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. 2012 Nov 14;288(2):785–792. doi: 10.1074/jbc.M112.419135

TABLE 1.

Reactions and Rate equations included in the model

All the enzymatic steps follow a Michaelis-Menten mechanism. The parameters of the Michaelis-Menten equations are Vmi and Kmi where subscript i represents the reaction ri with i = 0 to 5. The reactions catalysed by α-secretase, r1 and r5, have a slightly more complicated rate equations (vr1,α and vr5,α) since there are two competing substrates, C99 and APP, that individually give Michaelis-Menten kinetics when studied separately (40, 41). The same applies for the rate equations depending on γ-secretase, vr3,γ and vr4,γ, where C99 and C83 are substrates competing for this enzyme. vr,j represents the rate of reaction ri catalyze by secretase j, with j = α, β or γ and i = 1 to 5. vr0 is the rate of reaction r0.

Reaction Secretase Reaction rate
r0 (→ APP) vr0 = constant
r1 (APP → C83) α vr1,α=Vm1APP/Km11+APP/Km1+C99/Km5
r2 (APP → C99) β vr2,β=Vm2APP/Km21+APP/Km2
r3 (C83 → p3) γ vr3,γ=Vm3C83/Km31+C83/Km3+C99/Km4
r4 (C99 → Aβ) γ vr4,γ=Vm4C99/Km41+C83/Km3+C99/Km4
r5 (C99 → C83) α vr5,α=Vm5C99/Km51+APP/Km1+C99/Km5