16. The overall reaction for the glycolysis reaction is C6H₁2O6(aq) + 2NAD+ (aq) + 2ADP³- (aq) + 2HPO(aq) + 2H₂O(1) = 2CH3COCO₂ (aq) + 2NADH(aq) + 2ATP (aq) + 2H3O+ (aq). What is A,G at chemical equilibrium?
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- 5) 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 49.8The Keq (25C) of the reaction below is 635.67. Fructose 1,6-biphosphate <-->fructose -6-phosphate + Pi. a) What is the standard Gibbs free energy change for this reaction? b) if the concentrationof fructose 1,6 biphosphate is adjusted to 0.85 M and that of fructose 6 phosphate and phosphate adjusted to 0.055 M, what is the actual free energy changeThe equilibrium constant for the hydrolysis of the peptide alanylglycine (Gly-Ala in the reaction from Part B) by a peptidase is K = 9.0 × 10² at 310 K. Calculate AG for this reaction. Express the Gibbs free energy to three significant figures. AG = Submit ΠΑΠΙ ΑΣΦ Request Answer ? kJ/mol Keq [Gly] [Ala] [Gly-Ala]
- . The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins of bacterial wall) are 37 C - temperature and pH is 5.2. Explain the decrease in this enzyme activity if the temperature will rise up to 60 °C and pH will be changed to 8.0. To answer the question: a) draw the graph of the velocity dependency on temperature and pH; b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes the formation of 5 uM of the product per 2 minutes. Concidor NH3: 5.The protein catalase catalyzes the reaction 2H,O,(aq) — 2H,O(l) + O,(g) and has a Michaelis-Menten constant of KM = 25 mM and a turnover number of 4.0 × 107 s¯¹. The total enzyme concentration is 0.010 µM and the initial substrate concentration is 4.83 µM. Catalase has a single active site. Calculate the value of Rmax (often written as Vmax) for this enzyme. Rmax Calculate the initial rate, R (often written as V), of this reaction. R = ×10 mM.s-1 mM-s-1Write out the balanced chemical equation for the FIRST round of oxidation of C16:cis-9.
- Write a balanced equation for cach of the following reactions or reaction sequences. (a) The reaction catalyzed by PFK-2 (b) The conversion of 2 moles of oxaloacetate to glucose (c) The conversion of glucose to UDP-Gle (d) The conversion of 2 moles of glycerol to glucose (e) The conversion of 2 moles of malate to glucose-6-phosphateIn the hexokinase reaction (in glycolysis) Keq caclualtion, what is the OBVIOUS problem with getting a Keq of 678? what should keq be normally? how can you EXPLAIN a Keq of 678?We want to measure the activity of alanine aminotransferase (ALAT) present in a serum. The reaction catalyzed by the enzyme is: Reaction 1: +H3N- glutamate H C CH₂ CH₂ COO -COO + pyruvate CH3 C=0 0.1 M phosphate buffer pH 7.4 : 550 µL 1.2 M alanine : 100 μL CH3 time (min) A340 COO COO™ pyruvate lactate dehydrogenase* (LDH, 300 µg.mL-¹): 50 μL 1.5 mM NADH: 200 μL 0.04 M a-ketoglutarate: 500 μL serum containing ALAT: 600 μL The enzyme reaction is realized in the following conditions: In a 1 cm-cuvette are added: 0 0.915 ALAT NADH + H+ LDH a-cétoglutarate COO * Lactate dehydrogenase (LDH) reduces pyruvate into lactate, with the concomitant oxydation of NADH. This allows to indirectly measure the amount of product formed. Reaction 2: NAD+ 1 0.741 C=O H CH₂ CH₂ COO™ CH3 C-OH COO lactate The reaction is performed at 25 °C and the absorbance at 340 nm is monitored every minute, for 5 min. The absorbance values are given in the table below: Data: alanine ENADH at 340 nm = 6220 M¹.cm1. One…
- Consider the following interconversion, which occurs in glycolysis :(a) What is ΔG′° for the reaction ( K'eq measured at 25 °C)?(b) If the concentration of fructose 6-phosphate is adjusted to 1.5 M and that of glucose 6-phosphate is adjusted to 0.50 M, what is ΔG?(c) Why are ΔG′° and ΔG different?The active site of an enzyme that uses a general acid-base catalytic mechanism contains a Glu and an Asp residue (both of which are essential for catalysis) with pKa values of 5.9 and 4.5, respectively. If the enzyme is found in the lysosome (pH = 5.2), which residue will act as the general acid and which will act as the general base during the initial steps of the reaction?Study is being done where protein A isomerase (AI) is being phosphorylated by AI phosphorylase (AIP), at 37oC at physiological pH of approximately 7.4 with excess of Mg2+ and ATP. The Vmax and Km are determined to be 9 mM s-1 and 15 uM, respectively a) does AIP need any coenzymes, cofactors, co-substrates? b) what would be the formula for initial rate as a function of AI concentration? (Michaelis-Menten equation) c) what are the intial rates of reaction when [AI] = 3, 6 and 40 uM? Is the trend in initial rate vs [substrate] surprising? Explain.