Michaelis-Menten curve

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). The graph can be used to calculate the Michaelis constant (K_m), which is the concentration of a substrate required in order for an enzyme to act at half of its maximum velocity (V_max). 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.

External Links:

• http://web.lemoyne.edu/~giunta/menten.html -- Original paper on Michaelis-Menten kinetics