A graph that shows the relationship between the concentration of a substrate and the rate of the corresponding enzyme-controlled reaction. The curve only applies to enzyme reactions involving a single substrate. It was devised by Leonor Michaelis (1875–1949) and Maud Menten (1879–1960) in 1913. The graph can be used to calculate the Michaelis constant (Km), which is the concentration of a substrate required in order for an enzyme to act at half of its maximum velocity (Vmax). The Michaelis constant is a measure of the affinity of an enzyme for a substrate. A low value corresponds to a high affinity, and vice versa. See also enzyme kinetics.
https://web.lemoyne.edu/~giunta/menten.html Original paper on Michaelis–Menten kinetics