If the Go for ATP hydrolysis into ADP + inorganic phosphate is 7.3 kcal/mole, and the Go for glutamine synthesis from glutamic acid and NH3 is +3.4 kcal/mole, calculate the average Go for coupling these two reactions (glutamic acid + NH3 + ATP glutamine + ADP + inorganic phosphate
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- 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 change1. The enzyme glutamate dehydrogenase is important in the breakdown of amino acids to produce NH4+. High levels of NH4+ in the body are toxic, and for this reason it is used to form urea to be excreted in the urine. a) Using the information provided, calculate the delta G knot prime and the Keq value at 298K for the oxidation of glutamate catalyzed by glutamate dehydrogenase. (Constants: R=8.3J/degree.mol, F=96.1kJ/V.mol) b) Given the reaction above, why would high levels of NH4+ be toxic? c) Given the reaction above, explain how a high concentration of gutamate inside the cell would affect energy production. Be sure to be specific.1. Assuming that everything that’s needed to make tripalmitin comes from glucose, how many glucose would be used by adipose tissue in the synthesis of 1 mol tripalmitin? 2. How many ATP would be used (net of produced and used)? 3. If an animal absorbs 35 g glucose (MW = 180 g/mol) from drinking a can of pop, how many grams of tripalmitin (MW = 807 g/mol) can be produced from it in adipose tissue? Please provide only typed answer solution no handwritten solution needed allowed
- While furthering your studies of iocane powder you determine that a ceular enzyme, iocase will degrade it. Under normal conditions, iocase shows km 0f 1.85 uM and a kcat of 76. The drug sildenafil was found to have no effect on the km of iocanse yet the kcat was found to drop 58 minutes^-1, when the drug was added and no other changes were made in the reaction conditions. What can be inferred from this data? (remember kcat = vmax/et) Sildenafil acts as an uncompetitive inhibitor of iocanse Sildenafil acts as a noncompetitive inhibitor of iocanse The effect of sildenafil could be countered by adding more iocane to the reaction The y-intercept of the sildenafil inhibited iocanse would appear to be lower on a Lineweaver burke plot as compared to uninhibited iocanase The slope of a Lineweaver burke plot of the inhibited versus uninhibited iocanase would remain unchangedThe 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.1. The enzyme glutamate dehydrogenase is important in the breakdown of amino acids to produce NH4+. High levels of NH4+ in the body are toxic, and for this reason it is used to form urea to be excreted in the urine. Using the information provided, calculate the delta G knot prime and the Keq value at 298K for the oxidation of glutamate catalyzed by glutamate dehydrogenase. (Constants: R=8.3J/degree.mol, F=96.1kJ/V.mol) How to identify the final and initial reactions in a group of redox reactions and do we reverse the reduction reaction if the question asks for oxidation?
- 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?A) Is this reaction ( in picture provided) in equilibrium? B) If it is not then ,what is ∆G' at 25°C if the concentration of Glucose-1-phosphate is 15.04µM and the concentration of Glucose-6-phosphate is 1.62 mM? Answer in Joules. Round to the correct number of significant figures. (There are 103 µM in 1mM.) Thank you so Much!!!At body temperature (37°C), k of an enzyme-catalyzed reaction is 2.3X10¹⁴ times greater than k of the uncatalyzed reaction. Assuming that the frequency factor A is the same for both reactions, by how much does the enzyme lower the Eₐ?
- Based on the definition of kcat, substitute a value that can be measured and yet still represents the value associated with the original concentration of the R. What would the rate or velocity of the reaction be equal to under these circumstances? How can cells increase Vmax? What variable that we could change would directly impact Vmax? Would the value of KM be affected by the ways you determined that Vma,x could be increased? What does this indicate about KM? Thinking about how catalysts work, about the Michaelis-Menten Equation, and the definition of kcat, what specifically does the enzyme change in the reaction mechanism to increase the rate? If an enzyme follows the 2 step mechanism proposed by Michaelis-Menten, what do you know about this enzyme? Be very specific and comprehensive. Please answer very soon will give rating surelyThe 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.1 = 2, for sufficiently large values of 1. The energetic equivalent of two molecules of ATP is used to activate an amino acid, yet only one molecule of ATP is used. Explain