Mechanism for enzyme catalyzed reactions. To explain the kinetics of enzyme- substrate reactions, Michaelis  Menten (1913) came up with the following mechanism, which uses an equilibrium assumption
and where [E₀] represents the total enzyme and [E] represents the free unattached enzyme.

G. E. Briggs and J. B. S. Haldane, Biochem J., 19, 338 (1925), on the other hand, employed a steady-state assumption in place of the equilibrium assumption

What final rate form - r_A in terms of [A], [E₀], k₁, k₂, and k₃, does

(a) The Michaelis-Menten mechanism give?

(b) The Briggs-Haldane mechanism give?

Transcribed Image Text:

A+E=X k₂ XR+E with K = [X] [A][E]' and with [E] [E] + [X]