We re-visit previous analyses of the classical Michaelis-Menten substrate-e
nzyme reaction and, with the aid of the reverse quasi-steady-state assumpti
on, we challenge the approximation d[C]/dt approximate to 0 for the basic e
nzyme reaction at high enzyme concentration. For the first time, an approxi
mate solution for the concentrations of the reactants uniformly valid in ti
me is reported. Numerical simulations are presented to verify this solution
. We show that an analytical approximation can be found for the reactants f
or each initial condition using the appropriate quasi-steady-state assumpti
on. An advantage of the present formalism is that it provides a new procedu
re for fitting experimental data to determine reaction constants. Finally,
a new necessary criterion is found that ensures the validity of the reverse
quasi-steady-state assumption. This is verified numerically. (C) 2000 Soci
ety for Mathematical Biology.