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- Distinguishing the Mechanisms of Class I and Class I Aldolases Fructose bisphosphate aldolase in animal muscle is a class 1 aldolase, which forms a Schiff base intermediate between substrate (for example. fructose-1, 6-bisphosphate or dihydroxyacetone phosphate) and a lysine at the active site (see Figure I8.12). The chemical evidence for this intermediate conies from studies with aldolase and the reducing agent sodium borohydride, NaBH4. Incubation of the enzyme with dihydroxyacetone phosphate and NaBH4 inactivates the enzyme. Interestingly, no inactivation is observed if NabH4 is added to the enzyme in the absence of substrate. Write a mechanism that explains these observations and provides evidence for the formation of a Schiff base intermediate in the aldolase reaction.6. Malate dehydrogenase catalyzes the following reversible reaction: COO- HO-C-H CH₂ COO™ L-Malate NAD+ y malate NADH + H+ dehydrogenase COO- 0=C CH₂ COO™ Oxaloacetate AG'° = 29.7 kJ/mol Malate + NAD+→NADH + H+ + oxaloacetate Calculate AG" and the ratio or products and reactants for the malate dehydrogenase reaction to proceed from left to right as shown. (The Faraday constant. 3, is 96.48 kJ/V-mol; RT(37°C)= 2.58kJ/mol) Steps: 1. Explain how you determined which molecule is an electron donor Malate and which is an acceptor NAD*. -2- 2. Calculate AED (write equation, then show calculations, for standard reduction potentials (E_values) see table in the posted lecture) 3. Calculate AG (write equation, then show calculations) 4. Calculate the ratio of products and reactants needed to for Malate + NAD+→→NADH + H+ + oxaloacetate reaction to proceed forward (write equation, then show calculations)1. Identify the oxidized coenzyme (letter abbreviation only) that participates in this reaction of the Kreb’s cycle. Succinate --> Fumarate 2. How many mol of NADH can be obtained upon the beta oxidation of stearic acid? 3. How many mol of ATP can be obtained upon the complete oxidation of 1 mol stearic acid? 4. How many steps in glycolysis in which ATO is converted to ADP?
- From the complete oxidation of glucose (glucose → 6CO2), how many total NADH electron carriers are produced and how many total nucleotide triphosphates are yielded (be sure to deduct payback) as part of substrate level phosphorylation?(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 torrA dialyzed pigeon liver extract will catalyze the conversion of acetyl-CoAto palmitate and CoASH if supplied with Mg2+, NADPH, ATP, HCO3-, andcitrate.(a) If H14CO3– is supplied, what compounds will become labeled (permanently or transiently) during the course of the reaction? In whatcompounds will 14C accumulate?(b) Explain the role of citrate in this reaction.
- 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.For lactate dehydrogenase reaction if km for NADH is 2×10^-4 M . What concentration of it would be appropriate for determining Km for pyruvate?[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 CO2
- 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. Cyanide, oligomycin, and 2,4-dinitrophenol are all inhibitors of oxidative phosphorylation in mitochon- dria. Provide an explanation to the following conditions regarding these potent inhibitors. (a) Explain why adding cyanide to an active in vitro suspension of mitochondria blocks ATP synthesis. What happens to the rate of ATP synthesis when 2,4-dinitrophenol is added to this mitochon- drial suspension after it was treated with cyanide? (b) Explain why the rate of oxygen consumption decreases in an in vitro suspension of mito- chondria when oligomycin is added. What happens to the rate of oxygen consumption in this oligomycin- inhibited system after adding 2,4-dinitrophenol? Explain.Imagine a triglyceride comprised of (3) saturated C12 fatty acids. Calculate the number of ATP generated from the complete oxidation of one of these 12-carbon fatty acids to CO2 and water in the liver. Assume that each NADH = 2.5 ATP and each FADH2 = ETC generates 1.5 ATP. Any step that yields pyrophosphate as a product should be treated as an input (i.e. net loss) of (2) ATP.