Constant of Michaelis

See also: km

The Constante of Michaelis (Michaëlis) is a constant thermodynamics characterizing an enzymatic reaction. It is symbolized by Km and reflects the affinity of the enzyme for its substrate:

  • Plus it is large , more the enzyme is fixed badly on the substrate, the affinity of the enzyme for the substrate is small. The not very active enzymes have one km relatively high. For example proteases domestic.
  • Plus it is small , more the enzyme of course sets the substrate, the affinity of the enzyme for the substrate is large. The very active enzymes have one km relatively small. For example peroxidases.

The constant of Michaelis is characteristic of the Enzyme.

Km is the concentration in substrate for which the initial Speed of the reaction is with half of the maximum initial Speed. This constant is a concentration, it with the same unit: mol. L-1.

A competitive Inhibiteur increases the Constante of Michaelis. A pure noncompetitive inhibiter does not make vary the constant of Michaelis. An inhibiter mixed (or incompétitif) can make increase or decrease the constant of Michaelis.

See too

  • Equation of Michaelis Menten.

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