The scheme below describes the enzymatic inhibition mechanism where the substrate acts as an inhibitor.
Dissociation constant
E + S
K1
ES
KM = k-1/k1
K-1
ES + S
ESS
Ksi = k-2/k2
K-2
K3
ES
E + P
Using the rapid equilibrium assumption for both ES and ESS formation, show that the modified Michaelis-Menten equation for the rate v of formation of Vmax[S] product P is given by V where Vmax = k[Eo] and KM,app + [S] [S]^2 KMapp = KM + Ksi