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Michaelis-Menten Kinetics Overview

The Michaelis-Menten equation describes the rate of enzymatic reactions and relates the reaction rate to the concentration of a substrate. It indicates that the reaction rate increases with increasing substrate concentration until it reaches the maximum rate Vmax. The equation includes Vmax, which represents the maximum reaction rate achieved at high substrate concentrations, and KM, the substrate concentration at which the reaction rate is half of Vmax.

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Princess Janine Catral
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11 views1 page

Michaelis-Menten Kinetics Overview

The Michaelis-Menten equation describes the rate of enzymatic reactions and relates the reaction rate to the concentration of a substrate. It indicates that the reaction rate increases with increasing substrate concentration until it reaches the maximum rate Vmax. The equation includes Vmax, which represents the maximum reaction rate achieved at high substrate concentrations, and KM, the substrate concentration at which the reaction rate is half of Vmax.

Uploaded by

Princess Janine Catral
Copyright
© All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Princess Janine B.

Catral BS ChE IV

I. Michaelis-Menten Equation

In biochemistry, Michaelis–Menten kinetics is one of the best-known models of enzyme kinetics. It is named after
German biochemist Leonor Michaelis and Canadian physician Maud Menten. The model takes the form of an
equation describing the rate of enzymatic reactions, by relating reaction rate to , the concentration of
a substrate S. Its formula is given by

This equation is called Michaelis–Menten equation. Here, represents the maximum rate achieved by
the system, at maximum (saturating) substrate concentrations. The Michaelis constant is the substrate
concentration at which the reaction rate is half of .[1] Biochemical reactions involving a single substrate
are often assumed to follow Michaelis–Menten kinetics, without regard to the model's underlying assumptions.

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