For each of the (unbalanced) reactions shown below, indicate whether the reactant is being oxidized or reduced. For each reaction identify whether it is ar anabolic or catabolic process. Show how the cofactors NAD*, NADP*, NADH on NADPH are involved in the process. a) Glutamate synthesis from a-ketoglutarate diverted from the citric acid суcle. CO2 CH2 CH2 CO2 CH2 CH2 H-NH, H20 + NH4 Čo, CO2 b) A step in the pathway for fatty acid degradation. SCOA SCOA c) A step in the conversion of Propionyl-CoA into Acetyl-CoA. CO2 CO2 O=C HO-CH + CO2 CH2 CH3
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- In Bacillus subtilis, threonine is metabolized by the following sequence of reactions: (a) oxidation; (b) decarboxylation;(c) transamination; and (d) oxidation to produce pyruvate. Outline this sequence of steps, show the structures of thesubstances, use abbreviations for the cofactors, and show any enzyme-bound coenzymes. What type of enzyme bound intermediate is likely for reaction (d)?The immediate precursor to acetyl–CoA from glycolysis is pyruvate.a) Write the pathway (not the mechanism) for the series of steps for this conversion. Includestructures for all coenzymes and reactants for each step.b) Discuss the mechanistic advantages offered by this multienzyme complex. Be specific and giveexamples.c) The last step of the reaction, catalyzed by enzyme 3, includes three coenzymes and oxidation.Write the mechanism for this enzyme.Refer to Figure, which indicates ∆G for each glycolytic reaction under intracellular conditions. Assume that glyceraldehyde-3-phosphate dehydrogenase was inhibited with iodoacetate, which reacts with its active site cysteine sulfhydryl group. Which glycolytic intermediate would you expect to accumulate most rapidly, and why?
- Order the cofactors based on their use in the mechanism of the a-ketogluterate dehydrogenase complex. 1. Stabilizes a carbanion due to decarboxylation 2. Allows for the splitting of the carbon skeleton from the electron pair generated in a redox reaction 3. Enzyme bond electron carrier that is part of dihydrolipoyl dehydrogenase 4. Final electron acceptor in the overall reaction catalyzed by this complex 1 (Choose ] [Choose ] FAD Lipoamide 2 Fe 2S cluster TPP Biotin 3. NAD+ 4 [Choose ] 2.The krebs cycle has 8 enzymes: citrate synthase, aconitase, isocitrate dehyrogenase, a-ketoglutarate dehydrogenase, succinyl –CoA synthease, succinate dehyrogenase, fumarase and malate dehyrogenase. a)Write name the cofactors required by each enzyme reaction. b)For each enzyme determine which of the following deascribes the type of reactions catalyzed: condensation (Carbon-carbon bond formation), dehydration (Loss of water), hydration (addition of water), decarboxylation (loss of CO2), oxidation-reduction; subsrate level phospohorylation; isomerization.Which of the following statements is true about the chymotrypsin reaction? 1. The catalytic triad at the active site is formed by three residues: His, Gly, and Ser 2. When the substrate is p-Nitrophenylacetate, the rate-limiting step is the release of p-Nitrophenolate. 3. During the reaction, LBHB forms when the proton is donated to His from Ser or water. 4. The chymotrypsin reaction involves “only” specific acid-base catalysis 5. The “oxyanion hole” is formed by the amide nitrogens of Ser and Glu
- Below is an image of the Krebs cycle: acetyl-CoA oxaloacetate COASH H20 NADH NAD* H20 malate citrate fumarate isocitrate FADH2 NAD* CO2 FAD АТР NADH + ADP succinate GTP NAD+ a-ketoglutarate H20 GDP NADH + CO2 COASH succinyl CoA COASH Consider the conversion of succinate to fumarate, which is coupled with the production the electron carrier FADH2. If this reaction was NOT coupled with the production of FADH2 (and only catalyzed the conversion of succinate to fumarate), how would this impact ATP production through cell respiration? OATP production would stop because no high energy electron carriers would be produced ATP production would still occur, but there would be a much lower ATP yield because a large number of electron carriers are no longer being made ATP production would stop because without FADH2 we will no longer have electrons moving through the electron transport chain ATP production would still occur, but there would be a slightly lower ATP yield because a small number of…Indicate whether each of the following changes represents oxidation or reduction. Write: O = for oxidation ; R= for reduction Example: cyt ci (Fet) → cyt c1 (Fe2+) Answer: R Blank #1: COQH2 → CoQ Blank #2: NAD+ - NADH Blank #3: FMN → FMNH2 Blank # 4: FADH2 FAD Blank #5: Fe(III) SP → Fe(II) SP Blank # 1 Blank # 2Order the cofactors based on their use in the mechanism of the a-etogluterate dehydrogenase complex. 1. Stabilizes a carbanion due to decarboxylation 2. Allows for the splitting of the carbon skeleton from the electron pair generated in a redox reaction 3. Enzyme bond electron carrier that is part of dihydrolipoyl dehydrogenase 4. Final electron acceptor in the overall reaction catalyzed by this complex 1 2 3 4 answer choices: lipoamide, biotin, 2 Fe - 2S cluster, TPP, NAD+, FAD
- Why does biological Fe2+ oxidation under oxic conditions occurmainly at acidic pH?One process catalyzed by NADHNADH dehydrogenase is NADH+H^++ubiquinone ↽−−⇀ NAD+ubiquinolNADH+H^++ubiquinone ↽−−⇀ NAD^++ubiquinol The standard reduction potentials for the half‑reactions are given in the table. Oxidant Reductant ?′0 ubiquinone+2H++2e−ubiquinone+2H++2e^− ubiquinolubiquinol 0.045 NAD^++H^++2e−NAD^++H^++2e^− NADHNADH –0.32 Calculate Δ?′0 for the reaction as shown. Δ?′0=____(V) Calculate Δ?′0 . Δ?′0=____(kJ/mol)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.