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.
Michaelis determined the Michaelis constant (Km) that establishes the affinity between an enzyme and its substrate.
The Michaelis-Menten equation predicts and explains the reaction rate, that is, the amount of substrate that reacts with the enzyme per unit of time, as well as the factors that stimulate or inhibit this reaction rate.
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; this is the moment at which the maximum reaction rate (Vmax) is reached.
If an inhibitor is non-competitive, the reaction catalyzed by the enzyme will never reach its normal maximum reaction rate, even in the presence of a lot of substrate.