Which of these statements about enzyme-catalyzed reactions is false? The activation energy for the catalyzed reaction is the same as for the uncatalyzed reaction, but the equilibrium constant is more favorable in the enzyme-catalyzed reaction. The Michaelis-Menten constant Km equals the [S] at which V = 1/2 Vmax: O At saturating levels of substrate, the rate of an enzyme-catalyzed reaction is proportional to the enzyme concentration. The rate of a reaction decreases steadily with time as substrate is depleted. O If enough substrate is added, the normal Vmax of a reaction can be attained even in the presence of a competitive inhibitor.

The first reaction in Glycolysis is the phosphorylation of Glucose:Pi + Glucose → Glucose 6-Phosphate + waterThis is a thermodynamically unfavorable process with a ∆G0’ = +13.8 kJ/mol.  In a liver cell at370C the concentrations of both phosphate and glucose are normally maintained at about 0.005 M each.  What would be the equilibrium concentration of Glucose 6-Phosphate according to the above data?  Note:  In the biochemical standard state ​[H2O] = 1.0 a. 0.00000012 b. 0.0000025 c. 0.00000025 d. 0.00474 e. 0.005 f. 1.0 g. 0.1 h. 0.25 i. 2.4

What general effects would you expect the following changes to have on the rate of an enzyme-catalyzed reaction for an enzyme that has its maximum activity at body temperature (about 37 °C/310.15 K)?(a) Raising the temperature from 310 K (37 °C) to 343 K (70 °C)(b) Lowering the pH from 7 to 3(c) Adding an organic solvent, such as methanol

The first reaction in glycolysis is the phosphorylation of glucose:                 Pi + glucose → glucose-6-phosphate + H2O                                                   This is a thermodynamically unfavorable process, with ∆G°′ = +13.8 kJ/mol. (a) In a liver cell at 37 °C the concentrations of both phosphate and glucose are normally maintained at about 5 mM each. What would be the equilibrium concentration of glucose-6-phosphate, according to the above data? (b) This very low concentration of the desired product would be unfavorable for glycolysis. In fact, the reaction is coupled to ATP hydrolysis to give the overall reaction ATP + glucose → glucose-6-phosphate + ADP + H+ What is ∆G°′ for the coupled reaction? (c) If, in addition to the constraints on glucose concentration listed previously, we have in the liver cell ATP concentration = 3 mM and ADP concentration = 1 mM, what is the theoretical concentration of glucose6-phosphate at equilibrium at pH = 7.4 and 37 °C? The answer…