2. Threonine beta-epimerase is a pyridoxyl phosphate-dependent enzyme that catalyzes the reaction below. Provide a mechanism for the PLP-enzyme catalyzed reaction; you need to show the mechanism for the formation of the aldimine and the mechanism for the hydrolysis step that regenerates PLP. -20 PO OH NH₂3 Threonine beta-epimerase PLP OH co NH₂ H OH Pyridoxyl phosphate (PLP)
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- GTP or ATP is produced during the conversion of isocitrate into ketoglutarate succinyl CoA into succinate fumarate into malate malate into oxaloacetateEnergetic of Fructose-1 ,6-bis P Hydrolysis (Integrates with Chapter 3.) The standard free energy change (G) for hydrolysis of fructose-1. 6-bisphosphate (FBP) to fructose-S-phosphate (F-6-P) and P: is -16.7 KJ/mol: FBP + H2O fructose-6-P + Pi The standard free energy change (G) for ATP hydrolysis is -30.5 KJ/mol: ATP + H2O ADP + Pj What is the standard free energy change for the phosphofructokinase reaction: ATP + fructose-6-P ADP + FBP b. What is the equilibrium constant for this reaction? c. Assuming the intracellular concentrations of [ATP] and (ADP] are maintained constant at 4 mM and 1.6 mM, respectively, in a rat liver cell, what will be the ratio of [FBP]/[fructose-6-P] when the phosphofructokinase reaction reaches equilibrium?Understanding the Mechanisms of Reactions Related to Transketolase The mechanistic chemistry of the acetolactate synthase and phosphoketolase reactions (shown here) is similar to that of the transketolase reaction (Figure 22.30). Write suitable mechanisms for these reactions.
- 10. Chymotrypsin is a serine protease enzyme. The Km for the reaction of chymotrypsin with N-acetylvaline ethyl ester is 8.8*102, and the Km for the reaction of chymotrypsin with N- acetyltyrosine ethyl ester is 6.6*10“ M. catalytic triad Ser 195 His 57 Gly 193 N-H OH R-N- Ca N-H O-C- Asp 102 N-acetyl valine N-acetyl tyrosine Chymotrypsin Active Site a. What is the nucleophile here and how is it activated? b. Which substrate has an apparent higher affinity for the enzyme. c. Propose a reason for the difference in affinity based on the shape of each of the substrates (see active site figure, cleaves on the C-side of aromatic residues).17. Omeprazole is a bioprecursor prodrug that is activated by protonation to give active metabolite that inhibits H¨,K*-ATPase covalently. By using chemical equations show activation of Omeprazole and its reaction to inhibit the H*,K*-ATPase. CH3 H3CO. s=0 H3C HNN Omeprazole OCH3 18. The following compound is an open-chain prodrug of benzodiazepines which undergo N- dealkylation to triazolam. Using chemical equations show transformation of this prodrug to triazolam. H3C H3C CH3 CH3 triazolam open-chain prodrug of triazolam33. 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
- 38. The shown reaction is one of the four repeating steps during fatty acid biosynthesis. Which of the following statements is correct? 유 CH3-C-CH₂-C-S-ACP A B OH 유 CH3-C-CH₂-C-5-ACP → A. The small molecule in box A is NADPH + H* B. It is the second reduction reaction during fatty acid biosynthesis C. Both A and B D. Neither A nor BShown below is a substrate for a Trypsin. Draw the mechanism for this serine protease using the artificial substrate. Be sure to draw the catalytic triad, and show the role of the oxyanion hole. Draw the complete structure of every intermediate and product and PUSH ARROWS!!!!! Do not abbreviate structures using R and R' H₂N _N_CH. сно CH₂ CH₂ CH₂ NH d=19H₂ NH₂ O CH- H₂C HN O CH3. b. If chymotrypsin is treated with disopropylfluorophosphate, catalysis cannot occur even in the presence of excess substrate concentration. Is this Inhibltion reversible or Irreversible?. Dilsopropylfluorophosphate Hyd
- 1. A gluscose trasporter in teh liver cell binds with Km of 40mM. Calculate what fraction of vmax the Vo operating when blood glucose is 10mM 2. Draw a Michaelis-Menten kinetic curve and identify Vmax and Km. Indicate on the curve where the reaction is first order, where the reaction is zero order, where the reaction operates at half-saturation, and the range where most enzymes operate Be very clear about your labels.15. Write the metabolites of the following substrates due to phase Il reactions: a. b, R R C. R R NH ΝΗ LOH 3'-phosphoadenosine-5'-phosphosulfate Enzyme S-adenosylmethionine Enzyme Acetyl-SCOA16. 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?
