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 (µmol substrate/min/g tissue) Pigeon Enzyme Pheasant Hexokinase 3.0 2.3 Glycogen phosphorylase Phosphofructokinase-1 Citrate synthase Triacylglycerol lipase 18.0 24.0 120.0 143.0 100.0 15.0 0.07 0.01 Why wvore thoge onaa mag geleoted for oomporigon? Wlould the ativitio f triogo nhognhot
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- 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.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.
- . 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 (µmol 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. b. Compare oxygen consumption in the two birds. c. Judging from the data in the table, which bird is the long-distance flyer? Justify your answer. d. Why were these enzymes selected for comparison? Would the activities of triose phosphate isomerase and malate dehydrogenase be equally good bases for comparison? Explain. 18.0 120.0 24.0 143.0 100.0 15.0 0.07 0.01 а.. 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.What is the catalytic efficiency of Catalase ? Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Carbonic anhydrase Substrate CO2 HCO3 KM (M) 1.2 x 10-2 2.6 x 10-2 Kcat (s-1) 1.0 x 106 4.0 x 105 Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 O A. 4 x 108 M-s-1 O B. 4 x 108 M-1.s-1 OC25x 10-9 M-s1 D. 2.5 x 102 M-1.s-1 OE 1.0 x 107 s1
- 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.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.) As mentioned in the March1 outline a critical step in the glycolysis metabolic pathway (conversion for glucose to pyruvate that produces 2 ATP's) is the attachment of dihydroxyacetone phosphate to an isomerase enzyme via an iminium bridge (step1). There is a second step that takes the imine to the enamine that sets up the C-C formation reaction with an enol that you'll cover in two weeks. Show the mechanism for steps 1 (mild acid catalysis) and 2 (draw resonance forms for the iminium cation). In your mechanism, show the intermediate hemiaminal (carbinolamine). Step 2 may address one of the questions asked in Wednesday's class about the water taking out the N-H proton of the iminium cation versus a C-H proton? CH₂OPO3² E-NH₂ + O=C (step 1) CH₂OH Dihydroxyacetone phosphate Iminium (+) cation intermediate (step 2) Enamine (Enol) Intermediate H CH₂OPO32- E-N-C H C. OH H₂O E
- (b) ☐ The exergonic reactions catalyzed by isocitrate dehydrogenase (ICDH) and α- ketoglutarate dehydroge-nase (aKGDH) are regu- lated by metabolites, in addition to the reaction catalyzed by citrate synthase. The diagram to the right illustrates the activity of ICDH (A,▲) and aKGDH (O,●) in the presence of 1.5 mM ADP (O,A) or 1.5 mM ATP (●,▲). In muscle tissue contraction of sarcomeres initiated by a nerve im- pulse results first in the release of Ca 2+ from the sarcoplasmic reticulum. As indicated by the chang- es in velocity of the two enzymes, what are the flux changes of the TCA cycle in muscle tissue upon release of Ca2+ under the influence of ADP viz. ATP and under the influence of NAD+ viz. NADH on cit- rate synthase? 100 75 Stimulation of activity (% of maximum) ŏ 25 1. -8 -7 -6 log {[Ca2+] (M)}2. If glyceraldehyde-3-phosphate dehydrogenase in red blood cells is completely inhibited, which intermediates in glycolysis accumulate most? Please use the following equation and the provided information to explain your reasoning. AG=AG° + RTln [C][D]d [A] [B]¹ Fructose 1,6-bisphosphate → Glyceraldehyde 3-phosphate + Dihydroxyacetone phosphate The standard free energy for the above reaction is: AG" = +23.9 KJ/mol T° = 298 R = 8.314 J mol-¹ K-¹2. If glyceraldehyde-3-phosphate dehydrogenase in red blood cells is completely inhibited, which intermediates in glycolysis accumulate most? Please use the following equation and the provided information to explain your reasoning. AG=AG° + RTln [C] [D]d [A] [B]' Fructose 1,6-bisphosphate → Glyceraldehyde 3-phosphate + Dihydroxyacetone phosphate The standard free energy for the above reaction is: AG" = +23.9 KJ/mol T° = 298 R = 8.314 J mol-¹ K-1