Glucose + Pi When glucose-6-phosphate is incubated with the proper enzyme and the reaction runs until equilibrium has been reached, the final concentrations are found to be: glucose-6-phosphate (0.035 mM), glucose (100 mM), and Pi (100 mM). Calculate AG" at 25°C and pH 7. 10:21 PM 4/21/2021 F5 F6 F7 F8 F10 F9 7 8. Backspace ーの
A key step in the biosynthesis of triglycerides (fats) is the conversion of glycerol to glycerol-1-phosphate by ATP: At a steady state in the living cell, (ATP) = 10-3M and (ADP) = 10-4 M. The maximum (equilibrium) value of the ratio (glycerol-1-P)/(glycerol) is observed to be 770 at 25 °C and pH=7. Calculate K and DrG° for the reaction. Using the value of DrG° for the reaction ADP + Pi àATP + H2O, together with the answer to part (a), calculate DrG° and K for the reaction: glycerol + phosphateà glycerol-1-phosphate+ H2O .
Given that the AG" values for the hydrolysis of glucose 1-phosphate and glucose 6-phosphate are approximately -21 kJ/mol and –14 kJ/mol, respectively, which statement is true regarding the isomerization shown? glucose 1-phosphate → glucose 6-phosphate O The reaction can likely proceed in either direction and will therefore depend on the concentrations of glucose 1-phosphate and glucose 6-phosphate. O Only the anabolic direction will occur because the free energy change is positive. O The reaction will proceed in both directions simultaneously. This reaction can only proceed in one direction and must be the rate limiting reaction for this point in metabolism.
The phosphorylation and oxidative decarboxylation of oxaloacetate by inorganic phosphate (Pi) to make phosphoenolpyruvate and carbon dioxide is endergonic under intracellular conditions. It is characterized by this equation: Oxaloacetate + Pi ←→ Phosphoenolpyruvate + H2O + CO2 ΔG’ = +24.6 kJ/mol The synthesis of GTP from GDP and inorganic phosphate (Pi) in solution is endergonic under intracellular conditions, and it is characterized by this equation: GDP + Pi ←→ GTP + H2O ΔG’ = +30.5 kJ/mol Write a new net thermodynamically coupled reaction equation that describes the synthesis of phosphoenolpyruvate from oxaloacetate using the hydrolysis of GTP to power the reaction and calculate the new net ΔG’ of this reaction. Show all of your work.

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