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-phosphateglucose 1-phosphateThe standard free-energy change (AGº') for the reaction is +7.5 kJ mol¯¹ (+1.8 kcal mol−¹).PhosphoglucomutaseWhat is the final concentration of glucose 6-phosphate (G6P)?[G6P] =What is the final concentration of glucose 1-phosphate (G1P)?[G1P] =MM Does the reaction proceed as written?Yes, because the standard free-energy change for the reaction is positive.No, because the equilibrium constant is less than 1, which favors the reactant.Yes, because the enzyme will shift the equilibrium point toward the product.Yes, because the reactant concentration is much higher than the product concentration at equilibrium.Under what cellular conditions could you produce G1P at a high rate?Supply G1P and G6P at a high rate.Supply G1P at a high rate and remove G6P at a high rate by other reactions.Supply G6P at a high rate and remove G1P at a high rate by other reactions.Remove G1P and G6P at a high rate by other reactions.

Standards free energy change calculated at biochemical standards is called biochemical standard free…

Answered: Assume that you have a solution of 0.1…

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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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.
The standard Gibbs (free) energy of reaction (A,Gº') of the following reaction is equal to zero (at 25 °C and pH 7) pyruvate + aspartate Pyruvate, aspartate and L-alanine are mixed each at a concentration of 1 mM, without oxaloacetate. Calculate the molar concentrations of each compound when the reaction reaches equilibrium. oxaloacétate + L-alanine
Given the tri-acylglyceride (TAG) below as source of energy when administered from an organism's diet, H,C-O HC-0 H,C-o [A] Show the calculated maximum amount of ATP that could be generated by the full oxidation of the compound. Illustrate where the ATPS are derived from (show the reactions and enzymes involved). You can use general structure of the FFA in the reactions involved in the process. (B) Discuss the fate of the glycerol. (C] One of the FFAS derived from the TAG has the same carbon number as glucose. Compare the maximum yield of ATP derivable from this FFA as compared to the ATP yield from glucose.
A solution containing 0.00001 M ATP has transmission 70.2\% at 260 nm in 1 cm cuvette calculate the transmission of solution in a 3 cm cuvette
This is the kcat question. At maximum saturation, 28.3µg of enzyme in 25mL water catalyzes the oxidation of ethanol at a rate of 2.5mM/min. Calculate kcat in units of seconds if the enzyme has a molar mass of 65kg/mol. The more correct work you show, the more credit you will get.

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