Explanation of the non-hyperbolic kinetics of the glutathione S-transferases by the simplest steady-state random sequential Bi Bi mechanism.

We have demonstrated that the simplest steady-state random sequential Bi Bi mechanism is sufficient to explain the previously reported non-hyperbolic kinetics of glutathione S-transferase 3-3 [Pabst MJ et al., J Biol Chem 249: 7140-7150, 1974; Jakobson I et al., Biochem J 177: 861-868, 1979]. The metabolism of 1-chloro-2,4-dinitrobenzene by rat liver glutathione S-transferase isoenzymes 2-2 and 3-3 and of 1,2-dichloro-4-nitrobenzene by isoenzyme 3-4 was shown to exhibit non-hyperbolic kinetics, which are best fit by the simplest steady-state random sequential Bi Bi mechanism. Neither more complex steady-state mechanisms nor the superimposition of product inhibition or enzyme memory on the simplest steady-state mechanism was necessary to generate non-hyperbolic kinetics for the glutathione S-transferases.