web.pdx.edu/~rueterj/bi335web/unit3/mm_derivation.htm

Derivation of the Michaelis-Menten Equation

For the enzyme catalyzed reaction:
E + S --k1--> ES complex --k3--> E + P
......... <--k2--

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 the breakdown are equal. This steady state would only be temporary.

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

rearranging:

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

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

[ES] = [E][S]/ KM

[ET] = [E] + [ES] (The total amount of enzyme equals the free and that bound to substrate)

Substituting in [ET] - [ES] for [E]

[ES] = ([ET] - [ES]) [S]/ KM

Solving for [ES] leads to [ES] = ([ET] (([S]/ KM)/(1 + [S]/ KM ))

Which simplifies to

[ES] = ([ET] *([S]/([S] + KM )

Multiplying both sides by the kinetic constant k3 gives the velocity of the reaction

v = k3 * [ES] = k3*[ET] *(([S]/([S] + KM )

and substituting Vmax for k3*[ET] leads to the familiar form of the Michaelis Menten Equation

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


John Rueter Feb 4. 1997