12. Calculate the standard free energy change for each of the following metabolically importantenzyme-catalyzed reactions, using the equilibrium constants given for the reactions at 25°Cand pH 7.0a. Glutamate + oxaloacetateaspartate + aketoglutarateenz. Apartate aminotransferase; K'eg = 6.8b. Fructose 6-phopshate + ATP- fructose 1,6-bisphosphate + ADPenz. Triose phosphate isomerase; K'eg =254

All living organisms are made up of cells, which are the most basic unit of life. They are…

Answered: Calculate the standard free energy…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter18: Glycolysis

Section: Chapter Questions

Problem 13P

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1. The enzyme glutamate dehydrogenase is important in the breakdown of amino acids to produce NH4+. High levels of NH4+ in the body are toxic, and for this reason it is used to form urea to be excreted in the urine. a) Using the information provided, calculate the delta G knot prime and the Keq value at 298K for the oxidation of glutamate catalyzed by glutamate dehydrogenase. (Constants: R=8.3J/degree.mol, F=96.1kJ/V.mol) b) Given the reaction above, why would high levels of NH4+ be toxic? c) Given the reaction above, explain how a high concentration of gutamate inside the cell would affect energy production. Be sure to be specific.
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The Keq (25C) of the reaction below is 635.67. Fructose 1,6-biphosphate <-->fructose -6-phosphate + Pi. a) What is the standard Gibbs free energy change for this reaction? b) if the concentrationof fructose 1,6 biphosphate is adjusted to 0.85 M and that of fructose 6 phosphate and phosphate adjusted to 0.055 M, what is the actual free energy change
#1 Specify the role each of the following amino acids play within the crystal structure and/or active site for Be as specific as possible, with pictures (and mechanistic arrows) as necessary. His11 Arg140 Glu89 Trp68 #2 Provide a step-wise mechanism for the reaction Bisphosphoglycerate mutase catalyzes, using the amino acids responsible for aiding in catalysis. You do not need to add surrounding amino acids that aid in substrate specificity. (drawn out)
4.Pepsin is the proteolytic enzyme of gastric juice. The active form of this enzyme is formed from pepsinogen under HCL action.Optimum of enzyme action: pH = 1.5, t = 37°. Describe the properties of this enzyme. For this:1)Name and explain the mechanism of this enzyme activation.2)Draw the plot and explain the effects of pH and t on the reaction velocity.3) Explain how changes the velocity of this reaction in patients suffering from hypoacidie gastritis.
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?
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1. Consider the oxidation of the fatty acid with the common name arachidic acid. a. Draw the structure of arachidic acid. b. How many turns of the fatty acid oxidation cycle is required for the complete oxidation of arachidic acid? c. How many moles of ATP are formed from one mole of arachidic acid if the acetyl CoA produced go to the citric acid cycle and oxidative phosphorylation? Assume 1 mole of NADH is equivalent to 3 moles ATP and 1 mole FADH2 is equivalent to 2 moles of ATP. Show how you arrived at your answer

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