Glucose 1-phosphate is converted into fructose 6-phosphate in two successive reactions.Reaction 1: Glucose 1-phosphate→ glucose 6-phosphateAG'° = -7.3 kJ/molReaction 2: Glucose 6-phosphate→ fructose 6-phosphateAGʻ° = +1.7 kJ/molUsing the values given, calculate the standard free-energy change, AGʻ°,,for the sum of the two reactions:sum >Sum:Glucose 1-phosphate→ fructose 6-phosphateAG'°,kJ/molsumCalculate the equilibrium constant, K',eq >for the sum of the two reactions.K'eeqII

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Answered: Glucose 1-phosphate is converted into…

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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The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics: Vo (micromol/min) Substrate added (mM) 200 1.0 400 2.0 800 4.0 1600 8.0 3200 16.0 The enzyme concentration used in all reactions is 106 M. Which of the following is true: O A) The Km for the reaction must be less than 1 mM ○ B) It is possible to determine Km for the reaction, but not Vmax or kcat OC) It is possible to determine only kcat, not Vmax or Km D) It is not possible to determine Vmax for the reaction OE) The ratio Vmax/Km for the reaction cannot be determined
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
Could you explain step by step how to solve this? I'm not sure how to get all the numbers that are shown in the solved answer.
3. 1,3-bisphosphglycerate has a high energy bond that can be used to phosphorylate ADP to make ATP according to the equation below. The free energy of hydrolysis of 1,3- bisphophoglycerate and ATP under standard conditions are -49.4 kJ/mol and -30.5 kJ/mol, respectively. If the [ATP] to [ADP] is about 4 in the cell, how much 1,3-bisphophoglycerate is needed relative to 3-phosphoglycerate to keep this formation of ATP spontaneous? -203PO. H- -OH -OPO3-² + ADP H- -OH -OPO3-² + ATP
1) Define metabolism and describe the importance of metabolism to life. 2) Calculate the change in free energy (∆G ) for the below reaction and answer the two follow up questions: Gfinal state = 3.4 kcal/ mol and Ginitial state = 10.7 kcal/ mol Recall: ∆G = Gfinal state – Ginitial state a. Is this a spontaneous or non-spontaneous reaction? Explain. b. Is there energy released from this reaction which can be used to do work? Explain. 2) List four conditions which impact an enzymes rate of activity. Explain.
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
You obtain a calculated Vmax of 4.26uM/s and a Km of 122.5uM from a kinetics experiment performed using 0.5uM enzyme. What is the catalytic efficiency of this enzyme?
The enzyme, fumarate, has the following kinetic constants: k 1 k 2 k -1 where k 1 = 10 9 M -1 s -1 k -1 =4.4 x 10 4 s -1 k 2 = 10 3 s -1 a. What is the value of the Michaelis constant for this enzyme? b. At an enzyme concentration of 10 -6 M, what will be the initial rate of product"
Free energy changes under intracellular conditions differ markedly from those determined under standard conditions. ΔG°′ = -32.2 kJ/mol for ATP hydrolysis to ADP and Pi. Calculate ΔG for ATP hydrolysis in a cell at 37 °C that contains [ATP] = 3 mM, [ADP] = 1 mM, and 3Pi4 = 1 mM.

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