Which of the following is NOT required in order for an enzyme to display cooperative kinetics? A) Multiple subunits. B) A value for the Michaelis constant, K_M. C) Allosteric sites which affect the binding of substrate to the active site. D) Ability to display a V_max. E) All of these are characteristic of cooperative enzymes.

Question

Quizplus · Accepted Answer

Cooperative kinetics in enzymes typically involves multiple subunits and allosteric sites that affect substrate binding, leading to a sigmoidal (S-shaped) velocity vs. substrate concentration curve, indicative of cooperative binding. The Michaelis constant (Km) is a characteristic of Michaelis-Menten kinetics, not specifically required for cooperative behavior.

Which of the Following Is NOT Required in Order for an Enzyme