Final answer:
Enzymes exhibit two types of saturation kinetics: one for regulatory enzymes, resulting in a sigmoid curve, and one for non-regulatory enzymes, leading to a hyperbolic curve. These are characterized by kinetic properties, namely Km and Vmax. Km represents the substrate concentration at which the reaction rate is half its maximum, and Vmax is the maximum reaction rate when the enzyme is saturated with substrate.
Step-by-step explanation:
Types of Saturation Kinetics in Enzymes
The two types of saturation kinetics exhibited by various enzymes include the kinetics of regulatory enzymes, which give a sigmoid curve, and those of non-regulatory enzymes, which display a hyperbolic curve. The two most important kinetic properties that define these behaviors are Km and Vmax.
Km refers to the Michaelis-Menten constant, which is the substrate concentration at which the reaction rate is at half its maximum. The Vmax is the maximum rate at which an enzyme-catalyzed reaction can proceed when the enzyme is saturated with substrate. This occurs because at high substrate concentrations, all the active sites of the enzyme molecules are occupied by substrate, and further increases in substrate concentration will not increase the reaction rate.
In steady-state kinetics experiments, these parameters help to characterize an enzyme's catalysis and binding capabilities. The velocity of enzyme reactions is initially proportional to the substrate concentration but levels off as it approaches Vmax.