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- The enzyme aldolase catalyzes the reaction shown in the glycolytic pathway: Fructose 1,6-bisphosphate dihydroxyacetone phosphate + glyceraldehyde 3-phosphate The AG" for the reaction is +23.8 kJ mol¯¹ (+5.7 kcal mol−¹), whereas the AG in the cell is −1.3 kJ mol¯¹ (−0.3 kcal mol¯¹). Calculate the ratio of products to reactants under standard (equilibrium) conditions at 37°C. [products] [reactants] 7 x10-5 [products] [reactants] Incorrect Aldolase ===== Calculate the ratio of products to reactants under intracellular conditions at 37°C. 4 ×10-5 Incorrect Complete the statement using your results. under standard conditions under intracellular conditions A reaction that is endergonic under standard conditions can be converted into an exergonic reaction by maintaining the ratio of products to reactants below the equilibrium value.The glucose/glucose-6-phosphate substrate cycle involves distinct reactions of glycolysis and gluconeogenesis that interconvert these two metabolites. Assume that under physiological conditions, [ATP] = [ADP]; [P;] = 1 mM. Consider the glycolytic reaction catalyzed by hexokinase: ATP + glucose ADP + glucose-6-phosphate AG = - 16.7 kJ/mol (a) Calculate the equilibrium constant (K) for this reaction at 298°K, and from that, calculate the maximum [glucose-6-phosphate]/ Iglucose] ratio that would exist under conditions where the reaction is still thermodynamically favorable. (b) Reversal of this interconversion in gluconeogenesis is catalyzed by glucose-6-phosphatase: glucose-6-phosphate + H20 = glucose + P AG" = -13.8 kJ/mola) The following reaction which is catalyzed by aldolase: Fructose-,6-bisphosphate (FBP) + Glyceraldehyde 3-phosphate (GAP) + Dihydroxyacetone phosphate (DHAP) AG for this reaction is 22.8 kJ mol'. In the cell at 37°C, AG for this reaction is -5.9 kJ mol". Determine the ratio [GAP][DHAP]/[FBP]
- The glutamate dehydrogenase (GDH) catalyses the following reaction: *H₂N- H CH₂ CH₂ COO™ acide glutamique COO™ Time (min) A340 + NAD+ + H₂O The answer: GDH 2 1 1.760 1.718 [ammonium sulphate] = 0.33 M [NADH] = 0.205 mg.mL-¹ = 2.9.10-4 M [a-ketoglutarate] = 0.07 M [Protein] = 0.05 mg.mL-¹ COO™ CH₂ The activity of GDH is monitored in the sense of the formation of glutamate using the following conditions: 0.2 mL of 5 M ammonium sulphate 2.4 mL of buffer at pH 8 0.1 mL of NADH at 6.15 mg.mL-¹ (M = 709 g.mol-¹) 0.2 mL of 1 M a-ketoglutarate solution Warm mixture at 25 °C for 5 min Add 0.1 mL of GDH solution containing 1.6 mg.mL-¹protein to start the reaction. 5 3 4 1.675 1.635 1.595 !- Calculate ammonium sulphate, NADH, concentrations in the reaction medium at t = 0. CH₂ The change in absorbance at 340 nm is monitored, in a 1-cm cuvette, every minute for 10 min. Results are given in the table below: Data ENADH at 340 nm = 6220 M-¹.cm-¹ COO acide x-cétoglutarique O + NH4+ + NADH + H* 6 1.550…The ΔG°’ for the aldolase reaction of glycolysis in muscle is +22.8 kJ/mol. Why does the aldolase reaction proceed in the direction of glyceraldehyde-3-phosphate and dihydroxyacetone phosphate during glycolysis?A new drug, Proinebrium, that reduces Kcat (Ki = 2.0 uM) has been developed to treat ethylene glycol poisoning. (1) What concentration of Proinebrium is required to achieve 50% inhibition of ethylene glycol metabolism by alcohol dehydrogenase when the concentraion of ethlyene glycol in the blood is 50 uM?
- Proline racemase catalyzes the conversion between L-proline and D-proline. The Km and kcat for this reaction are 0.15 M and 550/sec respectively. If the enzyme concentration is 1.45 X 10-5 mmole/ml what is the Vmax of this reaction?What terms would best describe the above coupled reaction? (If the DGo for ATP hydrolysis into ADP + inorganic phosphate is -7.3 kcal/mole, and the DGo for maltose synthesis from glucose + glucose is +3.7 kcal/mole, calculate the standard free energy change for the combined reaction of ATP + glucose + glucose g ADP + maltose + inorganic phosphate.) it is non-spontaneous and endothermic (because the overall DGo is negative) it is spontaneous and exothermic (because the overall DGo is negative) it is non-spontaneous and endothermic (because the overall DGo is positive) it is spontaneous and exothermic (because the overall DGo is positive) it is non-spontaneous and exothermic (because the overall DGo is negative)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.
- The degradation of glycogen is catalyzed by the enzyme phosphorylase and has AGO" equal to +3.1 kJ · mol1. The equation for this reaction is shown below. glycogen (n residues) + P;→ glycogen (n-1 residues) + G1P What is the ratio of [P;]/[G1P] under standard conditions? Use 2 significant figures. [P;] : [G1P] = i :1 What is the value of AG under cellular conditions when the [P;/[G1P] ratio is 50/1? Use 2 significant figures. AG = i kJ. mol-1The glucose/glucose-6-phosphate substrate cycle involves distinct reactions of glycolysis and gluconcogenesis that interconvert these two metabolites. Assume that under physiological conditions, [ATP] = [ADP] and [Pi] =1 mM. Consider the following glycolytic reaction catalyzed by hexokinase: ATP + glucose = AG' = -16.7 kJ/mol ADP + glucose-6-phosphate (a) Calculate the equilibrium constant (K) for this reaction at 298 K, and from that, calculate the maximum [glucose-6-phosphate]/[glucose] ratio that would exist under conditions where the reaction is still thermody- namically favorable. (b) The reverse of this interconversion in gluconeogenesis is catalyzed by glucose-6-phosphatase: glucose-6-phosphate + H,0 = glucose + P, AGr = -13.8 kJ/mol K= 262 for this reaction. Calculate the maximum ratio of [glucose]/ [glucose-6-phosphate] that would exist under conditions where the reaction is still thermodynamically favorable. (c) Under what cellular conditions would both directions in the…If the DGo for ATP hydrolysis into ADP + inorganic phosphate is -7.3 kcal/mole, and the DGo for sucrose synthesis from glucose + fructose is +5.5 kcal/mole, calculate standard free energy change for the combined reaction of ATP + glucose + fructose g ADP + sucrose + inorganic phosphate. DGo = -12.8 kcal/mole DGo = -1.8 kcal/mole DGo = 0 kcal/mole DGo = +1.8 kcal/mole DGo = +12.8 kcal/mole