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Gene Review

ADH1A  -  alcohol dehydrogenase 1A (class I), alpha...

Homo sapiens

Synonyms: ADH1, Alcohol dehydrogenase 1A, Alcohol dehydrogenase subunit alpha
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Disease relevance of ADH1A

  • Promoter activity of human ADH3, but not ADH1 or ADH2, was shown to be activated by retinoic acid in transient transfection assays of Hep3B human hepatoma cells [1].
  • ADH1 null lines that do not possess this factor survive only a few hours of anoxia [2].
  • Both the Adh1 intron 1 and the intron from a second maize gene, Bronze1, stimulated expression from other promoters (cauliflower mosaic virus 35S and nopaline synthase) and of other coding regions (luciferase and neomycin phosphotransferase II) as well [3].
  • Undernutrition led to impairment of EtOH metabolism, increased blood EtOH concentrations (160%), and decreased maternal hepatic ADH1 mRNA, protein, and activity [4].

High impact information on ADH1A

  • The structure of the adh1 region appears to be standard relative to the other gene-containing regions of the maize genome, thus suggesting that retrotransposon insertions have increased the size of the maize genome from approximately 1200 Mb to 2400 Mb in the last three million years [5].
  • Here we employ a novel approach to determine the insertion dates for 17 of 23 retrotransposons found near the maize adh1 gene, and two others from unlinked sites in the maize genome, by comparison of long terminal repeat (LTR) divergences with the sequence divergence between adh1 in maize and sorghum [5].
  • These results indicated that introns increase both Adh1 and chimeric gene expression in maize and the optimal location for such an intron is near the 5' end of the mRNA [3].
  • The expression of a chimeric chloramphenicol acetyltransferase (CAT) gene utilizing the 5' promoter and 3' polyadenylation regions of the Adh1 gene was increased 100-fold by the addition of sequences containing the Adh1 intron 1 [3].
  • The TATA box promoter region of maize Adh1 affects its organ-specific expression [6].

Biological context of ADH1A

  • ADH1*B1 has the most restrictive substrate-binding site near the catalytic zinc atom, whereas both ADH1A and ADH1C*2 possess amino acid substitutions that correlate with their better efficiency for the oxidation of secondary alcohols [7].
  • Accordingly, the gene frequencies of the alleles ADH1/3 and ADH2/3 were calculated to be 0.88 and 0.12, respectively [8].
  • Haplotype tag SNPs were selected for the block in the ADH4 gene that provided evidence of association and subsequently used in association analysis; the haplotype was significantly associated with alcoholism (P=0.01) There was weaker evidence that variations in ADH1A and ADH1B might also play a role in modifying risk [9].
  • The structure and nucleotide sequence of an allele at the ADH1 locus have been determined [10].
  • Agarose-IEF analyses, substrate specificity studies and immunochemical titrations of the major kidney ADH (ADH-1) also support the occurrence of a second Class I isozyme [11].

Anatomical context of ADH1A

  • Using ARE mutants in a transient assay in maize protoplasts we have shown that mutation of the GCBP-1 binding sites prevents significant hypoxic activation of the maize Adh1 promoter [12].

Associations of ADH1A with chemical compounds

  • However, the substitution of Gly for Arg at position 47 in the ADH1A isoenzyme promotes a greater extent of domain closure in the ADH1A isoenzyme, whereas substitution at position 271 may account for the lower turnover rate for the ADH1C*2 isoenzyme relative to its polymorphic variant, ADH1C*1 [7].
  • ADH1A expression was not stimulated by either 5-aza-dC or TSA [13].
  • In this paper, we have identified several distal cis-acting elements that contribute to the regulation and tissue- specificity of ADH1A, which encodes an alcohol dehydrogenase (ADH) that metabolizes ethanol [14].
  • This region was also demonstrated to confer retinoic acid responsiveness on the ADH1 and ADH2 genes in heterologous promoter fusions [1].
  • Three pyrazole-sensitive bands of enzymatic activity, designated ADH-1, ADH-2, and ADH-3, are cathodic at pH 8.2, and the fourth, ADH-An, is neutral to slightly anodic and insensitive to pyrazole [15].

Regulatory relationships of ADH1A

  • Positive regulation of the ADH1A gene may be influenced by GATA-2 binding, while differences in HNF-3beta binding in cells/tissues may contribute to tissue specificity [14].
  • Transgenic maize (Zea mays) plants were generated with a construct harboring a maize caffeic acid O-methyltransferase (COMT) cDNA in the antisense (AS) orientation under the control of the maize Adh1 (alcohol dehydrogenase) promoter [16].

Other interactions of ADH1A

  • This review focuses upon the regulation of the three human class I alcohol dehydrogenase genes, ADH1, ADH2 and ADH3 [17].
  • The subunits are coded for by at least five gene loci, ADH1-ADH5 [18].
  • Second, the substrate repertoire is unique, e.g. rodent ADH2s are not saturated with ethanol as substrate, and while omega-hydroxy fatty acids are common substrates for the human ADH1-ADH4 isoenzymes, including ADH2, these compounds function as inhibitors rather than substrates [19].
  • Two linked genes, Adh1 and Adh2, specify three sets of ADH isozymes in pearl millet [20].
  • Densitometric tracings of the zymogram of a cleared gel and measurements of activities of homodimer isozymes eluted from gels follwoing D-R of an intergenic isozyme showed that the Adh2 isozymes were more that twice as active as those of Adh1 [21].

Analytical, diagnostic and therapeutic context of ADH1A

  • The experimental procedure was as follows: (i) amplify a portion of Adh1 and Adh2 genes with the locus-specific PCR primers; (ii) digest PCR products with restriction enzymes that distinguish different genomes; and (iii) run the digested products on 1.4% agarose gel, and photograph [22].
  • Sequence analysis of Mu1-hybridizing clones from a cDNA library of S3034 RNA indicated that these transcripts originated from the Adh1 locus and were produced by alternative processing of S3034 pre-mRNA [23].
  • We have identified a protein (GCBP-1) in nuclear extracts from maize suspension cell cultures that binds to specific sequences within the Anaerobic Responsive Element (ARE) of the maize Adh1 promoter [12].
  • Confocal scanning laser microscopy showed that the adh1 mutant formed thicker biofilm than the parent strain (210 microm and 140 microm, respectively) [24].


  1. Retinoic acid response element in the human alcohol dehydrogenase gene ADH3: implications for regulation of retinoic acid synthesis. Duester, G., Shean, M.L., McBride, M.S., Stewart, M.J. Mol. Cell. Biol. (1991) [Pubmed]
  2. Anaerobic tolerant null: a mutant that allows Adh1 nulls to survive anaerobic treatment. Lemke-Keyes, C.A., Sachs, M.M. J. Hered. (1989) [Pubmed]
  3. Introns increase gene expression in cultured maize cells. Callis, J., Fromm, M., Walbot, V. Genes Dev. (1987) [Pubmed]
  4. Physiologic and genomic analyses of nutrition-ethanol interactions during gestation: Implications for fetal ethanol toxicity. Shankar, K., Hidestrand, M., Liu, X., Xiao, R., Skinner, C.M., Simmen, F.A., Badger, T.M., Ronis, M.J. Exp. Biol. Med. (Maywood) (2006) [Pubmed]
  5. The paleontology of intergene retrotransposons of maize. SanMiguel, P., Gaut, B.S., Tikhonov, A., Nakajima, Y., Bennetzen, J.L. Nat. Genet. (1998) [Pubmed]
  6. The TATA box promoter region of maize Adh1 affects its organ-specific expression. Kloeckener-Gruissem, B., Vogel, J.M., Freeling, M. EMBO J. (1992) [Pubmed]
  7. Three-dimensional structures of the three human class I alcohol dehydrogenases. Niederhut, M.S., Gibbons, B.J., Perez-Miller, S., Hurley, T.D. Protein Sci. (2001) [Pubmed]
  8. Human stomach alcohol and aldehyde dehydrogenases (ALDH): a genetic model proposed for ALDH III isozymes. Yin, S.J., Cheng, T.C., Chang, C.P., Chen, Y.J., Chao, Y.C., Tang, H.S., Chang, T.M., Wu, C.W. Biochem. Genet. (1988) [Pubmed]
  9. Association of alcohol dehydrogenase genes with alcohol dependence: a comprehensive analysis. Edenberg, H.J., Xuei, X., Chen, H.J., Tian, H., Wetherill, L.F., Dick, D.M., Almasy, L., Bierut, L., Bucholz, K.K., Goate, A., Hesselbrock, V., Kuperman, S., Nurnberger, J., Porjesz, B., Rice, J., Schuckit, M., Tischfield, J., Begleiter, H., Foroud, T. Hum. Mol. Genet. (2006) [Pubmed]
  10. Molecular structure of the human alcohol dehydrogenase 1 gene. Matsuo, Y., Yokoyama, S. FEBS Lett. (1989) [Pubmed]
  11. Baboon alcohol dehydrogenase isozymes: purification and properties of liver class I ADH. Moderate alcohol consumption reduces liver class I and class II ADH activities. Holmes, R.S., Meyer, J., VandeBerg, J.L. Prog. Clin. Biol. Res. (1990) [Pubmed]
  12. The anaerobic responsive element contains two GC-rich sequences essential for binding a nuclear protein and hypoxic activation of the maize Adh1 promoter. Olive, M.R., Peacock, W.J., Dennis, E.S. Nucleic Acids Res. (1991) [Pubmed]
  13. Differential regulation of the alcohol dehydrogenase 1B (ADH1B) and ADH1C genes by DNA methylation and histone deacetylation. Dannenberg, L.O., Chen, H.J., Tian, H., Edenberg, H.J. Alcohol. Clin. Exp. Res. (2006) [Pubmed]
  14. GATA-2 and HNF-3beta regulate the human alcohol dehydrogenase 1A (ADH1A) gene. Dannenberg, L.O., Chen, H.J., Edenberg, H.J. DNA Cell Biol. (2005) [Pubmed]
  15. Characterization of Coturnix quail liver alcohol dehydrogenase enzymes. Nussrallah, B.A., Dam, R., Wagner, F.W. Biochemistry (1989) [Pubmed]
  16. Down-regulation of caffeic acid o-methyltransferase in maize revisited using a transgenic approach. Piquemal, J., Chamayou, S., Nadaud, I., Beckert, M., Barrière, Y., Mila, I., Lapierre, C., Rigau, J., Puigdomenech, P., Jauneau, A., Digonnet, C., Boudet, A.M., Goffner, D., Pichon, M. Plant Physiol. (2002) [Pubmed]
  17. Regulation of human alcohol dehydrogenase genes. Edenberg, H.J., Brown, C.J. Pharmacogenetics (1992) [Pubmed]
  18. Cloning and characterization of the human ADH4 gene. von Bahr-Lindström, H., Jörnvall, H., Höög, J.O. Gene (1991) [Pubmed]
  19. Class II alcohol dehydrogenase (ADH2)--adding the structure. Svensson, S., Strömberg, P., Sandalova, T., Höög, J. Chem. Biol. Interact. (2001) [Pubmed]
  20. Natural variants of pearl millet (Pennisetum typhoides) with altered levels of set II alcohol dehydrogenase activity. Banuett-Bourrillon, F. Biochem. Genet. (1982) [Pubmed]
  21. Dissociation-recombination of intergenic sunflower alcohol dehydrogenase isozymes and relative isozyme activities. Torres, A.M. Biochem. Genet. (1976) [Pubmed]
  22. Rapid and reliable identification of rice genomes by RFLP analysis of PCR-amplified Adh genes. Ge, S., Sang, T., Lu, B.R., Hong, D.Y. Genome (2001) [Pubmed]
  23. The Mu1 maize transposable element induces tissue-specific aberrant splicing and polyadenylation in two Adh1 mutants. Ortiz, D.F., Strommer, J.N. Mol. Cell. Biol. (1990) [Pubmed]
  24. Alcohol dehydrogenase restricts the ability of the pathogen Candida albicans to form a biofilm on catheter surfaces through an ethanol-based mechanism. Mukherjee, P.K., Mohamed, S., Chandra, J., Kuhn, D., Liu, S., Antar, O.S., Munyon, R., Mitchell, A.P., Andes, D., Chance, M.R., Rouabhia, M., Ghannoum, M.A. Infect. Immun. (2006) [Pubmed]
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