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
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Enzyme 1 is Aconitase and the starting material goes through both the hydration and dehydration mechanism.
I just need help with enzyme 2 and intermediate B, thank you
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- Some bacteria use the citric acid cycle intermediate, a-ketoglutarate, plus acetyl-CoA, as the starting point for lysine biosynthesis. The first part of this biosynthetic pathway uses the same chemical strategy found in the citric acid cycle. Propose a four-step pathway for the conversion of a-ketoglutarate to 2-oxoadipate. Draw the three missing intermediates, and indicate the chemistry involved in each reaction. Include any cofactors that you think might be required for specific steps.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 OHConsider 3 molecules of galactose: (write only the whole number; no decimal places) How many turns of Krebs Cycle will these molecules undergo for complete oxidation? b. How many moles of ATP are produced upon complete oxidation via malate-aspartate shuttle? c. If all the galactose molecules oxidize via pentose phosphate pathway (oxidative stage only), how many moles of NADPH will be produced?
- 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.Consider one of the reactions of the citric acid cycle shown below Malate + NAD+ ⇆ Oxaloacetate + NADH + H+ (malate dehydrogenase) ΔG˚′ = +29.7 kJ/mol. Describe two factors that allow this thermodynamically unfavorable reaction to occur in the direction of malate to oxaloacetate.(a) Consider the oxidation of malate to oxaloacetate by NAD*: malate + NAD+ → oxaloacetate + NADH + H+ In yeast mitochondria, where the pH = 8.1, this reaction is exergonic only at low oxaloacetate concentrations. Assuming a pH = 8.1, a temperature of 37 °C, and the steady-state concentrations given below, calculate the maximum concentration of oxaloacetate at which the reaction will still be exergonic. malate + NAD*→ oxaloacetate + NADH + H* lactate + NAD →→ pyruvate + NADH + H+ half reaction Pyruvate + 2H+ + 2e → lactate Pyruvate + CO₂ + H + 2e → malate Intracellular steady state concentrations: malate = 410 μM; NAD = 20.0 mM; pyruvate = 3.22 mM; NADH = 290 μM; AG=+29.7 kJ/mol AG¹ = +25.1 kJ/mol E° (V) - 0.190 - 0.330 lactate 1.1 mM CO₂ = 15.5 torr
- Consider the mechanism of the aldolase reaction given in figure 9.25. In chapter 12, we saw that the same enzyme was used to catalyze the reverse reaction, DHAP + glyceraldehyde-3-phosphatefructose-1,6-bisphosphate, in the first step of stage 3 in the Calvin Cycle. Using arrows and structures similar to what is shown in 9.25, propose a mechanism for this reverse reaction (which is an aldol condensationCertain microorganisms with a modified citric acid cycle decarboxylate a-ketoglutarate to produce succinate semialdehyde: (a) Succinate semialdehyde is then converted to succinate, which is furthermetabolized by standard citric acid cycle enzymes. What kind of reactionis required to convert succinate semialdehyde to succinate? Showany coenzymes that might be involved.(b) Based on your answer in part a, how does this pathway compare to thestandard citric acid cycle in energy yield?Consider the malate dehydrogenase reaction from the citric acid cycle. Given the listed concentrations, calculate the free energy change for this reaction at energy change for this reaction at 37.0 ˚C (310 K). AG' for the reaction is +29.7 kJ/mol. Assume that the reaction occurs at pH 7. [malate] = 1.45 mM AG: [oxaloacetate] = 0.130 mM [NAD+ ] = 110 mM [NADH] = 44 mM 47.06 Incorrect kJ.mol-1
- Consider the malate dehydrogenase reaction from the citric acid cycle. Given the listed concentrations, calculate the free energy change for this reaction at energy change for this reaction at 37.0 °C (310 K). AG' for the reaction is +29.7 kJ/mol. Assume that the reaction occurs at pH 7. [malate] = 1.43 mM [oxaloacetate] = 0.220 mM [NAD*] = 460 mM [NADH] = 180 mM AG : kJ-mol-1Consider the malate dehydrogenase reaction from the citric acid cycle. Given the listed concentrations, calculate the free energy change for this reaction at energy change for this reaction at 37.0 °C (310 K). AG' for the reaction is +29.7 kJ/mol. Assume that the reaction occurs at pH 7. [malate] 1.25 mM [oxaloacetate] = 0.290 mM [NAD+] = 430 mM [NADH] : = 170 mM AG : kJ-mol-1 * TOOLS x10Certain microorganisms with an incomplete citric acid cycle decarboxylate α-ketoglutarate to produce succinate semialdehyde. A dehydrogenase then converts succinate semialdehyde to succinate. These reactions can be combined with other standard citric acid cycle reactions to create a pathway from citrate to oxaloacetate. Compare the ATP and reduced cofactor yield of the standard and alternate pathways.