Draw the major product of this reaction. Ignore any inorganic byproducts
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- АТР, СОASH ADP, P ОН О COA "OOC the task is to DRAW a reasonable mechanism for reaction listed. Not all products or cofactors may be shown, add them as necessary. Disregard stereochemistry2) braw the product of each quelegoh'/re subrtifu fion reaction. hadicate the mechonism of coch reaction (SN/ or dr ?). 6) No CNAerobic degradation of an organic compound by mixed cultureof organism in wastewater can be represented by following reaction. C3H6O3 + a O2 + b NH3 → c C5H7NO2 + d H2o + e CO2 A. Determine a, b, c, d and e, if YX/S = 0.4 d X/g S. B. Determine the yield coefficients YX/O2 and YX/NH3. C. Determine the degree of reductions for the substrate, bacteria and RQ for the organisms
- An enzymatic reaction follows M-M kinetics with Vmax= 2.5 mol m-3s-1and Km = 5 mM.Calculate the time required for 50% conversion of the substrate in a batch reactor if theinitial substrate concentration is0.2 M.Show your calculation steps.0he rate of a reaction increases as wbich of the following Decreases! A Temperature BTemperatre and concentrationof reactant lconcentration of reactant Dparticle size8 7- 6- 2- 1- 45 90 135 180 225 270 315 360 405 450 495 540 58! [Substrate] (nM) What is the Vmax of the enzyme data shown above? rate (nM/sec) 3.
- ver is given. A +B C+ D 1) Calculate AG for the above react un and indicáte whether the reaction is favorable or unfavorable [A] = 0.9 M 20°C AG° = 4 KJ/mol %3D [B] = 15mM [C] = 4mM [D] = 3 M R= 8.314 J/moleK %3D %3D 4.7 and explain how you know.perity zobsened rotaton Specifil rototonof P.E •Opical 12.9.(40) F6.19 4. A 0.002- mole sample of 2- bromo-2- methylpropane is added to 500.0 mL of water and the mixture is stirred till the pH levels off. 100 (a) What is the molar conc. of the substrate at beginning of the reaction? 0.002 .004m (b) What is the molar conc. of the substrate at the end of the reaction? all substratel wrill be Consemedo (c) What is the molar conc. of [H ] at the end of the reaction? O04 HBr-sHt t Br^ . 002mle C HJ=-002 O.0024c give the product if the reaction will occur, write no reaction if none
- 4. 5. 1015MSC Chemistry of Biological Systems II How are the structures of the various COX enzymes different? Explain what you understand by the term active site. trivz daidenoiselen3.An enzyme catalyzed reaction is studied and the following kinetic analysis is obtained: |[S), mM 0.050 0.075 v, (µM min") 0.93 1.264 1.77 2.14 3.7 0.125 0.175 0.935 a. Using Excel, make a fully labeled Lineweaver-Burk plot and determine the Km and Vmax for the enzyme b. The reactions were set up dissolving 1 mg of the enzyme (MW= 100000 Da) in 100 ml of final reaction buffer. Determine the turnover number for the enzyme assuming 1 active site exists per enzyme molecule? c. Determine the catalytic efficiency for the enzyme d. The same reactions are performed in presence of an inhibitor A and the resulting velocities determined: v plus inhibitor, (µM min) 0.272 0.37 0.518 0.626 |1.08 |[S), mM 0.050 0.075 0.125 0.175 0.935 Plot these data on the same graph as above and determine the new Km and Vmax and the type of inhibitor (competitive, non-competitive). e. Can the effects of the inhibitor be over-ridden by adding more substrate? Why?24. Determine equilibrium constants for the hydrolysis of phosphoenolpyruvate (AG" is 61.9 kJ/mol) at pH 7 and 25°C: nariw (d)