Skip to main content
Life Science Dictionary

Michaelis constant

Biochemistry

Say it: mih-KAY-lis KON-stunt

The Michaelis constant (Km) is the substrate concentration at which an enzyme-catalyzed reaction runs at half its maximum rate.

Also: Km, Michaelis-Menten constant

Definition

What is the Michaelis constant?

The Michaelis constant, written Km, is a value in the Michaelis-Menten equation, which describes how the rate of an enzyme reaction depends on the amount of substrate. In that equation, v = Vmax[S] / (Km + [S]), v is the initial rate, [S] is the substrate concentration, and Vmax is the top rate reached when every enzyme molecule is busy. Setting [S] equal to Km gives exactly half of Vmax, which is the usual working definition. Km is a concentration, so it is reported in units such as millimolar or micromolar.

Km depends on both the enzyme and the substrate. A low Km means the enzyme reaches half its top speed at a low substrate concentration, which is often read as high affinity. Strictly, though, Km combines the rate constants for substrate binding, release and conversion to product, and it equals the true dissociation constant only in special cases.

Students meet Km in kinetics practicals and in questions on enzyme inhibition: a competitive inhibitor raises the apparent Km but leaves Vmax unchanged. It is named after Leonor Michaelis and Maud Menten, who published their analysis in 1913.

Practice it

Where you'll meet it

Related

Sources

Checked against

Keep going

Practice Biochemistry

Free biochemistry quizzes, with an explanation for every answer.

See the Quizzes