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.
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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.
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- 27. The standard-state free energy of hydrolysis for acetyl phosphate in 1,3-Bisphosphoglycerate is 1,3-Bisphosphoglycerate + H₂O 3-phosphoglycerate + Pi AGI-49.6 kJ/mol. Determine the free energy change for 1,3-Bisphosphoglycerate hydrolysis in a solution of 5.4 mM 3-phosphoglycerate, 0.0054 M inorganic phosphate, and 20 nM 1,3-Bisphosphoglycerate.A 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.-73.6Given 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.
- 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.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.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.
- [References) The AG" for the reaction ATP + H₂O ADP + P + H+ is -30.5 kJ mol'¹, Other organophosphate species also undergo hydrolysis of the phosphate moiety via a similar reaction. Determine the value of AG for the following reactions and indicate if the reaction will proceed spontaneously in the direction written if the reactants and products are initially in a 1:1 molar ratio. a. ATP + Glucose ADP+ Glucose-1-phosphate AG⁹¹ = kJ mol-1 The reaction is (The hydrolysis reaction for glucose-1-phosphate is Glucose-1-phosphate + H₂0 Glucose + P + H+; AG-20.9 kJ mol ¹.) b. ATP + Glutamate Carbamoyl phosphate + ADP AG The reaction is kJ mol-1 (The hydrolysis reaction for carbamoyl phosphate is Carbamoyl phosphate + H₂0 Glutamate + P, + H+ ; AG¹ = -51.4 kJ mol ¹.) Submit Answer Try Another Version 3 item attempts remaining80mL of a 0.3M solution of hexapeptide Leu-His-Cys-Glu-Asn-Arg is adjusted to pH=pI. The solution is then titrated with 0.2M HCL to a final pH of 2.1. Sketch the titration curve, labelling the pH and volume axes. Indicate the volume of HCL needed to reach relevant pKa value and equivalence point(s)z Relevant pKa values are: 2.1, 4.3, 6.0, 8.3, 9.8, and 12.5.Substrate Concentration (mol L1) Velocity (mM min-1) 2.500 0.588 1.000 0.500 0.714 0.417 0.526 0.370 0.250 0.256 Determine the values of Km and Vmax for the decarboxylation of a 훃-keto acid given the followingdata. You have to plot the graph by using excel and please include the scope of graph
- Quinine ( C20 H24 N2 O2) is the most important alkaloid derived from cinchona bark. It is used as an antimalarial drug. For quinine, pK, = 5.1 and pK, = 9.7 ( pKp = – log Kp). Only 1 g quinine will dissolve in 1920.0 mL of solution. Calculate the pH of a saturated aqueous solution of quinine. Consider only the reaction | Q+ H2O= QH+ + OH- described by pK, where Q = quinine. pH =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…80mL of a 0.3M solution of hexapeptide Leu-His-Cys-Glu-Asn-Arg is adjusted to pH=pl. The solution is then titrated with 0.2M HCI to a final pH of 2.1. Sketch the titration curve, labelling the pH and volume axes. Indicate the volume of HCl needed to reach each relevant pKa value and equivalence point(s). Relevant pka values are: 2.1, 4.3, 6.0, 8.3, 9.8, and 12.5.