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2 . 2 3 . Mechanism for enzyme catalyzed reactions. To explain the kinetics of en - zyme - substrate reactions, Michaelis and Menten (

2.23. Mechanism for enzyme catalyzed reactions. To explain the kinetics of en-
zyme-substrate reactions, Michaelis and 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 -rA in terms of [A],[E0],k1,k2, and k3 does
(a) the Michaelis-Menten mechanism give?
(b) the Briggs-Haldane mechanism give?
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