Question

Which of the following in not true for an enzymatic reaction that shows Michaelis-Menten kinetics?

Group of answer choices

the rate steadily decreases over the course of the reaction

Vmax depends on the concentration of the enzyme

in the presence of an inhibitor the v vs. [S] plot is a hyperbola

the equilibrium constant is lower as compared to the uncatalyzed reaction

K_M is determined by finding the [S] at which v = V_max/2

Answer 1

◆ the equilibrium constant is lower as compared to the uncatalyzed reaction ( wrong statement )

◆ Reason :-

• Equilibrium constants do not changed when catalyst is added or removed .
• The equilibrium constant can be changed by changing the temperature only.
• catalyst can only change rate of reaction by speeding up the reaction in forward as well as in backward direction by same extent.
• Ezymes are biological catalyst.
• Position of equilibrium can not be changed by catalyst.
• As temperature increases , the equilibrium constant decreases in exothermic reaction.
• As temperature increase , the equilibrium constant also increase in endothermic reaction.