The Michaelis-Menten equation

The mentioned assumptions and definitions regarding the Michaelis-Menten model lead to the Michaelis-Menten equation (for a more detailed derivation, see below), where k_m = (k_-1 + k₂) / k₁, and where the "0" in v₀ implies that this equation is only valid for describing the initial rates, where no significant amount of product has been formed. The 2 constants V_max and k_m will be described on the following pages. k m equals k minus 1 plus k 2 divided by k 1, and where the 0 in V 0 implies that this equation is only valid for describing the initial rates, where no significant amount of product has been formed. The 2 constants V max and k m will be described on the following pages.

V₀ = V_max[S]/K_m+[S] V 0 equals V max times the substrate concentration divided by k m plus the substrate concentration

Of course, the assumptions regarding the model do not apply to all enzymatic reactions; therefore, it is sometimes necessary to use more complicated models to describe them. However, the Michealis-Menten equation applies to many different enzymatic reactions, often involving several more steps than the 2-step mechanism proposed by Michaelis and Menten. Thus, enzymes that show a hyperbolic relationship between v₀ and [S] are said to follow Michaelis-Menten kinetics [1] v 0 and substrate concentration are said to follow Michaelis-Menten kinetics.

References

1. Lehninger, Albert L.; Nelson, David L.; Cox, Michael M. (2008). Principles of Biochemistry (5th ed.). New York, NY: W.H. Freeman and Company. ISBN 978-0-7167-7108-1.

Reaction rate

Theory overview