algae/notes/mm_derivation.html

Derivation of the Michaelis-Menten equation

 

For the enzyme catalyzed reaction

 

E + S --k1-->
<--k2--
ES --k3-->
<--k4--
E + P

 

v = k3*[ES]

Rate of formation of ES = k1* [E]*[S]

Rate of breakdown of ES = (k2 + k3) * [ES]

At steady state, the formation and breakdown are equal. This steady state would be temporary in any enzyme assay or nutrient uptake experiment.

k1* [E]*[S] = (k2 + k3) * [ES]

rearranging:

[ES] = [E]*[S]/((k2 + k3)/k1)

We can lump these kinetic constants to make a new constant called Km = (k2 + k3)/k1)

[ES] = [E]*[S]/Km

The total enzyme is the amount bound and unbound to the substrate

[Etot] = [E] + [ES]

Substituting [Etot] - [ES] for [E]

[ES] = ([Etot] - [ES]) *[S]/Km

Solving for [ES]

[ES] = ([Etot] *(( [S]/Km)/(1+[S]/Km))

Which simplifies to

[ES] = [Etot] * [S] / ([S] + Km)

Multiplying both sides by k3 gives the velocity of the reaction

v = k3*[ES] = k3* [Etot] * [S] / ([S] + Km)

substituting Vmax for k3* [Etot] gives the familar form of the MM equation

 

v = Vmax * [S] / ([S] + Km)