Final answer:
The graph of initial reaction rate versus substrate concentration for enzymes exhibiting Michaelis-Menten kinetics forms a hyperbolic curve, increasing until it plateaus at Vmax when the enzyme is saturated with substrate.
Step-by-step explanation:
When experiments are performed on enzymes that exhibit traditional Michaelis-Menten kinetics, the graph of initial reaction rate (V0) versus substrate concentration [S] displays a specific shape known as a hyperbolic curve. As the substrate concentration increases, the reaction rate also increases until it reaches a point where it remains constant regardless of further increases in substrate concentration. This plateau occurs because all active sites on the enzyme molecules are occupied, which means the enzyme is saturated with the substrate. The reaction rate at this stage does not increase and is called the maximum velocity (Vmax). The substrate concentration at which the reaction rate is half of Vmax is known as the Michaelis constant (Km).