We will be considering two kinetic mechanisms of enzyme inhibition shown in Scheme 1. In the single-step Mechanism A, the enzyme and inhibitor reversibly form a single noncovalent complex; k on is the association rate constant and k off is the dissociation rate constant. The two-step Mechanism B involves a rapid (effectively instantaneous) formation of an initial complex, which relatively slowly rearranges into a final complex; k for is the forward isomerization rate constant and k rev is the reverse isomerization rate constant.