Final answer:
An allosteric enzyme contains an allosteric site that can be regulated by effector molecules, affecting the enzyme's activity. M-M enzyme kinetics is a mathematical model that describes enzyme kinetics based on substrate concentration and reaction rate.
Step-by-step explanation:
An allosteric enzyme is an enzyme that contains an allosteric site, which is a site other than the active site. This site can be bound by effector molecules that can regulate the activity of the enzyme. When an effector molecule binds to the allosteric site, it can induce a conformational change in the enzyme, affecting its affinity for the substrate and reaction rates.
M-M enzyme kinetics, on the other hand, refers to Michaelis-Menten enzyme kinetics. This is a mathematical model used to describe enzyme kinetics based on the substrate concentration and the rate of product formation. It assumes that enzyme-substrate complexes form and break down in a reversible manner, and it gives us information about the enzyme's maximum reaction rate (Vmax) and the substrate concentration required for the enzyme to achieve half of its maximum rate (Km).
In summary, the main difference between allosteric enzymes and M-M enzyme kinetics lies in their focus. Allosteric enzymes involve the regulation of enzyme activity through interactions at an allosteric site, while M-M enzyme kinetics is a mathematical model that describes the relationship between substrate concentration and reaction rate.