Consider the following isomerization reactions of some simple sugars and values for their standard Gibbs free energy AGO: AG = -7.28 kJ/mol reaction A: glucose-1-phosphate →→→glucose-6-phosphate, reaction B: fructose-6-phosphate glucose-6-phosphate, AG° -1.67 kJ/mol Part A Calculate AG for the isomerization of glucose-1-phosphate to fructose-6-phosphate. Express your answer with the appropriate units. ► View Available Hint(s) O Submit ■ μA AG = Value Units ?
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- Calculate the standard-state free energy change for the isomerization of glucose-1-phosphate to glucose-6-phosphateThe equilibrium constant Kc for the reaction fructose-1,6-diphosphate ⇋ glyceraldehyde-3-phosphate + dihydroxyacetone phosphate is 8.9 x 10-5 M at 250C and the behavior is assumed to be ideal. Calculate the delta G for the process Suppose that we have a mixture that is initially 0.010 M in fructose-1,6-diphosphate and 1.0 x 10-5 M in both glyceraldehyde-3-phosphate and dihydroxyacetone phosphate. What is the delta GThe 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?
- The equilibrium constant Kc for the reaction fructose-1,6-diphosphate ⇋ glyceraldehyde-3-phosphate + dihydroxyacetone phosphate is 8.9 x 10-5 M at 250C and the behavior is assumed to be ideal. Calculate .for the process (standard state: 1M) Suppose that we have a mixture that is initially 0.010 M in fructose-1,6-diphosphate and 1.0 x 10-5 M in both glyceraldehyde-3-phosphate and dihydroxyacetone phosphate. What is ?The standard state free energy of hydrolysis of acetyl phosphate isΔG° = -42.3 kJ/mol. Acetyl-P + H2O acetate + Pi Calculate the free energy change for the acetyl phosphate hydrolysis in a solution of 2 mM acetate, 2 mM phosphate and 3 nM acetyl phosphate.Determine the values of KM and Vmax for the decarboxylation of a β-keto acid given the following data.
- One of the examples that we have used to illustrate the concept of equilibrium is the isomerization of glucose-6-phosphate (G6P) to fructose-6-phosphate (F6P), which is the second step in g ycolysis. Draw a graph to show how the reaction Gibbs energy varies with the fraction fof F6P in solution.Label the regions of the graph that correspond to the formation of F6P and G6P being spontaneous, respectively.The turnover number for an enzyme that approximates Michaelis-Menten kinetics is known to be 500 min^-1. From the results shown in the table, enumerate Km and total amount of enzyme present. What is the Km for this enzyme? What is the Vmax for this enzyme? And what is the [E]T for this enzyme?The turnover number of the enzyme fumarase that catalyzes the reaction, Fumarate + H20 ===→ L-malate, is 2.5 x 103 S - l and Km = 4.0 X 10- 6 mol/L. Calculate the rate of conversion of fumarate to L-malate if the fumarase concentration is 1.0 x 1 0 - 6 mol/L and the fumarate concentration is 2.04 x 10- 4 mol/L.
- Give the full biochemical name for a D-aldopentose with the following pattern of chiral centers: carbon #2 = D, carbon #3 = D.The formation of maltose, a disaccharide, from two glucose molecules, is not energetically favorable. However, if this reaction is coupled with the hydrolysis of ATP, the reaction occurs more favorably. Maltose + H2O = 2 Glucose , ΔG'o = -15.5 KJ/mol or -3.7 kcal/mol a. Determine if the coupled reaction will occur spontaneously at standard state through calculating the Gibbs Free Energy of Reaction. b. Calculate the equilibrium constant for each individual reaction, and for the coupled reaction (using free energy of reaction). Show that the equilibrium constant for the coupled reaction equals the equilibrium constants for the individual reactions multiplied together. c. If the reaction medium contains the following chemical species at their given concentrations (298 K and 1.0 atm, pH = 7.0), will the reaction proceed in the forward or the reverse direction? [Maltose] = [Glucose] = 10.0 mM; [ATP] = 5.0 mM; [ADP] = [Pi] = 20 mMConsider 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