Deriving the Michaelis-Menten Equation:

 

equation       (1)

Let v0 be the initial velocity of the reaction, i.e. the appearance of the product P in solution (d[P]/dt) whose first-order rate equation is:

v0 = k2[ES] (2)

containing an experimentally measurable variable, v0, a kinetic parameter, k2, and another unknown variable, [ES].

So in the steady state:

k-1[ES] + k2[ES] = k1[E][S] (3)

Collect together the kinetic constants, and the concentrations (variables):

(k-1 + k2) [ES] = k1 [E][S], and (4) (k-1 + k2)/k1 = [E][S]/[ES]

Group the kinetic constants, defining them as Km:

Km = (k-1 + k2)/k1 (5)

Express [E] in terms of [ES] and [E]total, to limit the number of unknowns:

[E] = [E]total - [ES] (6)

Substitute (5) and (6) into (4):

Km = ([E]total - [ES]) [S]/[ES] (7)

Solve for [ES]: 

First multiply both sides by [ES]:  

[ES] Km = [E]total[S] - [ES][S]  

Then collect terms containing [ES] on the left:  

[ES] Km + [ES][S] = [E]total[S]

Factor [ES] from the left-hand terms:

[ES](Km + [S]) = [E]total[S]

and divide both sides by (Km + [S]):

[ES] = [E]total [S]/(Km + [S]) (8)

Substitute (8) into (2):

v0 = k2[E]total [S]/(Km + [S]) (9)

The maximum velocity Vmax occurs when the enzyme is saturated - thus:

Vmax = k2 [E]total (10)

Substitute Vmax into (9) for k2 [E]total:

 

v0 = Vmax [S]/(Km + [S])     (11)