Abstract
Dihydrodiol dehydrogenase (DDH) [EC 1.3.1.20] has been suggested to play an important physiological role in the metabolic detoxication of polycyclic aromatic hydrocarbons (PAHs) (Glatt et al., 1979). The pathways for metabolic activation and detoxication of a typical PAH, benzo[a]pyrene, are shown in Scheme 1. Environmental PAH is mainly activated through the action of liver P-450. The resulting 7,8-epoxide moiety is hydrolyzed by epoxide hydrolase in microsome. Then, the 7,8-dihydrodiol of PAH is further oxygenated to the 7,8-dihydrodiol-9,10-epoxide form by P-450 (Penning, 1993). This compound is assumed to be an ultimate carcinogen which binds covalently to DNA. Alternatively, DDH is reported as an important converting enzyme of the 7,8-dihydrodiol moiety to less active 7,8-dione (dicarbonyl). The dicarbonyl compound is further detoxicated with nonenzymatic ghlutathione-conjugation reaction (Penning, 1993).
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Terada, T. et al. (1996). Cloning and Expression of cDNA Encoding Bovine Liver Dihydrodiol Dehydrogenase 3, DD3. In: Weiner, H., Lindahl, R., Crabb, D.W., Flynn, T.G. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 6. Advances in Experimental Medicine and Biology, vol 414. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5871-2_62
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