Velocity, activity units/mg protein 51 3 2 0 5 15 20 Aspartate concentration, mM - 10 Control With With CTP With ATP CTP 25 Figure 2: Kinetics of ATCase in the presence of ATP and CTP (based on Gerhart and Pardee, 1962). The kinetics of the ATCase reaction were examined using increasing concentrations of aspartate, in the presence and absence of CTP and ATP as shown in Figure 2. a. What information can you obtain by looking at the shapes of the curves in this figure? b. What kinetic parameter(s) change in the presence of CTP? What parameter(s) do not change? What is the significance of these observations? c. Answer question 2b for ATP.
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- Initial rate data for an enzyme that obeys Michaelis–Menten kinetics areshown in the following table. When the enzyme concentration is 3 nmolml-1, a Lineweaver–Burk plot of this data gives a line with a y-intercept of0.00426 (μmol-1 ml s). (a) Calculate kcat for the reaction.(b) Calculate KM for the enzyme.(c) When the reactions in part (b) are repeated in the presence of 12 μM ofan uncompetitive inhibitor, the y-intercept of the Lineweaver–Burk plotis 0.352 (μmol-1 ml s). Calculate K′I for this inhibitor.Standard redox potentials Eo' for some common compounds in biochemistry: Eo' (Volt) + 0,81 +0,42 + 0,25 12 O₂ + 2 H+ + 2 e NO3 + 2 H+ + 2 e 2 cyt c (ox) + 2 e 2 cyt b (ox) + 2 e Pyruvate + 2 H+ + 2 e* NAD + 2 H+ + 2 e Acétoacétate + 2 H+ + 2 e (2) acétoacétate + NADH + H+ H₂O NO₂ + H₂O 2 cyt c (red) 2 cyt b (red) Lactate (3) 2 cyt c (ox) + 2 cyt b (red) NADH + H+ B-hydroxybutyrate + 0,08 - 0,19 With the help of the above table, determine the spontaneous direction of the following reactions in the standard conditions. Justify your answers by calculating the Gibbs (free) energy of reaction in each case. (1) pyruvate + ß-hydroxybutyrate -0,32 - 0,35 lactate + acétoacétate B-hydroxybutyrate + NAD+ 2 cyt c (red) + 2 cyt b (ox)Begining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq (to one decimal point) of the reaction Pyruvate + NADH+H+ <=> Lactate + NAD+.Note the temperature of this reaction will not affect the standard reducton potential delta E'o in the table 13-7b. please provide a comprehensive explanation with each step taken.
- Begining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq of the reaction Pyruvate + NADH Lactate + NADH+H+. Note the temperature of this reaction will not affect the standard reducton potentialCALCULATIONS OF THE SOLUTIONS FOR EXPERIMENT Substrates Stock concentations Succinate + glutamatate (G/S) 150 mM Glutamtate + 150 mM Succinate Malate + pyruvate (M/P) 30 mM Malate + 30 mM Pyruvate Inhibitors Substrates of ETC ATP stock (50 µM): Make pre-dilutions with 20, 15, 10, 5, 2,5 and 1,25 μM ATP (1000 μL of each) Rotenone Oligomycin CCCP KCN Antimycin A Calculate the needed volumen of the standards! Inhibitors of ETC Stock concentations 400 µg/ml in DMSO 1250 µg/ml in EtOH 1000 µg/ml in DMSO 400 mM in Tris-buffer 1 mg/ml in DMSO Calculate the needed volumen! Final concentrations (in 250 μL) 8 μg/ml 25 µg/ml 20 µg/ml 8 mM 20 µg/mlBegining with 1 M concentrations of each reactant and product at pH=7 and 25.0 degrees C, calculate the K'eq of the reaction Pyruvate + NADH Lactate + NADH+H+. Note the temperature of this reaction will not affect the standard reducton potential delta E° in the table 13-7b.
- Many years later, in 1989, Wild, et al. revisited the idea of allosteric control of ATCase by CTP. They noted that CTP did indeed inhibit ATCase, but that the inhibition was always incomplete, even at high concentrations of CTP. They hypothesized that perhaps CTP did not act alone, but in combination with some other nucleotide. They tested the activity of ATCase in the presence of several nucleotide combinations. The results are shown in Table 3. a. What combination gives the most effective inhibition? b. What is the physiological significance of this combination? c. Revise Figure 1 to include this new information. d. Redraw Figure 2 to include this new information. How does the combination compare with the values for the nucleotides alone? Table 3: Relative specific activities for combinations of nucleotide effectors. A value greater than one indicates stimulation, a value less than one indicates inhibition. Nucleotide Effector ATP CTP GTP UTP ATP/CTP ATP/GTP ATP/UTP CTP/GTP CTP/UTP…Explain the difference between ΔG°’ and ΔG and calculate the free energy (delta G) of hydrolysis of ATP in a rat liver cell in which the ATP, ADP, and Pi concentrations are 3.4, 1.3, and 4.8 mM.Kinetic Parameters of Enzyme-Catalyzed Reactions TABLE 12-1 The Values of KM, Keat, and Keat/KM for Some Enzymes and Substrates Enzyme Substrate KM (M) 9.5 x 10-5 1.2 x 10-² 2.6 x 10-2 2.5 x 10-2 4.4 x 10-1 8.8 x 10-2 6.6 x 10-4 Acetylcholinesterase Carbonic anhydrase Catalase Chymotrypsin Fumarase Urease Acetylcholine CO₂ HCO₁ H₂O₂ N-Acetylglycine ethyl ester N-Acetylvaline ethyl ester N-Acetyltyrosine ethyl ester Fumarate Malate Urea 5.0 x 10-6 2.5 x 10-5 2.5 x 10-2 Keat (S-¹) 1.4 x 104 1.0 × 106 4.0 × 105 1.0 X 107 5.1 x 10-2 1.7 × 10-1 1.9 X 10² 8.0 x 10² 9.0 × 10² 1.0 X 104 Keat/KM (M¹s¹) 1.5 × 108 8.3 x 107 1.5 x 107 4.0 X 108 1.2 x 10-1 1.9 2.9 × 105 1.6 × 108 3.6 X 107 4.0 X 105 Which enzyme is the most catalytically efficient? Which substrate does chymotrypsin bind to most tightly (assume k_₁ >> K₂)? Is fumarate or malate a better substrate of fumarase? Is it possible to have a kcat/KM of greater than 1 x 10⁹ M-¹ s-¹? Why or why not?
- KINETIC CONSTANT No Na2HPO4 25mM Na2HPO4 50mM Na2HPO4 Vmax nmol p-NP. Min- 20.3252 14.30615 17.30104 Km mM -0.819106 -0.46495 -0.352941 1. What does this suggest about the structure of the active side of the enzyme?Arrange the balanced biochemical equations for all the reactions in the catabolism of glucose to two molecules of glyceraldehyde 3-phosphate (the preparatory phase of glycolysis). First step Last step Answer Bank Fructose 1,6-bisphosphate - dihydroxyacetone phosphate + glyceraldehyde 3-phosphate Fructose 6-phosphate + ATP →→→→ fructose 1,6-bisphosphate + ADP Glucose + ATP → glucose 6-phosphate + ADP Dihydroxyacetone phosphate glyceraldehyde 3-phosphate Glucose 6-phosphate →→→→ fructose 6-phosphateConsider decosanoic acid C12H43CO2H SUB PART TO BE SOLVED How many cycles of beta-oxidation are needed for complete oxidation? How many molecules of ATP are formed from the complete catabolism of this fatty acid? Show the complete computation. How many moles of ATP per gram of fatty acid is formed from the complete catabolism of the given fatty acid? What is the molar mass of the given fatty acid? Solution: Show here the complete computations, [from 1 to 4]