Abstract
In humans, there is a family of NAD+- and zinc-dependent alcohol dehydrogenases (E.C. 1.1.1.1) that exhibit broad substrate specificity toward aliphatic alcohols (Vallee and Bazzone, 1983, Smith, 1986, and Bosron et al., 1993). The various isozyme subunits are encoded by at least 6 different gene loci (ADH1 through ADH6). Most recently, a new isozyme called σ-ADH or μ-ADH has been isolated from human stomach tissue that has a high K m (about 30 mM) and relatively high catalytic efficiency for ethanol (k c /K m ∼ 52 min-1mM-1)(Wang et al., 1990, Stone et al, 1993, Moreno and Pares, 1991). One or more isozymes with similar electrophoretic mobility are found in the esophagus (Yin et al., 1990).
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