9 Synthesis of the activated form of acetate (acetyl-CoA) is carried out in an ATP-dependent process.Acetyl-CoA + AMP + PP₁The AG' for the hydrolysis of acetyl-CoA to acetate and CoA is -32.2 kJ/mol, and that for hydrolysis of ATP to AMP and PP;is -30.5 kJ/mol. Calculate AG" for the ATP-dependent synthesis of acetyl-CoA shown in the equation.Acetate + CoA + ATPAG' =Almost all cells contain the enzyme inorganic pyrophosphatase, which catalyzes the hydrolysis of PP; to P₁.What effect does the presence of this enzyme have on the synthesis of acetyl-CoA?Hydrolysis of pyrophosphate decreases the rate of the reaction.Hydrolysis of pyrophosphate has no effect on the reaction.Hydrolysis of pyrophosphate increases the rate of the reaction.Hydrolysis of pyrophosphate shifts the equilibrium of the reaction to the right, making the formation of acetyl-CoAenergetically more favorable.Hydrolysis of pyrophosphate shifts the equilibrium of the reaction to the left, making the formation of acetyl-CoAenergetically less favorable.kJmol

The nucleotide coenzyme adenosine triphosphate (ATP) is the most important form of chemical energy…

Answered: Synthesis of the activated form of…

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 18P: Distinguishing the Mechanisms of Class I and Class I Aldolases Fructose bisphosphate aldolase in...

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Extending the Mechanism of Methylmalonyl-CoA Mutase to Similar Reactions Based on the mechanism for the methylmalonyl-CoA mutase (see problem 14), write reasonable mechanisms for the following reactions shown.
Distinguishing the Mechanisms of Class I and Class I Aldolases Fructose bisphosphate aldolase in animal muscle is a class 1 aldolase, which forms a Schiff base intermediate between substrate (for example. fructose-1, 6-bisphosphate or dihydroxyacetone phosphate) and a lysine at the active site (see Figure I8.12). The chemical evidence for this intermediate conies from studies with aldolase and the reducing agent sodium borohydride, NaBH4. Incubation of the enzyme with dihydroxyacetone phosphate and NaBH4 inactivates the enzyme. Interestingly, no inactivation is observed if NabH4 is added to the enzyme in the absence of substrate. Write a mechanism that explains these observations and provides evidence for the formation of a Schiff base intermediate in the aldolase reaction.
The formation of acetyl-CoA from acetate is an ATP-driven reaction: Acetate + ATP + CoA Acetyl CoA + AMP + PP₁ Calculate AG" for this reaction given that the AG' for the hydrolysis of acetyl CoA to acetate and CoA is −31.4 kJ mol-¹ (−7.5 kcal mol¯¹) and that the AG°' for hydrolysis of ATP to AMP and PP; is -45.6 kJ mol-¹ (−10.9 kcal mol−¹ ). AG° reaction = AGO! i The PP, formed in the preceding reaction is rapidly hydrolyzed in vivo because of the ubiquity of inorganic pyrophosphatase. The AG" for the hydrolysis of pyrophosphate (PP;) is −19.2 KJ mol-¹ (-4.665 kcal mol-¹). Calculate the AGº' for the overall reaction, including pyrophosphate hydrolysis. reaction with PP, hydrolysis = What effect does the presence of pyrophosphatase have on the formation of acetyl CoA? kJ mol-¹ It does not affect the overall reaction. It brings the overall reaction closer to equilibrium. It makes the overall reaction even more exergonic. It makes the overall reaction even more endergonic. kJ mol-¹ -1
Synthesis of the activated form of acetate (acetyl-CoA) is carried out in an ATP-dependent process:(a) The ΔG′° for hydrolysis of acetyl-CoA to acetate and CoA is −32.2 kJ/mol and that for hydrolysis of ATP to AMP and PPi is −30.5 kJ/mol. Calculate ΔG′° for the ATPdependent synthesis of acetyl-CoA.(b) Almost all cells contain the enzyme inorganic pyrophosphatase, which catalyzes the hydrolysis of PPi to Pi. What effect does the presence of this enzyme have on the synthesis of acetyl-CoA? Explain.
The synthesis of the activated form of acetate (acetyl-CoA) is carried out in an ATP-dependent process: Acetate + CoA + ATP → acetyl-CoA + AMP + PPi (a) The ∆G’o for the hydrolysis of acetyl-CoA to acetate and CoA is - 32.2 kJ/mol and that for hydrolysis of ATP to AMP and PPi is - 30.5 kJ/mol. Calculate ∆G’o for the ATP-dependent synthesis of acetyl-CoA. (b) Almost all cells contain the enzyme inorganic pyrophosphatase, which catalyzes the hydrolysis of PPi to Pi. What effect does the presence of this enzyme have on the synthesis of acetyl-CoA? Explain.
The reaction catalyzed by malate dehydrogenase has a ΔG°′ value of +29.7 kJ⋅mol−1. Given what this says about the occurrence of the reaction catalyzed by malate dehydrogenase in cells explain how the reaction catalyzed by citrate synthase (−31.5 kJ⋅mol−1) influences that activity of malate dehydrogenase. In addition, explain how the activity of citrate synthase functions as a regulatory point for the citric acid cycle
Consider the complete oxidation of one mole of simple TAG containing behenic acid residues (22:0). I. For one mole of the fatty acid residue, determine the following: a. What is the number of ATP yield obtained from the oxidation of acetyl CoA entering the TCA cycle and ETC b. What is the number of ATP yield obtained from NADH coming from the complete β-oxidation of the fatty acid residue c. What is the number of ATP yield obtained from FADH2 coming from the complete β-oxidation of the fatty acid residue d. What is the number of net ATP yield of ATP in the complete oxidation of the fatty acid residue II. What is the net ATP yield for the complete oxidation of all the fatty acid residues of the simple TAG? (Note: glycerol backbone is not included)
Incubation of the norsolinic acid synthase holo-ACP with malonyl CoA gave malonyl-S-ACP (molecular weight 10112 Da). (ACP SH holo-ACP Malonyl-SNAC Calculate the molecular weight of holo-ACP. (ACP OH malonyl-S-ACP MW = 10112
Acetyl CoA + 2H* + 2e = pyruvate + COASH E = -0.48 V Ubiquinone + 2H* + 2e = Ubiquinol E" = +0.04 V Consider the redox rxn wherein a pair of e passes from pyruvate to ubiquinone. Calculate the change in standard Gibbs free energy (kJ/mol). Report answer to two decimal places.
Acetyl-CoA is formed from acetate by coupling two reactions: ATP + H20 = ADP + P; AG" = -36.03 kJ/mol %3D acetate + CoA acetyl CoA + H20 AG" = +33.21 kJ/mol %3D 1. Calculate the overall AG' (reported up to two decimal places) for the net reaction. kJ/mol 2. Calculate the Keg (reported up to two decimal places and do not use scientific notation) for the net reaction at 298.15K. NOTE: R= 8.314 x 103 kJ/mol-K
A number of genetic deficiencies in acyl CoA dehydrogenases have been described. This deficiency presents early in life after a period of fasting. Symptoms include vomiting, lethargy, and sometimes coma. Not only are blood levels of glucose low ( hypoglycemia), but starvation-induced ketosis is absent. Provide a biochemical explanation for these last two observations.
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.

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