Calculate the physiological free energy for the substrate level generation of ATP from PEPcatalyzed by the enzyme Pyruvate Kinase:Phosphoenolpyruvate + ADP --> Pyruvate + ATPat 37C in a red blood cell where {PEP]=4.7mM. [pyruvate]=1.0mM. [ADP] = 0.73mM and[ATP] = 2.6 mMThe standard free energies of hydrolysis are:PEP--> pyruvate +Pi: -61.9 kJ/molATP --> ADP+ Pi: -30.5 kJ/moleReport to 1 decimal as kJ/mol

Step 1: Calculate the standard free energy change (ΔG′∘) ΔG′∘ = ΔGPEP→Pyruvate - ΔGATP→ADPΔG′∘ =…

Answered: Calculate the physiological 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 17P

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The following two reactions are coupled in the last step of glycolysis (catalyzed by the enzyme pyruvate kinase). РЕР + Н.О € Руr + Pi ADP + Pi → ATP + H2O AG° = -14.8 kcal/mol AG° = +7.3 kcal/mol D) The steady-state concentrations of ATP, ADP, and pyruvate in human erythrocytes are 2.24 mM, 0.25 mM, and 0.051 mM, respectively. What would be the concentration of PEP in these cells if the coupled reaction was at equilibrium?
The phosphorylation and oxidative decarboxylation of oxaloacetate by inorganic phosphate (Pi) to make phosphoenolpyruvate and carbon dioxide is endergonic under intracellular conditions. It is characterized by this equation: Oxaloacetate + Pi ←→ Phosphoenolpyruvate + H2O + CO2 ΔG’ = +24.6 kJ/mol The synthesis of GTP from GDP and inorganic phosphate (Pi) in solution is endergonic under intracellular conditions, and it is characterized by this equation: GDP + Pi ←→ GTP + H2O ΔG’ = +30.5 kJ/mol Write a new net thermodynamically coupled reaction equation that describes the synthesis of phosphoenolpyruvate from oxaloacetate using the hydrolysis of GTP to power the reaction and calculate the new net ΔG’ of this reaction. Show all of your work.
Imagine a triglyceride comprised of (3) saturated C12 fatty acids. Calculate the number of ATP generated from the complete oxidation of one of these 12-carbon fatty acids to CO2 and water in the liver. Assume that each NADH = 2.5 ATP and each FADH2 = ETC generates 1.5 ATP. Any step that yields pyrophosphate as a product should be treated as an input (i.e. net loss) of (2) ATP.
Intracellular concentrations in resting muscle are as follows: fructose- 6-phosphate, 1.0 mM; fructose-1,6-bisphosphate, 10 mM; AMP, 0.1 mM; ADP, 0.5 mM; ATP, 5 mM; and P, 10 mM. Is the phosphofructokinase reac- tion in muscle more or less exergonic than under standard conditions? By how much?
Aconitase catalyzes the reaction: citrate ↔ HisocitrateThe standard free energy change, ΔG°′, for this reaction is +6.3 kJ/mol.However, the observed free energy change (ΔG) for this reaction in mammalian mitochondria at 25°C is ∼0 kJ>mol (Table 13.2).(a) Calculate the ratio of [isocitrate]>[citrate] in mitochondria.(b) Is this reaction likely to be a control point for the citric acid cycle? Whyor why not?
Given the following information, calculate the physiological ΔG of the isocitrate dehydrogenase reaction at 25°C and pH 7.0: [NAD+]/[NADH] = 8, [α-ketoglutarate] = 0.1 mM, and [isocitrate] = 0.02 mM. Assume standard conditions for CO2 (ΔG°′ is given in Table). Is this reaction a likely site for metabolic control?
Consider the typical beta oxidation of linoleic acid (C18:2 ^Δ9, 12): How many ATP are generated in complete oxidation of linoleic acid? How many NADH are generated in complete oxidation of linoleic acid? How many FADH2 are generated in complete oxidation of linoleic acid?
Write a balanced chemical equation for the pentose phosphate pathway in the first two modes depicted as shown, where (a) ribose-5-phosphate synthesis is maximized and (b) NADPH production is maximized, by conversion of the sugar phosphate products to glucose-6-phosphate for repeated operations of the pathway.
Phosphofructokinase-1 is the main flux controlling enzyme for glycolysis. It is inhibited by high [ATP]. There exist metabolic circumstances in which the inhibition by ATP is overridden. Draw velocity vs. [S] graphs showing the inhibition of PFK-1 activity by ATP and the circumstance in which the inhibition by ATP is overridden.
Decylic acid is a saturated fatty acid that occurs naturally in coconut oil and palm kernel oil. Calculate the net ATP yield when decylic acid undergoes complete B oxidation. The formula of decylic acid is shown below: (Given: The oxidation of one NADH yields 2.5 ATP; the oxidation of one FADH2 yields 1.5 ATP; and the oxidation of one acetyl CoA yields 10 ATP.) O 50 ATP O 52 ATP 66 ATP OH O 64 ATP
.Intramitochondrial ATP concentrations are about 5 mM, and phosphate con- centration is about 10 mM. If ADP is five times more abundant than AMP, calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate AG for ATP hydrolysis at 37 °C under these conditions. The energy charge is the concentration of ATP plus half the concentration of ADP divided by the total adenine nucleotide concentration: [ATP] + 1/2[ADP] [ATP] + [ADP] + [AMP]
The standard reduction potential for ubiquione (A or coenzyme Q) is .045 V, and the standard reduciton potential (E) for FAD is -0.219 V. Using these values, show that the oxidation for FADH2 by ubiquinone theoretically liberates enough energy to drive the synthesis of ATP. Faraday constant =96.48KJ/Vol delta G' standard for ATP Synthesis is +30.5 KJ/mol R=8.314 J/mol K=1.987 cal/mol K

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