Slow-tight inhibition occurs when the initial enzyme–inhibitor complex EI undergoes conformational isomerism (a change in shape) to a second more tightly held complex, EI*, but the overall inhibition process is reversible. This manifests itself as slowly increasing enzyme inhibition. Under these conditions, traditional Michaelis–Menten kinetics give a false value for K, which is time–dependent. The true value of K can be obtained through more complex analysis of the on (k) and off (k) rate constants for inhibitor association with kinetics similar to irreversible inhibition.