The enzyme aldolase catalyzes the reaction shown in the glycolytic pathway:Fructose 1,6-bisphosphatedihydroxyacetone phosphate + glyceraldehyde 3-phosphateThe AG" for the reaction is +23.8 kJ mol¯¹ (+5.7 kcal mol−¹), whereas the AG in the cell is −1.3 kJ mol¯¹ (−0.3 kcal mol¯¹).Calculate the ratio of products to reactants under standard (equilibrium) conditions at 37°C.[products][reactants]7 x10-5[products][reactants]IncorrectAldolase=====Calculate the ratio of products to reactants under intracellular conditions at 37°C.4 ×10-5IncorrectComplete the statement using your results.under standard conditionsunder intracellular conditionsA reaction that is endergonic under standard conditions can be converted into an exergonic reaction by maintaining the ratioof products to reactants below the equilibrium value.

The ratio of concentration of products to reactants for any reaction in a given condition at…

Answered: The enzyme aldolase catalyzes the…

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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Write a balanced equation for each of the following reactions or reactionsequences.(a) The reaction catalyzed by PFK-2(b) The conversion of 2 moles of oxaloacetate to glucose(c) The conversion of glucose to UDP-Glc(d) The conversion of 2 moles of glycerol to glucose(e) The conversion of 2 moles of malate to glucose-6-phosphate
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
Consider the following chemical equation whose delta(G) = 9kcal/mol: AC + BD ---> AB + CD what are the reactants and what are the products is this reaction spontaneous? How do you know? Is energy released or consumed by this reaction? If an enzyme, which catalyzes this reaction is added, what will happen to delta (G) If this reaction is coupled to another reaction, whose delta(G) is -12 kcal/mol, what will be the net delta(G) value? will the overall reaction be spontaneous
The phosphoryl group transfer potentials for glucose-1-phosphate and glucose-6-phosphate are 20.9 kJ/mol and 13.8 kJ/mol, respectively. (a) What is the equilibrium constant for the reaction shown below at 25 °C? (b) If a mixture was prepared containing 1 m glucose-6-phosphate and 1 x 10-3 M glucose-1-phosphate, what would be the thermodynamically favored direction for the reaction?
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-P ⇔ glucose-1-P ∆G°′ = +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?
The conversion of glucose-1-phosphate to glucose-6-phosphate by the enzyme phosphoglucomutase has a △G°' of -7.6 kJ/mol. Calculate the equilibrium constant for this reaction at 298 K and a pH of 7. (R = 8.315 J/K-mol) A. 0.003 B. 0.047 C. 1.00 D. 21
The standard free energy change for the reaction catalyzed by phosphoglucomutase is -7.1kJ/mol, (a) calculate ΔG at 37°C when the concentration of glucose-1-phosphate is 1-mM and the concentration of glucose-6-phosphate is 25-mM, (b) Is the reaction spontaneous under these conditions?
The complete combustion of palmitate and glucose yields 9781 kJ ∙ mol−1 and 2850 kJ ∙ mol−1 of free energy, respectively. Compare these values to the free energy (as ATP) obtained though catabolism of palmitate and glucose under standard conditions. Which process is more efficient?
Consider the coupled reactions: 1,3-BPG → 3-PG + Pi ΔG°'= -16.3 kcalmolkcalmol ATP → ADP + Pi ΔG°'= -7.3 kcalmolkcalmol Which of the following is TRUE about the total ΔG°’ for the coupled reactions? -9.0 kcal/mol; spontaneous +9.0 kcal/mol; nonspontaneous -23.6 kcal/mol; spontaneous +23.6 kcal/mol; nonspontaneous
Acetocholinesterase is an enzyme possessing a single active site that metabolizesacetylcholine with a turn over number of 1.4 x 10^4s-1. How many grams of acetylcholine(molecular formula C7NO2H16+) will 2.16 x 10^-6 g acetocholinesterase metabolize in 60minutes? (The enzyme’s molecular mass is 4.2 x 10^4 g/mol).
The breakdown of a complex carbohydrate into its monomeric unit can be described as an enzyme-catalyzed reaction that has a deltaG(∆G) of -90kcal/mol. Suppose you were to add triple the amount of enzyme into this reaction - what would be the ∆G of this reaction?
Consider the coupled reactions: 1,3-BPG → 3-PG + Pi ΔG°'= -16.3 kcalmolkcalmol ATP → ADP + Pi ΔG°'= -7.3 kcalmolkcalmol Which of the following is TRUE about the total ΔG°’ for the coupled reactions? A. +23.6 kcal/mol; nonspontaneous B. -23.6 kcal/mol; spontaneous C. +9.0 kcal/mol; nonspontaneous D. -9.0 kcal/mol; spontaneous

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