3. Describe the allosteric regulation of allosteric activation of the a-ketoglutarate dehydrogenase complex in mammalian tissue, by ATP and ADP. Which factor acts as an allosteric activator? Which acts an inhibitor? Why does this make "sense" given the role of this enzyme in the TCA cycle?
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- 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.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…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?…
- 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.2. Prokariotic aldolase are mediated by a Zn2+ and are inhibited by EDTA, eukaryotic aldolases though are inactivated by sodium borohydride. A) Draw out the mechanism of the eukaryotic aldolase and propose a parallel mechanism for the zinc catalyzed prokaryotic reaction. B) Propose a strategy that could be could be used to specifically inhibit prokaryotic aldolases and not eukaryotic?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?
- 5. Protein tyrosine phosphatase-1B (PTP1B) is an important enzyme regulating insulin signaling be- cause it catalyzes the hydrolysis of phosphorylated tyrosine residues on the insulin receptor and on insulin receptor substrates, proteins of approximately 200,000 molecular weight that serve as cell sig- naling intermediates. The reaction has been shown to adhere to the following mechanism in the scheme below: k3 E-P 2- E + AROPO, НОРО,* 2- E • AROPO, ArОH where ArOPO32- represents the phosphorylated aromatic group. (a) (. ) With p-nitrophenyl-phosphate (PNPP), a syn- thetic organic substrate under conditions [So] >> Eo], the traces illustrated in the diagram to the right were obtained whereby the optical density at 410 nm monitors the release of the p-nitrophenolate anion (see reaction scheme above) upon cleavage of the ArOPO32- substrate. What is this phe- nomenon called? What information does this observation 0.14 0.12 [PTP1]=0.054 mM 0.1 0.08 0.06 [PTP1]=0.027 mM 0.04 provide about…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. 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.Compare and contrast Pyruvate Dehydrogenase with a-ketoglutarate dehydrogenaseOutline the mechanisms of both enzymes. Discuss the functions of the coenzymes. List the similarities and the differences between the 2 enzymes. Both are very large membrane bound complexes. What are the advantages of this strategy?How detailed is the enzyme structure known below(It's Pyruvate Dehydrogenase )? What insight(s) does this structural detail give you about the enzyme mechanism.
- 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. |6. 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.19) Consider the table of allosteric effectors and their effect on the following metabolic processes. Glycolysis Gluconeogenesis PDH complex Krebs cycle acetyl-CoA Not applicable AMP Not applicable + glucagon Not applicable Not applicable - Each row contains one error. Correct the error in the table below Table 2 Correction (indicate process and effect (+ or -) acetyl-CoA AMP glucagon - Briefly explain the effect of each allosteric effector on the corrected pathway (based on Table 2 above)