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Inactivation of a Diol Epoxide by Dihydrodiol Dehydrogenase But Not by Two Epoxide Hydrolases

1982; American Association for the Advancement of Science; Volume: 215; Issue: 4539 Linguagem: Inglês

10.1126/science.7038877

1095-9203

Hansruedi Glatt, C.S. Cooper, P.L. Grover, Peter Sims, P. Bentley, Marcel MERDES, F. Waechter, K. Vogel, Thomas M. Guenthner, Franz Oesch,

Microbial bioremediation and biosurfactants

The mutagenicity of r -8, t -9-dihydroxy- t -10, 11-oxy-8,9,10,11-tetrahydrobenz[ a ]anthracene (BA-8,9-diol 10,11-oxide) toward Salmonella typhimurium TA 100 is not decreased by the presence of large amounts of highly purified microsomal or cytosolic epoxide hydrolase. However, highly purified dihydrodiol dehydrogenase inactivates this diol epoxide, which is a major DNA-binding metabolite of benz[ a ]anthracene. The K-region epoxide, benz[ a ]anthracene 5,6-oxide (BA 5,6-oxide) is efficiently inactivated by microsomal epoxide hydrolase, is much less readily inactivated by cytosolic epoxide hydrolase, and is not inactivated by dihydrodiol dehydrogenase. This inactivation of a diol epoxide by dihydrodiol dehydrogenase points to a new significance of this enzyme and a new level of control for diol epoxides.