Biochemists consider the citric acid cycle to be the cen-tral reaction sequence in metabolism. One of the key steps isan oxidation catalyzed by the enzyme isocitrate dehydrogenaseand the oxidizing agent NAD. Under certain conditions, thereaction in yeast obeys 11th-order kinetics Rate=k[enzyme][isocitrate]⁴[AMP]²[NAD⁺]m[Mg²⁺]² What is the order with respect to NAD⁺?
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- Ethanol as a Source of Metabolic Energy (Integrates with Chapters 19 and 20.) Acetate produced in ethanol metabolism can be transformed into acetyl-COA by the acetyl thiokinase reaction: Acetate+ATP+CoASHacetyleCoA+AMP+PPiAcetyle-CoA then can enter the citric acid cycle and undergo oxidation to 2 CO2by this route, assuming oxidative phosphorylation is part of the process? (Assume all reactions prior to acetyl-CoA entering the citric acid cycle occur outside the mitochondrion). Per carbon atom, which is a better metabolic fuel, ethanol or glucose? That is, how many ATP equivalents per carbon atom are generated by combustion of glucose versus ethanol to CO2?Page of 6 ZOOM + name: 3. In the last reaction of the citric acid cycle, malate is dehydrogenated to regenerate the oxaloacetate necessary for the entry of acetyl-CoA into the cycle: L-Malate + NAD+ → oxaloacetate + NADH + H* AG'° = 30.0 kJ/mol (a) Calculate the equilibrium constant for this reaction at 25 °C. (b) Because AG°' assumes a standard pH of 7, the equilibrium constant calculated in (a) corresponds to [oxaloacetate][NADH] Keq [L-malate][NAD*] The measured concentration of L-malate in rat liver mitochondria is about 0.20 mM when [NAD*]/[NADH] is 10. Calculate the concentration of oxaloacetate at pH 7 in these mitochondria. (c) To appreciate the magnitude of the mitochondrial oxaloacetate concentration, calculate the number of oxaloacetate molecules in a single rat liver mitochondrion. Assume the mitochondrion is a sphere of diameter 2.0 microns.[AktivGrid] Draw the product of the reaction of isocitrate catalyzed by isocitrate dehydrogenase in the TCA (citric acid) cycle. Provide the structure in the protonation state found in physiological conditions. rxn' F-C-H NAD+ isocitra te dehydro genase NADH, Dra H+, > Problem 5 of 12 Submit H Atoms, Bonds and Rings OH Charges CH2OH Drag To Pan CH2OH- H OH Undo Reset ―CH2OH- Remove Done ⚫SH CHO +
- 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?Do a bit or research on the structure one of these enzymes. (include one recent reference) – How detailed is the enzyme structure known? What insight(s) does this structural detail give you about the enzyme mechanism.Given what you know about the involvement of nicotinamide nucleotides inoxidative and reductive metabolic reactions, predict whether the followingintracellular concentration ratios should be 1, > 1, or < 1. Explain youranswers.(a) [NAD+] >[NADH](b) [NADP+] >[NADPH](c) Since NAD+ and NADP+ are essentially equivalent in their tendency to attract electrons, discuss how the two concentration ratios might bemaintained inside cells at greatly differing values.Oxidation-reduction reactionn a biochemical pathway, three ATP molecules are hydrolyzed. The endergonic reactions in the pathway require a total of 17.3 kcal/mole of energy to drive the reactions of the pathway. What is the overall change in free energy of the biochemical pathway? Is the overall pathway endergonic or exergonic?s can involve a wide variety of molecules. Why are those involving hydrogen and oxygen of paramount importance in biological systems
- T The oxidation of malate by NAD to form oxaloacetate is a highly endergonic reaction under standard conditions. AG° = +29 kJ mol¯¹ (+7 kcal mol¯¹) Malate + NAD+ = oxaloacetate + NADH + H+ The reaction proceeds readily under physiological conditions. Why does the reaction proceed readily as written under physiological conditions? Endergonic reactions such as this occur spontaneously without the input of free energy. The steady-state concentrations of the products are low compared with those of the substrates. The reaction is pushed forward by the energetically favorable oxidation of fumarate to malate. O The NADH produced during glycolysis drives the reaction in the direction of malate oxidation. Assuming an [NAD* ]/[NADH] ratio of 8, a temperature of 25°C, and a pH of 7, what is the lowest [malate]/[oxaloacetate] ratio at which oxaloacetate can be formed from malate? [malate] [oxaloacetate] =Citrate synthase catalyzes the reaction Oxaloacetate + acetyl-CoA →citrate + HS-CoA The standard free energy change for the reaction is −31.5 kJ · mol−1. (a) Calculate the equilibrium constant for this reaction at 37°C. (b) Would you expect this reaction to serve as a control point for its pathway (the citric acid cycle)?Propose structures for intermediates A and B in the scheme below. This three-step conversion is carried out by enzymes that require no redox cofactors (no FAD, NADH etc.) nor TPP. Which enzyme in the citric acid cycle has an activity most similar to enzyme 1? Which enzyme in the PPP or the citric acid cycle has an intermediate that bears similarity to intermediate B? H OH COO™ Enzl A Enz2 B Enz3 OH
- [AktivGrid] Draw the product of the reaction of isocitrate catalyzed by isocitrate dehydrogenase in the TCA (citric acid) cycle. Provide the structure in the protonation state found in physiological conditions. 9 H-C-OH 800- -H CH₂ ° Coo of NAD+ dehydrogen isocitrate ase NADH, H*, Drawing CO2ATP Synthase is known to catalyze the synthesis of ATP with a ΔG°’ close to zero, and a Keq' close to. Why is the value of ΔG°’ different from the known value which is 30.5 kJ/mol (the energy for the reverse of ATP hydrolysis)? If the Keq' value is close to one, how is it ensured that the reaction is driven to the product side and more ATP is obtained?Coupling ATP hydrolysis to glucose phosphorylation makes thermodynamic sense, but consider how the coupling might take place. Given that coupling requires a common intermediate, one conceivable mechanism is to use ATP hydrolysis to raise the intracellular concentration of P,. The increase in P, concentration would drive the unfavorable phosphorylation of glucose by P. Is increasing the P concentration a reasonable way to couple ATP hydrolysis and glucose phosphorylation? No. The phosphate salts of divalent cations would be present in excess and precipitate out. Yes. The extra ATP hydrolysis would provide enough free energy to drive the phosphorylation reaction. Yes. Increasing the concentration of P, would decrease K'e and shift equilibrium to the right. No. The extra P, would give a negative AG, but would give a positive AG. In hepatocytes, the enzyme glucokinase catalyzes the ATP-coupled phosphorylation of glucose. Glucokinase binds both ATP and glucose, forming a glucose-ATP-enzyme…