5. Consider the decarboxylation of dimethyloxaloacetate 7 to 3-methyl-2-oxobutyrate 8 shown below H3CO cat. Cu²+ & CO2 CH3OH (aq) cat. Cu²+ no reaction CH3OH (aq) 9 a. Provide a mechanism to account for the fact that Cu2+ catalyzes this reaction. b. In one sentence explain why Cu2+ does not similarly catalyze the decarboxylation of 9.
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- 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 above16. 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?10. Procaine is known to undergo faster metabolic hydrolysis than procainamide. Give explanation. -NET2 -NEt2 HN H2N- H2N- Procainamide Procaine 11. In phase 2 metabolic transformation chloramphenicol the primary alcohol is converted to a glucuronide conjugate. Draw chemical structure of the product. Provide the name of enzyme that catalyze this metabolic reaction. он ? CHCI2 O2N- но
- 9. For the following aspartate reaction in the presence of inhibitor, Km = 0.00065 M. Determine Vmax in both reactions and in the reaction without inhibitor, the Km. Identify whether the inhibition is competitive, non-competitive or uncompetitive. 110 100 1/V 70 60- 40- 30- 20- 10- 10. For your answer in #9, explain briefly: a. 1. how / and S bind to the E as shown by the Lineweaver Burk plot. b. the significance of the following obtained values for Km and Vmax. c. effect in slope and x-intercept F000 F0000 Fo008 F0009 F000 Fo00make a schematic diagram of BChE/AChE inhibitory determination Butyrylthiocholine iodide (BChI), as well as acetylthiocholine iodide(AChI) molecules were utilized as substrate compounds of the reaction. Inthis regard, 5,5′‐dithio‐bis(2‐nitro‐benzoic acid) compound (DTNB) wasused to estimate BChE/AChE activity. In summary, 100 μL Tris buffersolution (HCl, 1.0M, pH 8.0, Tris) and variety of concentrations of thesample solution (50‐200 mL) were added in deionized water and also20 μL of BChE/AChE enzymes solutions added. The mixture was thenincubated for 10 minutes at 20°C. Finally, 50 μL of DTNB (0.5 mM and25 mL) BChI/AChI were added to the incubator mixture. The reactionwas also started by adding 50 μL BChI/AChI. The activity of theseenzymes was evaluated using spectrophotometric spectra with awavelength of 412 nm.5.1
- Given the following choices,a. what is the structure of the product of the reaction catalysed by ACAT?b. structure of the product produced from the reaction catalysed by phospolipase A2?c. general structure of TAGd. structure of glycerolIn humans, the biosynthesis of L-glutamine is catalyzed by the L-glutamine synthetase. The global reaction can be written as follows: ATP + glutamate + NH3 ADP + phosphate + glutamine The A,Gº' value for this reaction is -16.3 kJ.mol-1 (from left to right). 1- Explain the significance this information. 2- This reaction can be considered as the sum of two component reactions which are exergonic and endergonic, respectively, under standard conditions. Write these two component reactions and evaluate A,Gº of the endergonic reaction. Data: A,Gº of ATP hydrolysis = -30.4 kJ mol-¹Draw a stepwise mechanism for conversion of radical intermediate A to prostaglandin PGG2.
- H. OH co co2 но H co, 1-isopropylmalate 2-isopropylmalate Biosynthesis of leucine involves conversion of 1-isopropyimalate to 2-isopropylmalate (see above). This proceeds in four steps under basic enzymic catalysis via an isolable compound produced in step 2. Write a detailed mechanism for this conversion. Then, draw the intermediate compound) produced in step 2. • You do not have to consider stereochemistry. • Draw uninvolved carboxyl groups in the anionic state, and enolates as carbanions. When needed, abbreviate CoenzymeA-S- as CH3S- In your drawing. aale1. Please fully explain (use illustrate where appropriate) the Modes of Enzyme Catalysis exemplified by the serine protease: Chymotrypsin. In your answer discuss employing the illustration whenever possible: the overall reaction mechanism, stability of the reaction transition state, proximity and orientation effects, acid-base catalysis, and covalent catalysis. (c) (0) Ap Asp Toe His Asp 10 C-N bond cleavage HN Ho Ser Ger Binding of substi 196 Ser Gly alto video LBHB NH Sere HAR Proton donation by H (h) Fel of amino product yest OHN Hig Ser Ap (0) Formation of covalent (ES) Alp Me complex Serios3. Subtilisin (Mol. weight 27,600) is a protease that can catalyze hydrolysis of certain amino acid esters and amides. For the synthetic substrate N-acetyl-L-tyrosine ethyl ester (Ac-Try-OEt), subtilisn exhibits Km and kcat values of 0.15 M and 550 s-¹, respectively. a) What is the Vmax when the subtilisin concentration is 0.4 mg/ml? b) Indole is a competitive inhibitor of subtilisin with a Ki of 0.05 M. What is the Vmax for Ac-Try-OEt hydrolysis by 0.4 mg/ml subtilisin in the presence of 6.25 mM indole? c) What is the Vo when 0.4 mg/ml subtilisin is incubated with 0.25 M Ac-Try-OEt and 1.0 M indole?