Simple enzyme mechanisms are capable of a surprisingly rich variety of
behavior. This paper presents a global analysis of this behavior for
several inhibition mechanisms, For instance, in competitive inhibition
one can vary the system parameters (typically total inhibitor concent
ration); then the ordinary differential equations describing this mech
anism can display two bifurcations which separate the relaxation behav
ior into three distinct regimes. In one of these regimes, the usual st
eady-state treatment does not describe the dynamics, even as a first a
pproximation. These different classes of relaxation kinetics are analy
zed in detail, and methods are presented for the extraction of the und
erlying invariant manifold structure. The global analysis of three rel
ated inhibition mechanisms is also discussed.