The free energy of hydrolysis for acetic anhydride is221.8 kJ/ mol. The conversion of ATP to ADP also involvesthe cleavage of an anhydride bond. Its free energy of hydrolysis is 230 kJ/ mol. Explain the difference in these values.
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The free energy of hydrolysis for acetic anhydride is
221.8 kJ/ mol. The conversion of ATP to ADP also involves
the cleavage of an anhydride bond. Its free energy of hydrolysis is 230 kJ/ mol. Explain the difference in these values.
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- The standard state free energy of hydrolysis of acetyl phosphate isΔG° = -42.3 kJ/mol. Acetyl-P + H2O acetate + Pi Calculate the free energy change for the acetyl phosphate hydrolysis in a solution of 2 mM acetate, 2 mM phosphate and 3 nM acetyl phosphate.Under typical circumstances, the free energy released by ATP hydrolysis is 30.5 kJ/mol. Is more or less free energy released when ATP is hydrolyzed under ordinary circumstances except at pH 5.0? Explain.The ΔG°′ for hydrolytically removing a phosphoryl group from ATP is about twice as large as the ΔG°′ for hydrolytically removing a phosphoryl group from AMP (−14 kJ · mol−1). Explain the discrepancy.
- Phosphocreatine (G0ʹ = -43.1 kJ/mol) has a higher phosphoryl group transfer potential than ATP (G0ʹ = -30.5 kJ/mol). However, under certain physiological conditions, phosphoryl group is transferred from ATP to creatine. Explain this discrepancy. Many biochemical conversions are carried out via multi-step pathways although similar conversions can be done in an organic chemistry lab in fewer steps. Explain why energetically it is reasonable to use multiple steps in biochemical conversions. What are isozymes? Humans contain several isozymes of hexokinase. Why does the body need several isozymes of hexokinase? 1,3-bisphosphoglycerate is used to produce ATP. Which of the two phosphates of 1,3- bisphosphoglycerate is transferred to ADP to make ATP. Explain why it is this specific phosphate and not the other one. Triose phosphate isomerase is a diffusion-controlled enzyme. What reaction is catalyzed by this enzyme (structures of molecules not needed)? Explain why…3. 1,3-bisphosphglycerate has a high energy bond that can be used to phosphorylate ADP to make ATP according to the equation below. The free energy of hydrolysis of 1,3- bisphophoglycerate and ATP under standard conditions are -49.4 kJ/mol and -30.5 kJ/mol, respectively. If the [ATP] to [ADP] is about 4 in the cell, how much 1,3-bisphophoglycerate is needed relative to 3-phosphoglycerate to keep this formation of ATP spontaneous? -203PO. H- -OH -OPO3-² + ADP H- -OH -OPO3-² + ATPA table of standard state free energies is shown below. For the reaction: Creatine phosphate + ADP----> Creatine + ATP the free energy under standard state conditions is kJ/mole. TABLE 14.1 Standard free energies of hydrolysis of some phosphorylated compounds Compound kcal mol kJ mol - 14.8 Phosphoenolpyruvate 1,3-Bisphosphoglycerate Creatine phosphate ATP (to ADP) Glucose 1-phosphate Pyrophosphate Glucose 6-phosphate -61.9 -11.8 - 49.4 - 10.3 -43.1 - 7.3 - 30.5 - 20.9 - 19.3 - 5.0 - 4.6 – 3.3 -13.8 Glycerol 3-phosphate – 2.2 - 9.2 A. +12.6 В. +73.6 С.-3.0 D. -12.6 ОЕ.-73.6
- Inside cells, the AG value for the hydrolysis of ATP to ADP + Pi is approximately -50 kJ/mol (-12 kcal/mol). Calculate the approximate ratio of [ATP] to [ADP][Pi ] in cells at 37°C. AG = AG + RT InKe R= 8.315 x 10³ kJ mol deg T= 298 K Table 15.1 Standard free energies of hydrolysis of some phosphorylated compounds Compound kJ mol- kcal mol- Phosphoenolpyruvate 1,3-Bisphosphoglycerate Creatine phosphate ATP (to ADP) -61.9 -14.8 -49.4 -11.8 -43.1 -10.3 -30.5 - 7.3 - 5.0 Glucose 1-phosphate Pyrophosphate Glucose 6-phosphate -20.9 -19.3 -4.6 -13.8 3.3 Glycerol 3-phosphate - 9.2 2.2 biochemistryA total of 30.5 kJ mol-1 of free energy is needed to synthesise ATP from ADP and Pi when the reactants and products are at 1.0 M concentrations and the temperature is 25oC. Because the actual physiological concentrations of ATP, ADP, and Pi are not 1.0 M, and the temperature is 37oC, the free energy required to synthesise ATP under physiological conditions is actually ~ 46.2 kJ mol-1. A 68 kg adult requires an energy intake of 8,550 kJ of food per day (24 hours). Calculate the mass (in Kg) of ATP synthesised by a human adult in 24 hours, assuming that the percentage efficiency of converting inputted calories in ATP is 50%. What percentage of the body weight does this represent?The free energy released by the hydrolysis of ATP under standard conditions is −30.5 kJ/mol. If ATP is hydrolyzed under standard conditions exceptat pH 5.0, is more or less free energy released? Explain.
- Balance the chemical equation for the oxidation of α-linolenic acid to ATP, CO2, and water. (Use the lowest possible ratio of reactants and products.) +The turnover number of the enzyme fumarase that catalyzes the reaction, Fumarate + H20 ===→ L-malate, is 2.5 x 103 S - l and Km = 4.0 X 10- 6 mol/L. Calculate the rate of conversion of fumarate to L-malate if the fumarase concentration is 1.0 x 1 0 - 6 mol/L and the fumarate concentration is 2.04 x 10- 4 mol/L.Given that the AG" values for the hydrolysis of glucose 1-phosphate and glucose 6-phosphate are approximately -21 kJ/mol and –14 kJ/mol, respectively, which statement is true regarding the isomerization shown? glucose 1-phosphate → glucose 6-phosphate O The reaction can likely proceed in either direction and will therefore depend on the concentrations of glucose 1-phosphate and glucose 6-phosphate. O Only the anabolic direction will occur because the free energy change is positive. O The reaction will proceed in both directions simultaneously. This reaction can only proceed in one direction and must be the rate limiting reaction for this point in metabolism.