What is the Michaelis-Menten equation and graph?

The Michaelis-Menten equation describes the change in the rate of an enzyme-catalyzed reaction as the concentration of the substrate varies.
The reaction between the enzyme and its substrate is preceded by the formation of a complex.
Michaelis determined the Michaelis constant (Km) that establishes the affinity between an enzyme and its substrate.
The successive additions of substrate to the reaction medium cause a sudden increase in the reaction rate until a certain point is reached, at which the enzyme is saturated and the subsequent addition of substrate no longer affects the rate.
Non-competitive inhibitors prevent the enzyme from reaching its normal maximum reaction rate, even in the presence of a lot of substrate.