Show your calculations for determining the number of ATPs that would be generated from the aerobic oxidation of the following triglyceride: H₂C H₂C -CH3
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- A critical reaction in the production of energy to do work or drive chemical reactions in biological systems is the hydrolysis of adenosine triphosphate, ATP, to adenosine diphosphate, ADP, as described by the reaction ATP(aq)+H2O(l)⟶ADP(aq)+HPO2−4(aq)ATP(aq)+H2O(l)⟶ADP(aq)+HPO42−(aq) for which Δ?∘rxn=−30.5 kJ/molΔGrxn∘=−30.5 kJ/mol at 37.0 °C and pH 7.0. Calculate the value of Δ?rxnΔGrxn in a biological cell in which [ATP]=5.0 mM,[ATP]=5.0 mM, [ADP]=0.10 mM,[ADP]=0.10 mM, and [HPO2−4]=5.0 mM.[HPO42−]=5.0 mM. Δ?rxn=ΔGrxn= kJ/molGiven 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 \muμMMyristoleic acid is a monounsaturated fatty acid found in small amounts in a variety of foods. Calculate the net ATP yield from the complete β-oxidation of myristoleic acid. The formula of myristoleic acid is shown below (it is assumed that the total ATP production is the same for both saturated and unsaturated fatty acids having the same carbon chain length). CH3-(CH2)3-CHCH-(CH2)7-COOH (Given: The oxidation of one NADH yields 2.5 ATP; the oxidation of one FADH2 yields 1.5 ATP; and the oxidation of one acetyl CoA yields 10 ATP. ) Group of answer choices a. 96 ATP b. 92 ATP c. 94 ATP d. 34 ATP e. 36 ATP
- What is the net ATP production for the complete degradation of a C20 fatty acid molecule to CO2 and H2O? Show your computation.How many ATP can be produced from the complete oxidation of myristic acid? (Assume that all acety) Co will enter the TC cycle). Type your solution.Indicate the energy yield or cost, in ATP equivalents, for the following processes: (a) glycogen (3 residues) → 6 pyruvate. (b) 3 glucose → 6 pyruvate(c) 6 pyruvate → 3 glucose.
- What is the ∆G naught' for a phosphoryl transfer from ATP to glycerol? The hydrolysis of α-glycerophosphate to glycerol and inorganic phosphate has a ∆G naught' of -8.37 kj/mol. ATP + H2O <--> ADP + Pi ∆G naught' = -30.5 kj/mol What is the efficiency of this reaction (i.e. what % of the available energy remains in the system after the reaction)? Express your answer as a % of the total amount of energy available in the system. Where does the rest of the energy go?You will perform the protocol below for the calf intestinal alkaline phosphatase (CIP) provided. For each reaction, your final enzyme concentration should be 10 nM CIP. Note: Enzymes purchased are typically labelled with their “units of activity” (U), as this relates to how much enzyme is needed to catalyze a reaction. The 100 nM CIP provided has approximately 3 U/mL and was diluted 1 in 1,000 from a 500 U/mL purchased enzyme. 1) Create a table (similar to the one below) to help you determine and keep track of what to add to each of the cuvettes in which your reactions will be measured. The five different concentrations of PNPP should be: 25, 50, 100, 200, 300 μM. Each reaction will be in a final volume of 1 mL and contain 10 nM alkaline phosphatase. Concentrations of stock solutions: 1.0 mM PNPP, 100 nM calf intestinal phosphataseHow many ATPs are there in this triglyceride? Showing NADH and FADH2 calculations and steps
- The enzyme ATCase (Aspartate TransCarbamoylase) catalyzes an early step in the synthesis of the pyrimidine nucleotides. The activities of the ATCase reactions are shown in the following plots. Which one of the following statements is most correct description about this enzyme and/or this enzyme-catalyzed reaction? ATP No allosteric effectors Vo CTP ATCase 10 20 30 40 (Aspartate] (mM) O A. This enzyme is allosterically inhibited by ATP. B. This enzyme is composed of multiple subunits. C. "ATP" binds to catalytic subunits of ATCase. O D."CTP" binds to the R-state enzyme. O E. At high concentrations of ATP, ATP binds to the T-state enzyme, thus increase the affinity for the substrate [S].Based on your knowiedge of oxidative phosphorylation, answer the following questions: a) Suppose you synthesize an ATP synthase that was devoid of the y (gamma) subunit. How would the catalytic sites of the B subunits of such an enzyme compare to one another? Why? What if only the c-terminus of the y subunit is missing?Glycerol backbone of a fat molecule can be converted to glyceraldehyde-3-phosphate, an intermediate in glycolysis. Assuming that the single glyceraldehyde-3-phosphate undergoes complete oxidation to CO₂, how many ATPs are produced by oxidative phosphorylation only (i.e. exclude ATPs from substrate level phosphorylation) from a single fat molecule? O 20 O 18 O 17 O 15 08