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Gene Review

Adh1  -  alcohol dehydrogenase 1 (class I)

Mus musculus

Synonyms: ADH-A2, ADH-AA, AI194826, Adh-1, Adh-1-t, ...
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Disease relevance of Adh1


Psychiatry related information on Adh1


High impact information on Adh1


Chemical compound and disease context of Adh1


Biological context of Adh1


Anatomical context of Adh1


Associations of Adh1 with chemical compounds

  • Here we have examined mice for the effect of either acute ethanol intoxication or Adh1 gene disruption on RA synthesis and degradation [21].
  • RA produced in Adh1-null mutant mice following a 50-mg/kg dose of retinol was reduced 82% relative to wild-type mice, thus similar to wild-type mice pretreated with ethanol [21].
  • Redundant roles for Adh1 and Adh4 in retinoic acid production may explain the apparent normal development of mutant mice [22].
  • Thus, Adh1 and Adh4 demonstrate overlapping functions in ethanol and retinol metabolism in vivo, whereas Adh3 plays no role with these substrates but instead functions in formaldehyde metabolism [22].
  • Whereas Adh1 plays a dominant role in the first step of the clearance pathway (oxidation of retinol to retinaldehyde), it is unknown what controls the second step (oxidation of retinaldehyde to RA) [1].

Physical interactions of Adh1


Enzymatic interactions of Adh1


Regulatory relationships of Adh1

  • Cosmids containing either 7 kb of upstream and 21 kb of downstream or 12 kb of upstream and 23 kb of downstream sequence flanking genetically marked Adh1 additionally promotes seminal vesicle expression suggesting downstream or intragenic sequence controls expression in this tissue [26].

Other interactions of Adh1

  • Genetic evidence that retinaldehyde dehydrogenase Raldh1 (Aldh1a1) functions downstream of alcohol dehydrogenase Adh1 in metabolism of retinol to retinoic acid [1].
  • Electrophoretic polymorphisms for stomach alcohol dehydrogenase (ADH-C2) and kidney L-alpha-hydroxyacid oxidase (HAOX-B4) have been identified in an Asian subspecies of mouse, Musmusculus castaneous [27].
  • An electrophoretic variant previously reported for the stomach isozyme of alcohol dehydrogenase (ADH-C2) in inbred strains of Mus musculus (Holmes, 1977) has been used to localize the gene encoding this enzyme (Adh-3) on chromosome 3 near Va (varitint) (9.6 +/- 3.6% recombinants) [15].
  • Ontogenetic analyses demonstrated that ADH-B2 is present throughout development from late fetal stages in stomach, liver, and kidney; similar results were found for ADH-C2 in developing kidney and stomach extracts, whereas ADH-A2 exhibited high activity in liver extracts after 3 weeks of age in both sexes and in male kidney extracts after 6 weeks [15].
  • Ethanol-induced sleep was significantly longer only in Adh1 -/- mice [22].

Analytical, diagnostic and therapeutic context of Adh1

  • Gene targeting was used to create knockout mice for either Adh1 or Adh4 [14].
  • Elimination of [2H]ethanol in vivo as studied by gas chromatography/mass spectrometry occurred at about half the rate in deer mice reported to lack alcohol dehydrogenase (ADH-) compared with ADH+ deer mice and exhibited kinetic isotope effects on Vmax and Km (D(V/K] of 2.2 +/- 0.1 and 3.2 +/- 0.8 in the two strains, respectively [18].
  • Using a panel of hybrid clones segregating rat chromosomes, and Southern blot analysis, alpha 1-AT (PI), PEPCK, ADH and FDP are assigned to rat Chromosomes (Chr) 6, 3, 2 and 17, respectively [28].
  • Overall, the relative expression of ADH and Zn-Cu SOD were higher in treatment groups than in positive controls; whereas, the relative expression of GPX5 was higher in positive control groups than in treatment groups [29].
  • Analysis of genetic crosses and recombinant inbred lines confirms that a single genetic locus, designated Adh-1-t, with additive alleles has a major effect in controlling the temporal difference in enzyme activity between strains [30].


  1. Genetic evidence that retinaldehyde dehydrogenase Raldh1 (Aldh1a1) functions downstream of alcohol dehydrogenase Adh1 in metabolism of retinol to retinoic acid. Molotkov, A., Duester, G. J. Biol. Chem. (2003) [Pubmed]
  2. Purification, characterization, and partial sequence of the glutathione-dependent formaldehyde dehydrogenase from Escherichia coli: a class III alcohol dehydrogenase. Gutheil, W.G., Holmquist, B., Vallee, B.L. Biochemistry (1992) [Pubmed]
  3. Overexpression of alcohol dehydrogenase exacerbates ethanol-induced contractile defect in cardiac myocytes. Duan, J., McFadden, G.E., Borgerding, A.J., Norby, F.L., Ren, B.H., Ye, G., Epstein, P.N., Ren, J. Am. J. Physiol. Heart Circ. Physiol. (2002) [Pubmed]
  4. Cardiac overexpression of alcohol dehydrogenase exacerbates cardiac contractile dysfunction, lipid peroxidation, and protein damage after chronic ethanol ingestion. Hintz, K.K., Relling, D.P., Saari, J.T., Borgerding, A.J., Duan, J., Ren, B.H., Kato, K., Epstein, P.N., Ren, J. Alcohol. Clin. Exp. Res. (2003) [Pubmed]
  5. Alcohol metabolism in Helicobacter pylori-infected stomach. Roine, R.P., Salmela, K.S., Salaspuro, M. Ann. Med. (1995) [Pubmed]
  6. Metabolic basis of ethanol-induced hepatic and pancreatic injury in hepatic alcohol dehydrogenase deficient deer mice. Bhopale, K.K., Wu, H., Boor, P.J., Popov, V.L., Ansari, G.A., Kaphalia, B.S. Alcohol (2006) [Pubmed]
  7. Inhibitory effects of butylated hydroxyanisole on methylazoxymethanol acetate-induced neoplasia of the large intestine and on nicotinamide adenine dinucleotide-dependent alcohol dehydrogenase activity in mice. Wattenberg, L.W., Sparnins, V.L. J. Natl. Cancer Inst. (1979) [Pubmed]
  8. Stimulation of retinoic acid production and growth by ubiquitously expressed alcohol dehydrogenase Adh3. Molotkov, A., Fan, X., Deltour, L., Foglio, M.H., Martras, S., Farrés, J., Parés, X., Duester, G. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  9. Tissue-specific genetic variation in the level of mouse alcohol dehydrogenase is controlled transcriptionally in kidney and posttranscriptionally in liver. Tussey, L., Felder, M.R. Proc. Natl. Acad. Sci. U.S.A. (1989) [Pubmed]
  10. Excessive vitamin A toxicity in mice genetically deficient in either alcohol dehydrogenase Adh1 or Adh3. Molotkov, A., Fan, X., Duester, G. Eur. J. Biochem. (2002) [Pubmed]
  11. Distinct retinoid metabolic functions for alcohol dehydrogenase genes Adh1 and Adh4 in protection against vitamin A toxicity or deficiency revealed in double null mutant mice. Molotkov, A., Deltour, L., Foglio, M.H., Cuenca, A.E., Duester, G. J. Biol. Chem. (2002) [Pubmed]
  12. Hepatotoxicity due to allyl alcohol in deermice depends on alcohol dehydrogenase. Belinsky, S.A., Bradford, B.U., Forman, D.T., Glassman, E.B., Felder, M.R., Thurman, R.G. Hepatology (1985) [Pubmed]
  13. Organization of six functional mouse alcohol dehydrogenase genes on two overlapping bacterial artificial chromosomes. Szalai, G., Duester, G., Friedman, R., Jia, H., Lin, S., Roe, B.A., Felder, M.R. Eur. J. Biochem. (2002) [Pubmed]
  14. Genetic dissection of retinoid dehydrogenases. Duester, G. Chem. Biol. Interact. (2001) [Pubmed]
  15. Genetics and ontogeny of alcohol dehydrogenase isozymes in the mouse: evidence for a cis-acting regulator gene (Adt-i) controlling C2 isozyme expression in reproductive tissues and close linkage of Adh-3 and Adt-i on chromosome 3. Holmes, R.S. Biochem. Genet. (1979) [Pubmed]
  16. Alcohol dehydrogenase isozymes in the mouse: genetic regulation, allelic variation among inbred strains and sex differences of liver and kidney A2 isozyme activity. Holmes, R.S., Duley, J.A., Imai, S. Animal blood groups and biochemical genetics. (1982) [Pubmed]
  17. Cloning of the mouse class IV alcohol dehydrogenase (retinol dehydrogenase) cDNA and tissue-specific expression patterns of the murine ADH gene family. Zgombić-Knight, M., Ang, H.L., Foglio, M.H., Duester, G. J. Biol. Chem. (1995) [Pubmed]
  18. Dehydrogenase-dependent ethanol metabolism in deer mice (Peromyscus maniculatus) lacking cytosolic alcohol dehydrogenase. Reversibility and isotope effects in vivo and in subcellular fractions. Norsten, C., Cronholm, T., Ekström, G., Handler, J.A., Thurman, R.G., Ingelman-Sundberg, M. J. Biol. Chem. (1989) [Pubmed]
  19. Expression patterns of class I and class IV alcohol dehydrogenase genes in developing epithelia suggest a role for alcohol dehydrogenase in local retinoic acid synthesis. Ang, H.L., Deltour, L., Zgombić-Knight, M., Wagner, M.A., Duester, G. Alcohol. Clin. Exp. Res. (1996) [Pubmed]
  20. Evidence that catalase is a major pathway of ethanol oxidation in vivo: dose-response studies in deer mice using methanol as a selective substrate. Bradford, B.U., Seed, C.B., Handler, J.A., Forman, D.T., Thurman, R.G. Arch. Biochem. Biophys. (1993) [Pubmed]
  21. Retinol/ethanol drug interaction during acute alcohol intoxication in mice involves inhibition of retinol metabolism to retinoic acid by alcohol dehydrogenase. Molotkov, A., Duester, G. J. Biol. Chem. (2002) [Pubmed]
  22. Metabolic deficiencies in alcohol dehydrogenase Adh1, Adh3, and Adh4 null mutant mice. Overlapping roles of Adh1 and Adh4 in ethanol clearance and metabolism of retinol to retinoic acid. Deltour, L., Foglio, M.H., Duester, G. J. Biol. Chem. (1999) [Pubmed]
  23. Amyloid beta -peptide-binding alcohol dehydrogenase is a component of the cellular response to nutritional stress. Du Yan, S., Zhu, Y., Stern, E.D., Hwang, Y.C., Hori, O., Ogawa, S., Frosch, M.P., Connolly, E.S., McTaggert, R., Pinsky, D.J., Clarke, S., Stern, D.M., Ramasamy, R. J. Biol. Chem. (2000) [Pubmed]
  24. The role of alcohol dehydrogenase in retinoic acid homeostasis and fetal alcohol syndrome. Shean, M.L., Duester, G. Alcohol and alcoholism (Oxford, Oxfordshire). Supplement. (1993) [Pubmed]
  25. The oxidation of 9-cis-retinol: a possible synthesis pathway for 9-cis-retinoic acid. Wolf, G. Nutr. Rev. (2000) [Pubmed]
  26. Distal and proximal cis-linked sequences are needed for the total expression phenotype of the mouse alcohol dehydrogenase 1 (Adh1) gene. Szalai, G., Xie, D., Wassenich, M., Veres, M., Ceci, J.D., Dewey, M.J., Molotkov, A., Duester, G., Felder, M.R. Gene (2002) [Pubmed]
  27. The genetics of alpha-hydroxyacid oxidase and alcohol dehydrogenase in the mouse: evidence for multiple gene loci and linkage between Hao-2 and Adh-3. Holmes, R.S. Genetics (1977) [Pubmed]
  28. Assignment of the rat genes coding for alpha 1-antitrypsin (PI), phosphoenolpyruvate carboxykinase (PEPCK), alcohol dehydrogenase (ADH), and fructose-1,6-bisphosphatase (FDP). Fulchignoni-Lataud, M.C., Szpirer, J., Levan, G., Weiss, M.C. Mamm. Genome (1992) [Pubmed]
  29. Effect of Evodiae fructus extracts on gene expressions related with alcohol metabolism and antioxidation in ethanol-loaded mice. Cho, M.H., Shim, S.M., Lee, S.R., Mar, W., Kim, G.H. Food Chem. Toxicol. (2005) [Pubmed]
  30. Genetic and developmental regulation of mouse liver alcohol dehydrogenase. Balak, K.J., Keith, R.H., Felder, M.R. J. Biol. Chem. (1982) [Pubmed]
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