4) What is the net ATP produced from the complete oxidation to CO2 and H20 of a C10 saturated fatty acid? Show calculations below.
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- 4) What is the net ATP produced from the complete oxidation to CO2 and H20 of a Cao saturated fatty acid? Show calculations below.Carbonic anhydrase catalyzes the hydration of CO. CO2 + H2O ¬ H½CO3 The Km of this enzyme for CO, is 1.20×104 µ.M. When [CO,] = 3.60×104 µM, the rate of reaction was 4.50 umol·mL! sec-1 a What is Vmax for this enzyme? umol·mL-!sec-!a) Calculate the enzyme and specific activity of a reaction with 3 pM Hsp90 using the following information: The rate is measured in a spectrophotometer as 0.028 OD units/min in a 1 ml reaction volume. The absorbance was detected at 340nm and the extinction coefficient for NADH at this wavelength is 6200L M- 1 min-1 and the molecular mass of Hsp90 is 82.7 kDa. The rate of NADH utilisation is equivalent to the rate of ATP utilised by Hsp90. Show all your calculations and the units for your answers. b) Calculate the turnover number for the reaction described in (a) above
- a) Calculate the enzyme and specific activity of a reaction with 3 μM Hsp90 using the following information: The rate is measured in a spectrophotometer as 0.028 OD units/min in a 1 ml reaction volume. The absorbance was detected at 340nm and the extinction coefficient for NADH at this wavelength is 6200 L M-1 min-1 and the molecular mass of Hsp90 is 82.7 kDa. The rate of NADH utilisation is equivalent to the rate of ATP utilised by Hsp90. Show all your calculations and the units for your answers. b) Calculate the turnover number for the reaction described in (a) aboveB) The actual concentrations of ATP, ADP and Pi differ by tissue/cell type (see table). Tissue/Cell Type ATP (mM) ADP (mM) Pi (mM) Liver 3.5 1.8 5.0 8.0 2.7 Skeletal Muscle 8.0 0.9 Brain 2.6 0.7 Calculate AG' for ATP hydrolysis in liver. (NOTE: assume 25°C and omit the concentration of water in your calculations).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
- Imagine that in red blood cells (RBCS) the following concentrations were noted for the "adenylate pool": [ATP] = 2000 uM; [ADP] = 270 uM; and [AMP] = 30 uM. ASsume that the pH is 7 and remains constant. a) calculate the Energy change (EC) (to four decimal places for RBCS given the above values. Show work b) If the [ATP] decreases by 5%, calculate the new [ATP], [ADP], and [AMP] given that the concentrations of all three species are "connected" by the adenylate kinase reaction, which is shown below. You will need to use the quadratic equation for this one. show your work. %3| %3D ADP + ADP ATP + AMP Keq = 0.44Discuss the relationship between redox potentials E0’ and the organization of the components of the electron transport chain. Be specific, i.e., use data/actual values to back up your discussion. a) What are the values of E0’ for all the components of the ETS? b)How are the E0’ related to ∆G values? c) How do the values of E0’ vary among the participants in the ETS relative to their position in the ETS?Discuss how many ATP would be synthesized from the complete oxidation of stearic acid or linoleic acid to carbon dioxide and water. Discuss how many ATP would be synthesized from the complete oxidation of stearic acid to carbon dioxide and water. What additional steps are required to oxidize linoleic acid? Include relevant chemical structures and reactions. Explain why the complete oxidation of linoleic acid leads to fewer ATP than the oxidation of stearic acid.
- Study is being done where protein A isomerase (AI) is being phosphorylated by AI phosphorylase (AIP), at 37oC at physiological pH of approximately 7.4 with excess of Mg2+ and ATP. The Vmax and Km are determined to be 9 mM s-1 and 15 uM, respectively a) does AIP need any coenzymes, cofactors, co-substrates? b) what would be the formula for initial rate as a function of AI concentration? (Michaelis-Menten equation) c) what are the intial rates of reaction when [AI] = 3, 6 and 40 uM? Is the trend in initial rate vs [substrate] surprising? Explain.The standard free energy variation of the ATP hydrolysis reaction is ΔGº’ = -30.5 kJ / mol ATP + H2O ⇄ ADP + Pi In red blood cells, when the concentration of Pi is 1.6 mM, the real change in energy free is ΔG = - 50'2 kJ / mol. a) Calculate under these conditions what is the ratio [ATP] / [ADP] in the red blood cells. b) Determine the equilibrium constant K 'of the reaction outlined above. c) If the ADP concentration were 0.2mM, what would be the effective concentration of ATP corresponding to equilibrium.Given the following information, calculate the catalytic efficiency of the enzyme. Step by step please [S] = 100 mM k1 = 10 sec-1 k2 = 3000 sec-1 k-1 = 20 sec-1 [E]T = 1 \muμM