..a) Draw all of the reactions that occur in the aerobic metabolism of glucose that hydrolyze athiolester bond. In your answer, include complete structural formulae as well as the names ofany cofactors, enzymes, reactants and products.b) Explain why the free energy changes that characterize these reactions are so exergonic.Include a figure in your answer. (c) If you were to completely catabolize 3 molecules of glucose under aerobic conditions, whatwould the ATP yield be as a result of the reactions that you've drawn above?

Complete catabolism of Glucose includes Glycolysis, TCA cycle and ETC. Glycolysis of single molecule…

Answered: c) If you were to completely catabolize…

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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In the degradation of glycogen, the purpose of the debranching enzyme is to remove the last four glucose molecules from branches structure of glycogen. It does this by catalyzing three different reactions. Use the equations below to answer parts a-c. Synthesis of α(1,6) link ΔG = +7.1 kJ Hydrolysis of α(1,4) link ΔG = ─15.5 kJ a)What are the three chemical reactions performed during the removal of the last four glucose molecules of the branching structure of glycogen? b) Calculate ΔG for each of the three reactions described in part a. c) Now calculate the overall energy change for the net reaction carried out by this enzyme. d) Why is this reaction favorable?
The oxidation of 1 mol of glucose supplies enough metabolic energy to form 36 mol of ATP. Oxidation of 1 mol of a typical dietary fat like tristearin (C57H116O6) yields enough energy toform 458 mol of ATP. How many molecules of ATP can form per gram of (a) glucose; (b) tristearin?
Describe how a) Mean Arterial Pressure, b) Maximal Oxygen Consumption, and c) Blood Flow are determined using its formula. In addition, you should explain what those factors are including cardiac output, stroke volume, heart rate, resistance, a-vO2 difference, etc. Describe how many ATPs can be generated by complete cycles of beta oxidation of free fatty acid with 20 carbons. You should indicate how many cycles of beta oxidation and Krebs cycle, and total number of products as well
Arrange the following molecules in order of their biological energy content per mole: glucose, caproic acid (C10), sucrose (C12), myristic acid (C14) Write the structural equation for the transamination reaction that involves threonine and pyruvate as pair of reactants [provide the structure of the AA and pyruvate)
(i) During the Pyruvate Decarboxylase (PDC) catalysed reaction, a covalent coenzyme intermediate is formed. On the skeleton of the covalent coenzyme intermediate below draw the appropriate double bonds, charges, and electron pairs to illustrate the two resonance forms of this intermediate. Name each form in the boxes provided. HO S R' N -R HO S R' N -R
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.
10) The phosphorylation of glucose is an unfavorable reaction, with ΔG°’ = 13.8 kJ/mol. We can couple this to the favorable reaction of ATP hydrolysis to make the overall process favorable. a) Describe how this works. b) If ΔG°’ for ATP hydrolysis = -32.2 kJ/mol, what is the overall ΔG°’ of the reaction?
Consider the following list of phosphorylated compounds with their free energy changes of phosphate hydrolysis: Glucose-1-phosphate (-5.0 kcal/mol), PEP (-14.8 kcal/mole), 1,3-bisphosphoglycerate (-11.8 kcal/mole) and Glucose-6-Phosphate (-3.3 kcal/mol). Given that the free energy change of ATP hydrolysis is -7.3 kcal/mole, which of these molecules be directly synthesized by the transfer of a phospho- group from ATP? 1,3-bisphosphoglycerate Glucose-6-phosphate All of those phosphorylated compounds. PEP Glucose-1-phosphate
Write balanced chemical equations for each of the following: (a) anaerobic glycolysis of 1 mole of sucrose, cleaved initially by sucrose phosphorylase; (b) aerobic glycolysis of 1 mole of maltose; (c) fermentation of one glucose residue in starch to ethanol, with the initial cleavage involving a-amylase.
5) A certain aerobic organism is able to metabolize the following glycolipid: "CH,OH OH HO OH A. Draw the 2 resulting structures that would occur upon initial hydrolysis of the O-glycosidic bond. B. Calculate how much ATP is formed upon complete aerobic oxidation of one mole of the compound. Assume that no ATP is produced when one mole of the glycosidic bond in the above compound is hydrolyzed. Show calculation below.
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.
Consider the following mechanism: What kind of reaction is occurring during this step of glycolysis? What metabolite is in Box 1? What metabolite is in Box 2? What metabolite is in Box 3? What enzyme catalyzes this reaction? Circle and label one place on the mechanism where covalent catalysis is occurring. Suggest an amino acid that could fill the role of residue “A” in the mechanism above and draw its structure at pH 7.4. Suggest an amino acid that could fill the role of residue “B” in the mechanism above and draw its structure at pH 7.4. Under standard conditions, this reaction is unfavorable (DG¢° = 23.8 kJ/mol). What conditions in the cell allow for the actual free energy change to be lower (DG » 0), making the reaction readily reversible? Explain your answer. *please help and explain as well as you can*

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c) If you were to completely catabolize 3 molecules of glucose under aerobic conditions, what would the ATP yield be as a result of the reactions that you've drawn above?