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- W1895217811 abstract "Alcohol dehydrogenase (ADH; EC 1.1.1.1.) is a zinc metalloenzyme with at least five classes. Class I enzymes (α, β, and γ) form homodimeric and heterodimeric isoenzymes, the subunits of which are encoded by the ADH1, ADH2, and ADH3 genes, respectively, and play an important role in the metabolism of ingested ethanol. Among the α, β, and γ enzymes, the largest kinetic differences occur in the three polymorphic variants at ADH2. A G-to-A transition that resulted in conversion of arginine 47 (β1, encoded by ADH2) to histidine (β2, encoded by ADH2) in exon 3, and a substitution of an arginine 369 to cystine (β3, encoded by ADH2) of the ADH2 gene have been observed. We have focused on ADH2 and ADH2, as β3 has been identified only in Africans (1). The atypical enzymes involving the β2 subunit(s) have a high activity as indicated by V max values (2)(3), but the significance of ADH2 genotypes in patients with alcohol-related problems is still controversial: Takeshita et al. reported that drinking habits were not significantly associated with the ADH2 genotype (4); Muramatsu et al. reported that the ADH2/2 homozygote appeared less frequently in nonalcoholic subjects (though not statistically significantly) and that the ADH2 allele was present with significantly lower incidence among alcoholics than nonalcoholics (5); and Tanaka et al. reported …" @default.
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- W1895217811 date "1998-03-01" @default.
- W1895217811 modified "2023-10-16" @default.
- W1895217811 title "Detection of ADH21 and ADH22 Alleles in Fingernails from Japanese" @default.
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- W1895217811 doi "https://doi.org/10.1093/clinchem/44.3.675" @default.
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