Abstract
Class III ADHs are not saturable with ethanol as substrate; long chain alcohols and ω-hydroxyfatty acids are better substrates (Pares and Vallee, 1981; Wagner et al., 1984; Kaiser et al., 1988; Giri et al., 1989b). These ADHs also function as glutathione-dependent formaldehyde dehydrogenases (FDH), as shown by Koivusalo et. al. (1989). Class III ADH, in contrast to the other ADH classes, is expressed in virtually all tissues (Adinolfi et al., 1984; Seeley et al., 1984; Duley et al, 1985; Holmes et al., 1986b; Holmes et al., 1986a; Julia et al., 1987; Edenberg, 1991). The amount of expression is higher in liver and kidney than in other tissues (Adinolfi et al., 1984; Seeley et al., 1984; Duley et al., 1985; Holmes et al., 1986b; Holmes et al., 1986a; Julia et al., 1987; Hur et al., 1992). The class III alcohol dehydrogenases (ADH) have been highly conserved during evolution, suggesting important roles in cellular metabolism (Sharma et al., 1989; Giri et al., 1989a; Edenberg et al., 1991; Hur et al., 1992; Gutheil et al., 1992).
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Edenberg, H.J., Ho, WH., Hur, MW. (1995). Promoters of the Mammalian Class III Alcohol Dehydrogenase Genes. In: Weiner, H., Holmes, R.S., Wermuth, B. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 5. Advances in Experimental Medicine and Biology, vol 372. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1965-2_35
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DOI: https://doi.org/10.1007/978-1-4615-1965-2_35
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