Write balanced biochemical equations for all the reactions in the catabolism of glucose to two molecules of pyruvate (the preparatory & payoff phase of glycolysis), including the standard free-energy change ΔG for each reaction. Then write the overall or net equation of glycolysis, with the net standard free-energy change when one molecule of glucose is converted into 2 molecules of pyruvate

Write balanced biochemical equations for all the reactions in the catabolism of glucose to two molecules of pyruvate (the preparatory & payoff phase of glycolysis), including the standard free-energy change ΔG for each reaction. Then write the overall or net equation of glycolysis, with the net standard free-energy change when one molecule of glucose is converted into 2 molecules of pyruvate

Biochemistry

9th Edition

ISBN:9781305961135

Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Chapter20: Electron Transport And Oxidative Phosphorylation

Section: Chapter Questions

Problem 49RE: MATHEMATICAL What yield of ATP can be expected from complete oxidation of each of the following...

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Write balanced biochemical equations for all the reactions in the catabolism of glucose to two molecules of glyceraldehyde 3-phosphate (the preparatory phase of glycolysis), including the standard free-energy change for each reaction. Then write the overall or net equation for the preparatory phase of glycolysis, with the net standard free-energy change.
In working skeletal muscle under anaerobic conditions, glyceraldehyde 3-phosphate is converted to pyruvate (the payoff phase of glycolysis), and the pyruvate is reduced to lactate. Write balanced biochemical equations for all the reactions in this process, with the standard free-energy change for eachreaction. Then write the overall or net equation for the payoff phase of glycolysis (with lactate as the end product), including the net standard free-energy change.
Arrange the balanced biochemical equations for all the reactions in the payoff phase of glycolysis and the conversion of pyruvate to lactate.
Calculate the standard free-energy change of the reaction catalyzed by theenzyme phosphoglucomutase, given that, starting with 20 mM glucose 1-phosphate and no glucose 6- phosphate, the final equilibrium mixture at 25 °C and pH 7.0 contains 1.0 mM glucose 1-phosphate and 19 mM glucose 6-phosphate. Does the reaction in the direction of glucose 6-phosphate formation proceed with a loss or a gain of free energy?
Saccharides: Using the following substrates, estimate the net ATP yield after glycolytic pathway, Kreb’s cycle and electron transport chain. Assume that the estimate for ATP yield per mole of NADH is 3 moles of ATP, while 1 mole of FADH2 is equivalent to 2 moles of ATP, and one mole of GTP is equivalent to one mole of ATP. Show all pertinent solutions and determine: a) ATP used, b) ATP produced, and c) Net ATP. Based on your solutions, rank the substrates based on increasing yield of ATP 1. Three moles of glucose-6-phosphate
Saccharides: Using the following substrates, estimate the net ATP yield after glycolytic pathway, Kreb’s cycle and electron transport chain. Assume that the estimate for ATP yield per mole of NADH is 3 moles of ATP, while 1 mole of FADH2 is equivalent to 2 moles of ATP, and one mole of GTP is equivalent to one mole of ATP. Show all pertinent solutions and determine: a) ATP used, b) ATP produced, and c) Net ATP. Based on your solutions, rank the substrates based on increasing yield of ATP 1. Three moles of glucose-6-phosphate 2. Four moles of pyruvic acid
Saccharides: Using the following substrates, estimate the net ATP yield after glycolytic pathway, Kreb’s cycle and electron transport chain. Assume that the estimate for ATP yield per mole of NADH is 3 moles of ATP, while 1 mole of FADH2 is equivalent to 2 moles of ATP, and one mole of GTP is equivalent to one mole of ATP. Show all pertinent solutions and determine: a) ATP used, b) ATP produced, and c) Net ATP. Based on your solutions, rank the substrates based on increasing yield of ATP Five moles of Acetyl coenzyme A
Show summary computation in a table Net ATP yield for complete oxidation of 1 mol of galactose to CO2 and H2O (using both Malate-Aspartate and Glycerol-3-Phosphate Shuttles)
In the skeletal muscle, in anaerobic conditions, glyceraldehyde 3-phosphate is converted into pyruvate during the payoff phase of glycolysis; and this pyruvate is reduced into lactate during lactic fermentation. Part 1-Write the 11 balanced biochemical equations corresponding to all the reaction steps leading to the conversion of glyceraldehyde-3-phosphate into lactate through glycolysis followed by lactic fermentation. Part 2-Write the net equation of the whole transformation process (i.e. with glyceraldehyde-3-phosphate as the starting substrate; and lactate as the end product).
The muscle isozyme of lactate dehydrogenase is inhibited by lactate.Steady-state kinetic analysis yielded the following data, with lactate eitherabsent or present at a fixed concentration. (a) Pyruvate is the substrate whose concentration is varied in one plot, NADH in the other. Identify each. Use an arrow and the appropriate letter (b,c,d,ore) to identify each of the following. (b) Reciprocal of Vmax for the uninhibited enzyme. (c) The line representing data obtained in the presence of lactate acting as a competitive inhibitor with respect to the variable substrate. (d) The line representing data obtained in the presence of lactate acting as a noncompetitive inhibitor with respect to the variable substrate. (e) Reciprocal of KM in the presence of lactate acting as a competitive inhibitor. (f) If KM for NADH is 2 x 10-5 M, then which of the following is the most appropriate NADH concentration to use when determining KM for pyruvate: 10-7 M, 10-6 M, 10-5 M, 10-4 M, or 10-3 M?M
The standard state free energy change for Step 4 of glycolysis (where an aldolase enzyme splits fructose 1,6-bisphosphate into GAP and DHAP) is +23.8 kJ/mol. Yet, glycolysis still proceeds spontaneously in the vast majority of cells. Why does this step in particular proceed spontaneously under typical cellular conditions?
If a reaction has a ΔG°′ value of at least −30.5 kJ · mol−1, suffi -cient to drive the synthesis of ATP (ΔG°′ = 30.5 kJ · mol−1), can it still drive the synthesis of ATP in vivo when its ΔG is only −10 kJ · mol−1? Explain.