Distribution of Dimeric Dihydrodiol Dehydrogenase in Pig Tissues and its Role in Carbonyl Metabolism

• DOI: 10.1007/978-1-4684-5901-2_21
• Publication Date: 2012-04-01T04:02:09Z
• Authors: Toshihiro Nakayama; Hideo Sawada; Yoshihiro Deyashiki; Takushi Kanazu; Akira Hara; Michio Shinoda; Kazuya Matsuura; Yasuo Bunai; Isao Ohya
• Keywords: Aldehydes; Immunodiffusion; Oxidoreductases Acting on CH-CH Group Donors; Macromolecular Substances; Swine; Ketones; Chromatography, Ion Exchange; Antibodies; Substrate Specificity; Alcohol Oxidoreductases; Kinetics; Organ Specificity; Chromatography, Gel; Animals; Oxidoreductases

A cytosolic NADP+-dependent dihydrodiol dehydrogenase (EC 1.3.1.20), that oxidizes dihydrodiol derivatives of benzene and naphthalene to the corresponding catechols, has been thought to play an important role in metabolic detoxification of carcinogenic polycyclic aromatic hydrocarbons (Oesch, et al., 1984) and in bioactivation of naphthalene in rabbit eye (van Heyningen, 1976). Dihydrodiol dehydrogenase was first isolated from rat liver (Vogel, et al., 1980) and has been subsequently identified as 3α-hydroxysteroid dehydrogenase (Penning, et al., 1984). The enzyme is a monomer of Mr35,000 and shows dehydrogenase activity for xenobiotic alicyclic alcohols and carbonyl reductase activity, which indicate that it also functions in carbonyl metabolism. Similar monomeric dihydrodiol dehydrogenases with broad substrate specificity for xenobiotics have been purified from other mammalian livers, and have been reported to be identical with 17s-hydroxysteroid dehydrogenase in the guinea pig (Hara, et al., 1986a), mouse (Sawada, et al., 1988) and rabbit (Hara, et al., 1986b), 3α(17β)-hydroxysteroid dehydrogenases in the hamster (Ohmura, et al., 1990), 3(20)α-hydroxysteroid dehydrogenase in the monkey (Hara, et al., 1989a), and aldehyde reductase.