3. For an endergonic, what is the value of AG?
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- Calculate the standard free energy change (ΔG°′) for the following reaction: ½ O2 + FADH2 → H2O + FADThe following data were collected in the study of a new enzyme and an inhibitor of the new enzyme: Vo (nmol/sec) [S] (uM) 1.3 - Inhibitor + Inhibitor 2.50 0.62 2.6 4.00 1.42 6.5 6.30 2.65 13.0 7.60 3.12 26.0 9.00 3.58 What is the Km of the inhibited enzyme reaction?The following questions are based on the reaction A+ B ↔ C+D shown in Figure 8.1. 1. Which of the following terms best describes the progress of the reaction with respect to free energy change? a) endergonic, ∆G> 0 b) exergonic, ∆G> 0 c) exergonic, ∆G< 0 d) endergonic, ∆G< 0 2. Which of the following in Figure 8.1 remains unchanged by having an enzyme included? a) b b) d c) a d) c 3. The part labeled “C” on the above graph represents a) Energy of activation without enzyme b) Energy of activation with enzyme c) Amount of free energy released d) amount of energy required for the reaction progress
- The following data were collected in the study of a new enzyme and an inhibitor of the new enzyme: Vo (nmol/sec) - Inhibitor + Inhibitor 0.62 [S](HM) 1.3 2.50 2.6 4.00 1.42 6.5 6.30 2.65 13.0 7.60 3.12 26.0 9.00 3.58 What is the Vmax of the uninhibited enzyme reaction?For a particular reaction, AH° = −16.1 kJ/mol and AS° = −21.8 J/(mol·K). Assuming these values change very little with temperature, at what temperature does the reaction change from nonspontaneous to spontaneous in the forward direction? OT= Is the reaction in the forward direction spontaneous at temperatures greater than or less than the calculated temperature? less than greater than KThe primary source of phosphate for chemical reactions in cells comes as ATP, ADP, or AMP. The ΔG˚’ for the hydrolysis of ATP into ADP and Pi is -30.5 kJ/mol. Calculate the equilibrium constant for the hydrolysis of ATP.
- How many net molecules of nucleoside triphosphate (ATP and equivalent molecules) are produced by complete aerobic catabolism of a glucose going through glycolysis, the pyruvate dehydrogenase complex and the citric acid cycle (TCA cycle)? Do not count the ATP eventually generated by re-oxidation of reduced coenzymes, just the number of NTPs produced in reactions of these pathways. Choose the one best answer. 02 03 04 05 06 8Consider a general reaction enzyme A(aq) B(aq) The AGo of the reaction is -9.150 kJ mol-. Calculate the equilibrium constant for the reaction at 25 °C. Keg = What is AG for the reaction at body temperature (37.0 °C) if the concentration of A is 1.9 M and the concentration of B is 0.50 M? 9:26 PM 35% 77°F 6/14/2021The following were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics: Reaction Velocity (mmol/min) Substrate added (mmol/L) 217 0.8 325 2 433 4 488 6 647 20 652 1000 The Km for this enzyme is approximately _____________. (Round to the nearest integer)
- The following data were collected in the study of a new enzyme and an inhibitor of the new enzyme: Vo (nmol/sec) [S] (uM) Inhibitor + Inhibitor 1.3 2.50 0.62 2.6 4.00 1.42 6.5 6.30 2.65 13.0 7.60 3.12 26.0 9.00 3.58 What class of reversible enzyme inhibitor is being employed in this enzyme reaction?From data in the table, calculate the AG'º value for the reactions. Reaction AG° (kJ/mol) Phosphocreatine + H,O → creatine + P; |-43.0 |ADP + P; → ATP + H,O |+30.5 Fructose + P; → fructose 6-phosphate + H,0 +15.9 Phosphocreatine + ADP → creatine + ATP AG'º = kJ/mol ATP + fructose → ADP + fructose 6-phosphate AG'º = kJ/molGiven the following set of kinetic data, what is the KM of the enzyme? Numerical answer, only (assuming the same units as seen in the table). [S] (micro M) vo (Micro mol/sec) 1 49 2 96 8 249 50 498 100 656 1000 778 5000 999