Abstract
Alcohol dehydrogenase (ADH) of class I is the principal enzyme in liver ethanol oxidation, and has been the subject of much research. It has been studied in many species and is a part of the enzyme system now constituting ADHs at large. The different mammalian ADHs can be divided into at least five classes according to structural properties (Pares et al., 1992). Class I is the classical liver ADH (Vallee and Bazzone, 1983), and class III ADH is the glutathione-dependent formaldehyde dehydrogenase (Koivusalo et al., 1989). ADH of class II shows a higher Km for ethanol than class I, and exhibits activity toward norepinephrine metabolites (Mardh et al., 1986), but is less studied than class I and class III ADH. Class IV is a stomach ADH characterized in rat and man (Pares et al., 1990; 1992; Moreno and Pares, 1991), and class V is a DNA-derived human structure recently reported (Yasunami et al., 1991).
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