Glucolate is oxidized into Glvoxylate by cytechrome C using the glycolate oxidase enzyme. The two half- reactions are shown below in their standard reduction forms. но +2 H* (aq) + 2 e Glyoxylate Glycolate
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- 1. (a) write, using structural formulas, the sequence of TCA cycle intermediates. Indicate the position of the 14C atom in each intermediate. Do not name enzymes or cofactors catalyzing the reactions. Starting with citrate formed immediately after reaction of [2-14C]acetyl-SCOA with OAA,1) Which of the following redox reactions would be expected to proceed as written? (Assume standard conditions; E°’ values are shown above.) A. Malate + NAD+ ® Oxaloacetate + NADH + H+ B. Acetoacetate + NADH + H+ ® b-hydorxybutyrate + NAD+ C. Pyruvate + b-hydorxybutyrate ® Lactate + Acetoacetate D. Malate + Pyruvate ® Oxaloacetate + Lactate E. Acetaldehyde + Succinate ® Ethanol + Fumarate Half Reaction E°’ (V) Fumarate + 2 H+ + 2 e- ® Succinate 0.031 Oxaloacetate + 2 H+ + 2 e- ® Malate -0.166 Pyruvate + 2 H+ + 2 e- ® Lactate -0.185 Acetaldehyde + 2 H+ + 2 e- ® Ethanol -0.197 NAD+ + H+ + 2 e- ® NADH -0.320 Acetoacetate + 2 H+ + 2 e- ® b-hydorxybutyrate -0.346 2) Calculate the DE° for the reaction shown in option A question 1.33. Which of the following statements is true for the shown reaction? P-O-CH₂ P-O-CH₂ OH A Coo I C=O HOTHS CH₂ Coo A HỌ он D A. The reaction is catalyzed by PFK-1 B. Stimulation of the reaction eventually slows down gluconeogenesis C. Inhibition of glyceraldehyde 3-phopshate dehydrogenase leads to the accumulation of the product B D. All of the above E. None of the above OH 34. Which of the following statements is true for the shown reaction? COO™ CH₂OH HQ -℗ B CH₂ B C-o-℗ + CO₂ A. Insulin can eventually inhibit the reaction B. The reaction only take place in the presence of acetyl-CoA C. The product B is a high-energy molecule, and the next logical step is to use the energy released from B to synthesize ATP D. All of above E. None of the above
- 16. The overall reaction for the glycolysis reaction is C6H₁2O6(aq) + 2NAD+ (aq) + 2ADP³(aq) + 2HPO(aq) + 2H₂O(1) 2CH3COCO₂ (aq) + 2NADH(aq) + 2ATP4 (aq) + 2H3O+ (aq). What is A,G at chemical equilibrium?There are parts A-C for this picture included. A) What type of enzyme is Malate Dehydrogenase? choices: Hydrolase, Isomerase, Ligase, Oxideoreductase, Transferase, or Translocase B) Which of the following statements are true in biochemical standard conditions? There can be more than 1. Choices: The reaction is spontaneous since ∆G°' is positive The reaction is spontaneous since ∆G°' is negative The reaction is not spontaneous since ∆G°' is positive The reaction is not spontaneous since ∆G°' is positive The equilibrium favors products since K is greater than 1 The equilibrium favors reactants since K is greater than 1 The equilibrium favors products since K is less than 1 The equilibrium favors reactants since K is less than 1 The reaction is always at equilibrium C) If the concentration of Oxaloacetate is 10^7 times lower than the concentration of Malate D.,Is the reaction Spontanuous? Choices: No, because RTInQ is very positive Yes, because RTlnQ is very…2. a) Outline the general mechanism of a coenzyme B12-dependent enzyme which catalyzes the following reaction. HO H R-C-C-H ĤIÓN - H₂O HIC-H R-C-C O= H b) When R is CH3, what would the name of the enzyme be, and what would be the full EC number? Justify the first number of the EC number.
- 3. The succinate dehydrogenase reaction in the direction it proceeds within the CAC is shown below (left to right): FAD FADH, H-C-H H-C-H coo- succinate dehydrogenase Succinate Fumarate AG" - O kl/mol a) Calculate the standard reduction potential for the overall reaction above. b) Based on the reduction potential, calculate and compare your standard transformed free energy change to the textbook value (above), and venture to explain any discrepancies. c) Assuming the temperature of the cell is 37 °C, calculate the equilibrium ratio of oxidized to reduced cofactor when the ratio of oxidized product to reduced substrate is 1.2. .22) answer the following question.. Refer to the kinetic scheme for competitive inhibition and the structures shown below to E+S ES E +P -co- CO- 1 2 EI Compound 1 was determined to act as a competitive inhibitor through standard inhibition studies. Structural studies did not show any resemblance to the transition state. Compound 2 was also determined to act as a competitive inhibitor. Structural studies showed that it does resemble the transition-state. The K, constant is used to assess relative affinity of inhibitors for enzymes. That is, each compound has its own K, value. We can interpret K, the same way we do with Ka values. True or False: K, > Kµ2. Briefly explain your answer.Beginning with the 1st tetrahedral intermediate, show the complete steps in chymotrypsin mechanism that occurs to form the 2nd chymotrypsin intermediate in the chymotrypsin active site. The substrate for chymotrypsin to be used is Ala-Tyr-Gly. Further, name the amino acid(s) that would be released as a result of the reactions you'd illustrated above.
- When grown anaerobically on glucose, yeast (S. cerevisiae) converts pyruvate to acetaldehyde, then reduces acetaldehyde to Pethanol using electrons from NADH. Write the chemical equation for the reaction that reduces acetaldehyde (CH3CHO) to ethanol (CH3CH2OH). The table provides the standard reduction potential, E', of the relevant half-reactions. Half-reaction Acetaldehyde + 2 H+ + 2e¯ → ethanol NAD+ + 2H+ + 2e¯ → NADH + H+ E'° (V) -.197 -.320 Calculate the equilibrium constant, K'eq, at 25.0 °C for the reaction that reduces acetaldehyde to ethanol. K'e ×10 = eq(i) During the Pyruvate Decarboxylase (PDC) catalysed reaction, a covalent coenzyme intermediate is formed. On the skeleton of the covalent coenzyme intermediate below draw the appropriate double bonds, charges, and electron pairs to illustrate the two resonance forms of this intermediate. Name each form in the boxes provided. HO S R' N -R HO S R' N -R5) In an experiment to investigate the inhibition of the enzyme-glucosidase the following data for the rates of reaction with glucopyranoside for various substrate concentrations was obtained. By constructing a Leaver-Burk plot, determine the value of the Michaelis constant. [S]/ (10-6 mol dm-3) v/ (10-3 mol dm-3 s-1) 1.00 2.00 3.00 4.00 16.7 33.3 41.1 49.8