The kinetics of the conjugation of carcinogenic anti-diol epoxides of chrysene (anti-CDE) and benzo(g)chrysene [anti-B(g)CDE] with glutathione (GSH) catalyzed by GSH S-transferase (GST) isoenzymes mGSTP1-1, mGSTM1-1, mGSTA3-3, mGSTA4-4, and GST 9.5 of female A/J mouse tissues has been investigated. When GST activity was measured as a function of varying anti-CDE or anti-B(g)-CDE concentrations at a fixed concentration of GSH, each isoenzyme obeyed Michaelis-Menten kinetics. The catalytic efficiencies (k(cat)/Km) of murine GSTs in the GSH conjugation of anti-CDE were in the order of GST 9.5 > mGSTP1-1 > mGSTM1-1 > mGSTA3-3 > mGSTA4-4. While each GST isoenzyme examined in the present study exhibited preference for the GSH conjugation of (+)-anti-CDE with the (R,S)-diol (S,R)-epoxide absolute configuration, which is a far more potent carcinogen than the (-)-anti-CDE [(S,R)-diol (R,S)-epoxide absolute configuration], the enantioselectivity was relatively more pronounced for mGSTP1-1 compared with other murine GSTs. Anti-B(g)CDE was a relatively poor substrate for each GST isoenzyme examined compared with anti-CDE. The catalytic efficiencies of murine GSTs in the GSH conjugation of anti-B(g)CDE were in the order of GST 9.5 > mGSTP1-1 > mGSTM1-1 > mGSTA3-3. With the exception of mGSTM1-1, all other murine GSTs exhibited preference for the GSH conjugation of anti-B(g)CDE enantiomer with the (R,S)-diol (S,R)-epoxide absolute configuration. In summary, the results of the present study indicate that the murine GSTs significantly differ in their catalytic efficiency and enantioselectivity in the GSH conjugation of both anti-CDE and anti-B(g)CDE, and that anti-B(g)CDE is a relatively poor substrate for murine GSTs compared with anti-CDE, which may partially account for the observed relatively higher carcinogenic potency of the former compound.