3. Calculate the ATP that is produced when linoleic acid (9,12-octadecadienoic acid; 18:2) is (a) oxidized to CO2 and H20 or (b) converted to the ketone body acetoacetate in the liver and then oxidized to CO2 and H20 in the peripheral tissues. 4. Explain the role of AMP-dependent protein kinase in regulating fatty acid metabolism. What are the ways hormonal control of fatty acid metabolism works between fed and fasted states? Please draw by hand/digitally, schematics showing this regulation in adipose tissue, muscle and liver.
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- 1. Outline the first round of lipid catabolism using a C18 saturated fatty acid. Indicate cofactors and type of chemistry that takes place. a. How much NADH, FADH2 and ACCOA are you getting from complete catabolism of this fatty acid? b. How many moles of ATP are you getting from the breakdown of this fatty acid? Keep in mind that in the mitochondria 1 mole FADH2 gives about 1.5 moles of ATP while 1 mole NADH yields about 2.5 moles of ATP.2A. Red blood cells synthesize and degrade 2,3-bisphosphoglycerate (2,3-BPG) by a detour of the glycolytic pathway, as shown below: glyeeraldehyde 3-phosphate GAP dehydrogenase 1,3-bisphosphoglycerate bisphosphoglycerate mutase ADP phosphoglycerate kinase 2,3-bisphosphoglycerate ATP 3-phosphoglycerate 2,3-bisphosphoglycerate phosphatase phosphoglycerate mutase 2-phosphoglycerate (i) The bisphosphoglycerate mutase/2,3-bisphosphoglcerate phosphatase reaction is catalyzed by a single enzyme, BPGM. At alkaline pH, BPGM favors the mutase activity while at lower pH, BPGM favors the phosphatase reaction. Use this information, along with the Bohr effect, to explain in the space below how red blood cells respond to a metabolic defect where a patient experiences chronic, elevated levels of lactic acid. I (ii) Individuals with red blood cell phosphoglycerate kinase deficiency suffer from moderate hemolytic anemia (a condition where red blood cells self-destruct before their normal lifespan). They…1. Explain the reaction mechanism involved how glucogenic amino acids can yield either a pyruvic acid or an oxaloacetic acid. In what pathway will pyruvic or oxaloacetic acid be used and why is this pathway important? 2. Discuss the reaction mechanism involved how the -NH2 groups of amino acids are being metabolized. 3. Explain why gluconeogenesis under conditions of starvation or diabetes breaks down body proteins. Complete answer please. Thank you. |
- Consider docosanoic acid C12H43CO2H a. Label the alpha and beta Carbons. Show the beta-oxidation in an EXPANDED structure. b. Draw each acyl CoA derived from this fatty acid. c. How many acetyl Co A molecules are formed by complete beta-oxidation? d. How many cycles of beta-oxidation are needed for complete oxidation? e. How many molecules of ATP are formed from the complete catabolism of this fatty acid? Show the complete computation. f. How many moles of ATP per gram of fatty acid is formed from the complete catabolism of the given fatty acid? g. What is the molar mass of the given fatty acid? Solution: Show here the complete computations, [from a to e]1. The second high energy intermediate metabolite of glycolysis that can be used for substrate level phosphorylation is also a precursor molecule for the synthesis of several amino acids. Name 5 of these amino acids. 2. Explain the indirect effect that allosteric effectors have on pyruvate dehydrogenase activity through phosphorylation/dephosphorylation of components within the PDH-complex.6. A. List all of the ionizable functional groups that are found in insulin when in aqueous solution. List which amino acid residues have these ionizable groups and list all of the pka and pKb values (including the R groups) that are on both polypeptide chains that make up insulin. (see the table at the end of this HW set; note that tyrosine and cysteine both have unusual pka's, since these side groups ionize above the pKR's given to have a negative charge). B. The isoelectric point of insulin is reported to be around 5.3-5.35. Using the method covered in class, estimate the isoelectric point of insulin and compare your answer to the values above. C. For a polypeptide to be soluble in an aqueous solution, is it good to be near the isoelectric point? Why or why not? Notes: a couple of unusual R group's that ionize (cysteine and tyrosine have R groups that have pka values; histidine has a pkb). The table at the end of this homework set (also in the lecture notes) lists the pka's and…
- 1. Select the INCORRECT statement about Glutamate dehydrogenase : a. Catalyzes the removal of NH4+ into glutamate b.Catalyzes the incorporation of NH*4 into a-ketoglutarate c. Catalyzes the removal of NH*4 from glutamate C d. Catalyzes the incorporation of NH'4 into a-keto acid6. Lovastatin (see picture), is a potent competitive inhibitor of HMG-COA reductase (B-hydroxy- B-methylglutaryl-COA reductase). In addition, the synthetic compound, Terbinafine (see picture), is a potent inhibitor of squalene monooxygenase. Both compounds could be used to treat hypercholesterolemia, a genetic disorder where the patient synthesizes too much cholesterol regardless of dietary intake of cholesterol. a. Predict and explain the effect of these drug on serum cholesterol levels in humans. b. Based on squalene monooxygenase's role in synthesizing sterols, explain why terbinafine is marketed as an anti-fungal agent, and not for hypercholesterolemia.2. (a) ( In contrast to the pyruvate dehydrogen- ase complex, the a-ketoglutarate dehydrogenase (aKGDH) complex is not up- or downregulated by phosphorylation or dephosphorylation. However, the complex exhibits cooperativity modulated by the presence of ADP, ATP, inorganic phosphate (Pi), and Ca2+, as illustrated by the diagram on the right for the bovine kidney enzyme complex. Note in the diagram how the addition of 10 μM Ca2+ shifts the affinity of the enzyme complex for aKG from 20 mM Pi/-Ca2+ to 20 mM Pi/+Ca2+. Calcium especially en- hances the cooperative influence of ADP and ATP. Using the expanded copy of the diagram at the end of the problem set, estimate the change in S0.5 (re- member that for allosteric enzymes S0.5 corresponds to KM of a nonallosteric enzyme) for the enzyme complex in the presence of 20 mM Pi/-Ca2+ and in the presence of 20 mM Pi/+Ca2+. Compare similarly the change in S0.5 for the enzyme in the presence of 20 mM Pi/-Ca2+ plus 1.6 mM ADP to the enzyme in the…
- Consider the docosanoic acid, C21H43CO2H a. Label the a and B carbons b. Draw the acyl CoA derived from this fatty acid c. How many acetyl CoA molecules are formed by complete B-oxidation? d. How many cycles of B-oxidation are needed for complete oxidation? e. How many molecules of ATP are formed from the complete catabolism of this fatty acid?6. Phosphofructokinase is an allosteric enzyme that catalyzes the conversion of fructose 6-phosphate to fructose 1,6-bisphosphate and represents the key control point in mammalian glycolysis. The enzyme is a homotetramer that is inhibited by ATP binding, activated by AMP binding, negatively regulated by phosphorylation, and competitively inhibited by 2,5-anhydro-D-glucotiol-1,6-diphosphate. (a) Would you expect a plot of the initial rate of fructose 1,6-bisphosphate formation as a function of substrate concentration to show a sigmoidal or hyperbolic curve in the absence of any regulators? (b) How would each of the regulators above affect the dynamics of the T state to R state equilibrium of phosphofructokinase? Briefly explain your reasoning. (c) If it were possible to isolate phosphofructokinase monomers in an active form, how would you expect the kinetics in (a) to be affected? How would the rate of the reaction be affected by ATP, AMP, and 2,5-anhydro-D-glucotiol-1,6-diphosphate?…Two of the steps in the oxidative decarboxylation of pyruvate (steps 4 and 5 in the figure) do not involve any of the three carbons of pyruvate, yet are essential to the operation of the pyruvate dehydrogenase (PDH) complex. CH3 Pyruvate Hydroxyethyl TPP 1 TPP TPP CHOH 1 CH3 2 Pyruvate dehydrogenase, E₁ CH3 SH Acetyl lipoyllysine 515 CoA-SH CH3- C-S-COA Acetyl-CoA Oxidized lipoyllysine. Reduced 3 lipoyllysine Dihydrolipoyl transacetylase, E₂ Lys FAD -SH SH FADH₂ Dihydrolipoyl dehydrogenase, E3 NADH + H+ NAD+