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- .Intramitochondrial ATP concentrations are about 5 mM, and phosphate con- centration is about 10 mM. If ADP is five times more abundant than AMP, calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate AG for ATP hydrolysis at 37 °C under these conditions. The energy charge is the concentration of ATP plus half the concentration of ADP divided by the total adenine nucleotide concentration: [ATP] + 1/2[ADP] [ATP] + [ADP] + [AMP](d) of glucose oxidation in diabetic human patients treated with Metformin (●) and in (nondiabetic) control human patients (0). At –150 min both groups of subjects were started on an intravenous feed of 3-(®H)-glucose, and at t = 0 min they were started on an oral glucose tolerance test whereby a measured amount of glucose in water (a syrupy mixture) was swallowed followed by measure- ment of blood glucose levels at 30 min intervals. The flux of glucose oxidation was measured by the appear- ance of 3H2O in the blood stream. While the information The diagram to the right compares the rate 8000 ORAL GLUCOSE 6000- 4000- 2000- -120 -60 60 120 180 240 300 Minutes cannot be directly extracted from the reaction mecha- nism diagrams in the textbook, the glycolytic step in which the tritium is first released into water is that catalyzed by TPI, as illustrated at the beginning of Question #3. Explain why this step is suitable for measuring the flux of glycolysis through the release of °H…3. Triose-phosphate isomerase (TPI) catalyzes the movement of a single proton to interconvert dihy- droxyacetone phosphate and glyceraldehyde 3-phosphate in glycolysis and gluconeogenesis. The enzyme, a dimer of identical subunits that are 248 amino acids in humans, has no cofactors, required metal ions, or cooperativity between subunits. The enzyme is found in all tissues. The value of Kcat/KM - 9.2 x 106 sec-'M-1 is close to the rate constant expected for a diffusion-limited reaction. The mechanism of the proton transfer is illustrated in the diagram below. Glu-165 Giu-165 Glu-165 ks HR H 20,PO HO, OH His-95 His-95 His-95 (a) ing structural formulas and naming enzymes and glycolytic intermediates, the reactions of the payoff phase. Consider only anerobic glycolysis. Remember that each glucose molecule yields two mole- cules of glyceraldehyde-3-phosphate (GAP). Indicate the net yield of ATP and NADH generated through anaerobic glycolysis per glucose molecule. The reaction catalyzed by…
- 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…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?…9. In a patient with a hereditary disease caused by liver phosphorylase kinase defect, hepatomegaly is observed (an increase in liver size), glycogen of the normal structure accumulates in the liver cells, moderate hypoglycemia is observed 3 hours after a meal. Explain the listed symptoms and the accumulation of unchanged structure glycogen in this pathology. For this: a) draw a process diagram in which phosphorylase kinase is involved; b) indicate the metabolic block on the diagram and explain the symptoms observed in the patient.
- . Because of the position of arsenic in the periodic table, arsenate (AsO}-) is chemically similar to inorganic phosphate and is used by phosphate-requiring enzymes as an alternative substrate. However, organic arsenates are quite unstable and spontaneously hydrolyze. Arsenate is known to inhibit ATP production in glycolysis. Identify the target enzyme, and explain the mechanism of inhibition.Because it resembles the two physiological substrates, phosphonacetyl L - aspartate (PALA) is a strong inhibitor of ATCase. Low concentrations of this unreactive bisubstrate analog, on the other hand, enhance reaction velocity in the presence of substrates. The reaction rate rises as PALA is added, until three molecules of PALA are attached per molecule of enzyme. This maximum velocity is 17 times higher than it would be without PALA. With the addition of three additional molecules of PALA per molecule of enzyme, the reaction rate drops to practically nil. Why does PALA activate ATCase at such low concentrations?3. One indication of the relative importance of various ATP-producing pathways is the Vmax of certain enzymes of these pathways. The values of Vmax of several enzymes from the pectoral muscles (chest muscles used for flying) of pigeon and pheasant are listed below. Vmax (umol substrate/min/g tissue) Pigeon Enzyme Pheasant Hexokinase 3.0 2.3 Glycogen phosphorylase Phosphofructokinase-1 Citrate synthase Triacylglycerol lipase 18.0 120.0 24.0 143.0 100.0 15.0 0.07 0.01 c. Judging from the data in the table, which bird is the long-distance flyer? Justify your answer.
- 3. One indication of the relative importance of various ATP-producing pathways is the Vmax of certain enzymes of these pathways. The values of Vmax of several enzymes from the pectoral muscles (chest muscles used for flying) of pigeon and pheasant are listed below. Vmax (umol substrate/min/g tissue) Enzyme Pigeon Pheasant Hexokinase 3.0 2.3 Glycogen phosphorylase Phosphofructokinase-1 Citrate synthase Triacylglycerol lipase 18.0 120.0 143.0 24.0 100.0 15.0 0.07 0.01 b. Compare oxygen consumption in the two birds.3. One indication of the relative importance of various ATP-producing pathways is the Vmax of certain enzymes of these pathways. The values of Vmax of several enzymes from the pectoral muscles (chest muscles used for flying) of pigeon and pheasant are listed below. Vmax (umol substrate/min/g tissue) Pigeon Enzyme Pheasant Hexokinase 3.0 2.3 Glycogen phosphorylase Phosphofructokinase-1 Citrate synthase Triacylglycerol lipase Discuss the relative importance of glycogen metabolism and fat metabolism in generating ATP in the pectoral muscles of these birds. 18.0 120.0 24.0 143.0 100.0 15.0 0.07 0.01 а.Select a property that does not belong to allosteric enzymes. They conform to hyperbolic Michaelis-Menten kinetics They may have binding sites for regulatory molecules that are separate from active sites They tend to have a signmoidal curve of rate versus [S] They undergo conformation changes as a result of modulator binding.