Abstract
Publisher Summary (–)t–7, 8–dihydrodiol benzo(a)pyrene (BP) is activated to diol expoxide I and II by the microsomal mixed-function oxidase (MFO) systems. These are major mutagenic and carcinogenic metabolites of BP and bind to DNA, RNA, and proteins. This chapter discusses the role of epoxide hydratase in the hydrolysis and binding of diol epoxides (DE) I and II to DNA and proteins. Studies indicate that DNA diol epoxide binding is stereoselective. In the study discussed in the chapter, it showed that the binding of reactive metabolites formed from 3 H(–)t–7, 8–dihydrodiol BP to DNA and proteins was reduced by epoxide hydratase. The inhibition of DNA and protein binding by epoxide hydratase indicates that the hydratase has some stereospecific interaction with diol epoxides, binds them covalently, alters their mode of hydrolysis, and may reduce their activity as carcinogenic intermediates. Therefore, these results indicate that epoxide hydratase may play a role in diol epoxide detoxification.
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