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Study on Dihydrodiol Dehydrogenase (I) Molecular Forms of the Enzyme and the Presence of a Dihydrodiol Specific Enzyme in Bovine Liver Cytosol

  • Tohru Nishinaka
  • Tomoyuki Terada
  • Toshifumi Umemura
  • Hirofumi Nanjo
  • Tadashi Mizoguchi
  • Tsutomu Nishihara
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 284)

Abstract

It has been known that benzo(a)pyrene and benzo(a)anthracene, typical carcinogenic polycyclic aromatic hydrocarbons, are metabolized in microsome to the corresponding dihydrodiols via epoxides (Yang, et al., 1976; Thakker, et al., 1982) and then converted to the ultimate carcinogens (Buening, et al., 1978). Dihydrodiol dehydrogenase is an enzyme which catalyzes the dehydrogenation of the dihydrodiols of benzo(a)pyrene and benzo(a)anthracene in the presence of NADP+ and forms o-quinone (Vogel, et al., 1980; Smithgall, et al., 1988). The addition of this enzyme to the Ames test significantly reduced the mutagenicity of benzo(a)pyrene, suggesting that this enzyme might detoxify the trans-dihydrodiols which were formed in situ by oxidizing them to the less reactive o-quinones (Glatt, et al., 1979). In addition, similar experiments showed that the purified enzyme reduced the mutagenicity of other polycyclic aromatic hydrocarbons (Smithgall, et al., 1986). On the basis of these facts, Penning and coworkers suggested that dihydrodiol/ 3α -hydroxysteroid dehydrogenase might play an important role in the detoxification of these carcinogenic polycyclic aromatic hydrocarbons in rat liver (Smithgall, et al., 1988). Recently, many dihydrodiol dehydrogenases were purified from various animals and tissues, and these enzymes were identified as 3α -hydroxysteroid dehydrogenase, 17β -hydroxysteroid dehydrogenase and aldehyde reductase from their substrate specificities and inhibitor sensitivities (Smithgall, et al., 1988; Sawada, et al., 1988; Terada, et al., 1990).

Keywords

Polycyclic Aromatic Hydrocarbon Bovine Liver Hydroxysteroid Dehydrogenase Aldehyde Reductase Inhibitor Sensitivity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Tohru Nishinaka
    • 1
  • Tomoyuki Terada
    • 1
  • Toshifumi Umemura
    • 1
  • Hirofumi Nanjo
    • 1
  • Tadashi Mizoguchi
    • 1
  • Tsutomu Nishihara
    • 1
  1. 1.Laboratory of Biochemistry, Faculty of Pharmaceutical SciencesOsaka UniversitySuita, Osaka 565Japan

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