1.The reaction catalyzed by aldolase splits fructose-1,6-bisphosphate (F16BP) intoglyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP). The AG°" for thereaction is 23.8 kJ/mole. If the concentrations of G3P and DHAP are 2.5 mM and 1 mM,respectively, what concentration of F16BP is needed for the reaction to be at equilibrium in ahuman cell?

Given: Concentration of Glyceraldehyde-3-phosphate (G3P) = 2.5 mM Concentration of dihydroxyacetone…

The reaction catalyzed by aldolase splits fructose-1,6-bisphosphate (F16BP) into glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP). The AGº' for the 1. reaction is 23.8 kJ/mole. If the concentrations of G3P and DHAP are 2.5 mM and 1 mM, respectively, what concentration of F16BP is needed for the reaction to be at equilibrium in a human cell?

The reaction catalyzed by aldolase splits fructose-1,6-bisphosphate (F16BP) into glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP). The AGº' for the 1. reaction is 23.8 kJ/mole. If the concentrations of G3P and DHAP are 2.5 mM and 1 mM, respectively, what concentration of F16BP is needed for the reaction to be at equilibrium in a human cell?

Chemistry & Chemical Reactivity

10th Edition

ISBN:9781337399074

Author:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel

Publisher:John C. Kotz, Paul M. Treichel, John Townsend, David Treichel

Chapter24: Biochemistry

Section: Chapter Questions

Problem 34GQ: The first step of the metabolic process known as glycolysis is the conversion of glucose to glucose-...

See similar textbooks

Similar questions

One step in glycolysis is the conversion of fructose-6-phosphate to fructose-1,6-bisphosphate. The direct reaction of fructose-6-phosphate with inorganic phosphate fructose-6-phosphate + Pi ⇌ fructose-1,6-bisphosphate + H₂O is very unfavorable, with ∆G'°= 16.3 kJ/mol and K'eq = 1.39×10⁻³. However, in glycolysis the reaction is coupled to ATP hydrolysis: fructose-6-phosphate + ATP ⇌ fructose-1,6-phosphate + ADP and the reaction if favorable. What is the equilibrium [fructose-1,6-bisphosphate]/[fructose-6-phosphate] ratio in the coupled reaction when [ATP] = [ADP]? For ATP hydrolysis ∆G'°= -30.5 kJ/mol at 25°C.
3) The enzyme aldolase catalyzes the conversion of fructose-1,6-diphosphate (FDP)to dihydroxyacetone phosphate (DHAP) and glyceraldehide-3-phosphate (G3P). Thereaction isFDP ⇄ DHAP + G3P , ∆rG0(298.15 K) = 23.8 kJ mol−1In red blood cells the concentration of these species are [FDP] = 35 µM, [DHAP] =130 µM, and [G3P] = 15 µM. (Remember that 1.0 µM = 1.0 × 10−6 mol L−1. Thestandard state for reactions in solution can be taken as c0 = 1.0 mol L−1).Calculate ∆rG in a red blood cell at 25 0C. Will the reaction occur spontaneouslyin the cell at this temperature?
TPP is a coenzyme for transketolase, the enzyme that catalyzes the conversion of a ketopentose (xylulose5-phosphate) and an aldopentose (ribose-5-phosphate) to an aldotriose (glyceraldehyde-3-phosphate) and a ketoheptose (sedoheptulose-7-phosphate). Notice that the total number of carbons in the reactants and products is the same (5 + 5 = 3 + 7). Propose a mechanism for this reaction.
The standard free energy change (ΔG°') for hydrolysis of fructose-l,6-bisphosphate (FBP) to fructose-6-phosphate (F-6-P) and Pi is -16.7 kJ/mol: FBP + H2O → Fructose-6-P + Pi The standard free energy change (ΔG°') for ATP hydrolysis is -30.5 kJ/mol: ATP + H2O → ADP + Pi a What is the standard free energy change for the phosphofructokinase reaction: ATP + Fructose-6-phosphate → ADP + FBP ΔG°' = -13.8 kJ/mol b What is the equilibrium constant for this reaction at 25.0 °C? K'eq =
In one of the steps in this pathway fructose 1,6-biphosphate (F1,6BP) is converted to gylceraldehyde-3-phosphate (G-3-p) and dihydroxyacetone phosphate (DHAP). This reaction is catalyzed by the enzyme aldolase. For this reaction at 25 celcuius and Ph7 we have: Keq= 10-4M and Delta G = +5456 cal/mol Calculate the following: The concentration of F1, 6BP, DHAP and G-3-P at equilibrium when the initial F1,6BP is (A) 1M, (b) 10-2 M, (c) 2 X 10*4 M and (d) 10-5 M. I been trying to solve this problem but I dont even know where to begin with. Atleast help me with problem A, I would be able to guide myself through.
The first step of the metabolic process known as glycolysis is the conversion of glucose to glucose- 6-phosphate. This process has a positive value for rG' Glucose + Pi Glucose-6-phosphate + H2O rG' = +13.8 kJ/mol-rxn This reaction is coupled to the hydrolysis of ATP ATP + H2O ADP + Pi rG' = -30.5 kJ/mol-rxn What is the sum of these two equations and the value of rG' for the coupled reaction? Is the coupled reaction product-favored at equilibrium?
TPP is a coenzyme for transketolase, the enzyme that catalyzes the conversion of a ketopentose (xylulose- 5-phosphate) and an aldopentose (ribose-5-phosphate) to an aldotriose (glyceraldehyde-3-phosphate) anda ketoheptose (sedoheptulose-7-phosphate). Notice that the total number of carbons in the reactants and products is the same (5 + 5 = 3 + 7). Propose a mechanism for this reaction.
a tetrose if it has 4 C's; What are these ?
1. Why is the development of catalysis important to the development of life? 2. Why was the development of coding system important to the development of life? 3. Did symbiosis play a role in the development of eukaryotes?
1.) Did the lactase enzyme show specificity? Support your answer by comparing yor data for lactose and sucrose. 2.) How is the rate of enzyme-catalyzed conversion affected by temperature? Explain? 3.) How is the rate of enzyme-catalyzes conversion affected by acidity (ph) of the solution. Explain?
Chorismate mutase is an enzyme that promotes a pericyclic reaction by forcing the substrate to assume the conformation needed for the reaction. The product of the pericyclic reaction is prephenate that is subsequently converted into the amino acids phenylalanine and tyrosine. What kind of a pericyclic reaction does chorismate mutase catalyze?
Wheeler and Mathews (J. Biol. Chem. 287:31218–31222 (2012)) reportedthe NAD+ and NADH concentrations in yeast mitochondria as 20 mM and0.3 mM, respectively. Consider the malate dehydrogenase reaction, which is part of the citric acid cycle:malate + NAD+ → oxaloacetate + NADH + H+ ΔG∘' = +29.7 kJ/molIf malate concentration in yeast mitochondria is 0.4 mM, what is the maximum concentration of oxaloacetate needed to make the reaction exergonic at pH 7.0 and 37°C?