Final answer:
The type of enzyme-catalyzed reactions that exhibit non-Michaelis-Menten kinetics are Allosteric enzyme reactions. Allosteric enzymes can change their conformation upon effector molecule binding, which affects enzyme activity and results in a sigmoidal relationship between reaction rate and substrate concentration.
Step-by-step explanation:
The type of enzyme-catalyzed reactions that follow non-Michaelis-Menten kinetics are d) Allosteric enzyme reactions. Allosteric enzymes exhibit a different kinetic behavior compared to enzymes that follow the Michaelis-Menten model. Michaelis-Menten kinetics assume that the binding of substrate to the enzyme follows a simple binding process that can be characterized by a hyperbolic relationship between the reaction rate and the concentration of substrate.
However, allosteric enzymes have multiple active sites and can be regulated by the binding of effector molecules at separate sites from where the substrate binds. Allosteric enzymes show a sigmoidal (S-shaped) relationship between reaction rate and substrate concentration. This is because the binding of a substrate or an effector molecule can change the conformation of the enzyme, which can either inhibit or activate the enzyme, thereby not following the simple Michaelis-Menten model. Examples of non-Michaelis-Menten kinetics include the binding of an allosteric inhibitor which reduces enzyme activity, or an allosteric activator, which increases it. Bisubstrate reactions, on the other hand, whether they follow a random, ping pong, or ordered mechanism, typically still adhere to Michaelis-Menten kinetics when analyzed in terms of each individual substrate.