Indicate the total number of ATPs produced in each of the following oxidation reactions from 5 moles of glucose. A. pyruvate to Acetyl CoA B. glucose to Acetyl CoA C. Citric acid cycle
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Problem #1: Indicate the total number of ATPs produced in each of the following oxidation reactions from 5 moles of glucose.
A. pyruvate to Acetyl CoA
B. glucose to Acetyl CoA
C. Citric acid cycle
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- Problem # 3: Calculate the number of moles of ATP produced from the complete oxidation of 900 g glucose in the cells. Show your computation/solution.Problem 2. When alcohol is consumed in excessive quantities, the resulting levels of NADH cause metabolic abnormalities, and one of which is high levels of fatty acid synthesis. Fatty acid synthesis, also a cytoplasmic process, uses acetyl-CoA as a substrate and NADPH as a reducing agent. Based on the above, we can see how acetate is converted to acetyl-CoA in the mitochondria, but fatty acid synthesis takes place in the cytosol. Complete the analysis by accounting for high acetyl-CoA concentration in the cytosol. Study the summary of reactions of citrate metabolism. E. How would increasing the rate of the reaction catalyzed by malate dehydrogenase decrease the concentration of oxaloacetic acid (OAA) in the cytosol? F. How would decreasing the concentration of OAA increase the concentration of acetyl-CoA in the cytosol by Le Chatelier’s principle?Problem 3. Excess alcohol consumption can result in fatty liver disease. Liver cells synthesize triacylglycerides from fatty acids formed by fatty acid synthesis. Excess triacylglycerides can accumulate in the liver compromising normal liver function. D.Explain how stimulation of the rate of fatty acid synthesis changes the rate of fatty acid oxidation based on allosteric regulation of the rate-limiting step of beta-oxidation.
- Problem 3. Excess alcohol consumption can result in fatty liver disease. Liver cells synthesize triacylglycerides from fatty acids formed by fatty acid synthesis. Excess triacylglycerides can accumulate in the liver compromising normal liver function. A.Explain how palmitoyl-CoA is related to fatty acyl CoASH esters (acyl-CoA) B.Explain how increasing the rate of triglyceride formation changes the concentration of acyl-CoA in the cytosol. C.Explain how the rate of triglyceride formation stimulates the rate of fatty acid synthesis based on the concentration of palmitoyl-CoA in the cytosolI am needing help with problems 1 and 3, please. Thank you. 1) Yeast uses anaerobic respiration. If yeast utilized aerobic respiration, would the balloons have inflated faster or slower? Why? 2) Glycolysis in an anaerobic environment produces a net of 2 ATP and Pyruvate. Why does Yeast bother to ferment Pyruvate to Ethanol? Also, what do you think would happen if yeast DID NOT ferment pyruvate to ethanol? 3) Glycolysis in an aerobic environment leads to the production of many more ATP biomolecules. Briefly describe the additional steps necessary to harvest more energy from glucose breakdown. Include the step where Oxygen is used, since it is the key factor that determines the amount of ATP produced.Task 1. How many ATP is produced in entire oxidation of 1 acetoacetate molecule? Will you get more or less ATPs oxidizing β-hydroxybutyrate?
- Question 27 options: If 4 molecules of glucose entered into cellular respiration in the presence of O2, how many molecules of NADH will be formed assuming complete oxidation of each glucose molecule?Lab Exercise 10C, the purpose of adding NaCl (table salt) to Pizza Dough is to: a. catalyze oxidation of fatty acids to lactic acid b. carry H2 reducing equivalents during the baking process c. hydrolyze alcohol so that it does not accumulate in the dough d. tighten cross-linkages in the gluten matrix making the dough more elastic and chewy e. control how fast yeast cells produce CO2 during the leavening processProblems 14 and 15: some of the exponents are unclear. Here they are: 14. Calculate vi and the degree of inhibition caused by a competitive inhibitor under the following conditions:(a) [S]=2x10-3 Mand[I]=2x10-3 M(b) [S]=4x10-4 Mand[I]=2x10-3 M (c) [S]=7.5x10-3 Mand[I]=10-5 MAssume that Km = 2 x 10-3 M, Ki = 1.5 x 10-4 M and Vmax = 270 nmoles x liter-1 x min-1.The degree of inhibition is the percent of the uninhibited velocity reached in the presence of the inhibitor. 15. (a) What concentration of competitive inhibitor is required to yield 75% inhibition at a substrate concentration of 1.5 x 10-3 M if Km =2.9x10-4 M and Ki =2x10-5 M? (b)Towhatconcentration must the substrate be increased to reestablish the velocity at theoriginal uninhibited value?
- Question: Determine the Km and Vmax for this enzyme/substrate combination. [Substrate] (mM) V0 (mM/min) 0.25 0.183 0.50 0.356 1.00 0.665 2.50 1.45 5.00 2.35 What is the concentration of substrate necessary to achieve a turnover rate of 1.00 mM/min?Problem: Alcohol Dehydrogenase catalyzes the conversion of ethanol to acetaldehyde. This enzyme, in its active state, consists of a protein molecule and a zinc ion. On the basis of this information, identify the following for this chemical system. Substrate Apoenzyme Cofactor HoloenzymePlease provide an explanation for how to work through this practice problem: Using table 12.1, calculate the free energy change for the synthesis of ATP from cAMP and inorganic phosphate. (Note: cAMP is hydolyzed to AMP, and the free engery of hydrolysis for ATP and ADP is approximately equal.) Table 12.1: (Compound: Change in Free Energy in kJ/mol) cAMP: -50.4 Creatine phosphate: -43.3 ATP: -30.5 Glucose 6-phosphate: -13.9 AMP: -9.2