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The Biology Project > Biomath > Rational Functions > Applications > Michaelis-Menten Kinetics

Rational Function Applications

Michaelis-Menten Kinetics

One of the ways biochemists characterize enzymes is to study the rates of enzyme-catalyzed reactions, a field known as enzyme kinetics. The study of enzyme kinetics provides researchers with clues as to how enzymes work. In 1913, Leonor Michaelis and Maud Menten derived a rate law that governs enzyme kinetics.


Michaelis-Menten enzyme kinetics can be modeled by the rational function,

where V represents the reaction velocity, Vmax represents the maximum reaction velocity, Km represents the Michaelis-Menten constant, and [S] represents the substrate concentration. The velocity of the reaction, V,is dependent on the substrate concentration, [S].

Note of caution

This equation assumes that during the reaction the concentration of the enzyme-substrate complex remains constant and is lower than the concentrations of unbound substrate. These conditions are known as steady-state.


Use the Michaelis-Menten equation to answer the following questions:

Find the velocity of a reaction given the substrate concentration.

Find the substrate concentration given the reaction velocity.

Determine the velocity of a reaction as the substrate concentration approaches infinity.


The Biology Project > Biomath > Rational Functions > Applications > Michaelis-Menten Kinetics

The Biology Project
Department of Biochemistry and Molecular Biophysics

The University of Arizona

February 2007
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