Calculate the actual, physiological AG for the reaction Phosphocreatine + ADP = creatine + ATP
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- Calculate the standard free-energy change of the reaction catalyzed by theenzyme phosphoglucomutase, given that, starting with 20 mM glucose 1-phosphate and no glucose 6- phosphate, the final equilibrium mixture at 25 °C and pH 7.0 contains 1.0 mM glucose 1-phosphate and 19 mM glucose 6-phosphate. Does the reaction in the direction of glucose 6-phosphate formation proceed with a loss or a gain of free energy?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 changeThe phosphoryl group transfer potentials for glucose-1-phosphate and glucose-6-phosphate are 20.9 kJ/mol and 13.8 kJ/mol, respectively. (a) What is the equilibrium constant for the reaction shown below at 25 °C? (b) If a mixture was prepared containing 1 m glucose-6-phosphate and 1 x 10-3 M glucose-1-phosphate, what would be the thermodynamically favored direction for the reaction?
- 1. a. Calculate the physiological DG of the reaction shown below at 37°C, as it occurs in the cytosol ofneurons, with phosphocreatine at 4.7 mM, creatine at 1.0 mM, ADP at 0.73 mM, and ATP at 2.6mM. The standard free energy change for the overall reaction is –12.5 kJ/mol. Phosphocreatine + ADP ® creatine + ATP b. The enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose6-phosphate. Calculate the standard free energy change of this reaction if incubation of 20 mMglucose 1-phosphate (no glucose-6 phosphate initially present) yields a final equilibrium mixtureof 1.0 mM glucose 1-phosphate and 19 mM glucose 6-phosphate at 25°C and pH 7.0. c. If the rate of a nonenzymatic reaction is 1.2 x 10–2 μM s–1, what is the rate of the reaction at 37℃ inthe presence of an enzyme that reduces the activation energy by 30.5 kJ/mol?The standard free energy change for the reaction catalyzed by phosphoglucomutase is -7.1kJ/mol, (a) calculate ΔG at 37°C when the concentration of glucose-1-phosphate is 1-mM and the concentration of glucose-6-phosphate is 25-mM, (b) Is the reaction spontaneous under these conditions?Given the following data, calculate Keq for the denaturation reaction of the protein β-lactoglobin at 25oC: ΔH° = –88 kJ/mol ΔS° = 0.3 kJ/mol. The free energy of hydrolysis of ATP in systems free of Mg2+ is −35.7 kJ/mol. When the concentration of this ion is 5 mM, ΔG°observed is approximately −31 kJ/mol at pH 7 and 38°C. Suggest a possible reason for this effect.
- The turnover number for an enzyme that approximates Michaelis-Menten kinetics is known to be 500 min^-1. From the results shown in the table, enumerate Km and total amount of enzyme present. What is the Km for this enzyme? What is the Vmax for this enzyme? And what is the [E]T for this enzyme?Calculate the standard-state free energy change for the isomerization of glucose-1-phosphate to glucose-6-phosphateIf a 0.1 M solution of glucose 1- phosphate at 25 °C is incubated with a catalytic amount of phosphoglucomutase, the glucose 1-phosphate is transformed to glucose 6-phosphate. At equilibrium, the concentrations of the reaction components are Calculate Keq and ΔG′° for this reaction.
- If a reaction has a ΔG°′ value of at least −30.5 kJ · mol−1, suffi -cient to drive the synthesis of ATP (ΔG°′ = 30.5 kJ · mol−1), can it still drive the synthesis of ATP in vivo when its ΔG is only −10 kJ · mol−1? Explain.Neutral sphingomyelinase 2 converts sphingomyelin into ceramide and phosphorcholine. What kind of enzyme is it? Assume Vmax is 35 µM min-1. When you provide 3.0 x 10-5 M of sphingomyelin, you observe an initial velocity of 6.0 µM min-1. Calculate the KM.Determine the values of KM and Vmax for the decarboxylation of a β-keto acid given the following data.