Advertisement

Human and Rat Class IV Alcohol Dehydrogenases

Correlations of Primary Structures with Enzymatic Properties
  • Jaume Farrés
  • Alberto Moreno
  • Bernat Crosas
  • Ella Cederlund
  • Abdellah Allali-Hassani
  • Josep M. Peralba
  • Lars Hjelmqvist
  • Hans Jörnvall
  • Xavier Parés
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 372)

Abstract

Mammalian alcohol dehydrogenase (ADH, EC 1.1.1.1) is a complex enzymatic system composed of multiple molecular forms, which have been grouped into classes according to their enzymatic and structural characteristics. In addition to the three classes (I-III) early recognized (Vallee and Bazzone, 1983), more recent studies have led to the identification of three more classes: class IV (Parés et al., 1990, Parés et al., 1992), class V (Yasunami et al., 1991), and class VI (Zheng et al., 1993).

Keywords

Alcohol Dehydrogenase Aldehyde Dehydrogenase Amino Acid Exchange Human Class Coenzyme Binding 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Boleda, M.D., Julià, P., Moreno, A., and Parés, X. (1989) Role of extrahepatic alcohol dehydrogenase in rat ethanol metabolism, Arch. Biochem. Biophys. 274, 74–81.PubMedCrossRefGoogle Scholar
  2. Boleda, M.D., Saubi, N., Farrés, J., and Parés, X. (1993) Physiological substrates for rat alcohol dehydrogenase classes: Aldehydes of lipid peroxidation, ω-hydroxyfatty acids, and retinoids, Arch. Biochem. Biophys. 307, 85–90.PubMedCrossRefGoogle Scholar
  3. Bosron, W.F., Magnes, L.J., and Li, T.-K. (1983) Kinetic and electrophoretic properties of native and recombined isoenzymes of human liver alcohol dehydrogenase, Biochemistry 22 1852–1857.PubMedCrossRefGoogle Scholar
  4. Burnell, J.C., and Bosron, W.F. (1989) Genetic polymorphism of human liver alcohol dehydrogenase and kinetic properties of the isoenzymes, in Human metabolism of alcohol, vol. II (Crow, K.E. and Batt, R.D., eds.), CRC Press, Boca Raton, Florida, 1989, pp. 65–75.Google Scholar
  5. Cederlund, E., Peralba, J.M., Parés, X., and Jörnvall, H. (1991) Amphibian alcohol dehydrogenase, the major frog liver enzyme. Relationships to other forms and assessment of an early gene duplication separating vertebrate class I and class III alcohol dehydrogenases, Biochemistry 30, 2811–2816.PubMedCrossRefGoogle Scholar
  6. Eklund, H., Samama, J.P., and Jones, T.A. (1984) Crystallographic investigations of nicotinamide adenine dinucleotide binding to horse liver alcohol dehydrogenase, Biochemistry 23, 5982–5996.PubMedCrossRefGoogle Scholar
  7. Eklund, H., Müller-Wille, P., Horjales, E., Futer, O., Holmquist, B., Vallee, B.L., Höög, J.-O., Kaiser, R., and Jörnvall, H. (1990) Comparison of three classes of human liver alcohol dehydrogenase. Emphasis on different substrate-binding pockets, Eur. J. Biochem. 193, 303–310.PubMedCrossRefGoogle Scholar
  8. Farrés, J., Moreno, A., Crosas, B., Peralba, J.M., Allali-Hassani, A., Hjelmqvist, L., Jörnvall, H., and Parés, X. (1994) Alcohol dehydrogenase of class IV (σσ-ADH) from human stomach: cDNA sequence and structure/function relationships, Eur. J. Biochem. 224, 549–557.PubMedCrossRefGoogle Scholar
  9. Holmes, R.S. (1988) Alcohol dehydrogenases and aldehyde dehydrogenases of anterior eye tissues from humans and other mammals, in Biomedical and Social Aspects of Alcohol and Alcoholism (Kuriyama, K., Takada, A., and Ishii, H., eds.), Elsevier Science Publishers, New York, pp. 51–57.Google Scholar
  10. Höög, J.-O., Hedén, L.-O., Larsson, K., Jörnvall, H., and von Bahr Lindström, H. (1986) The γ1 and γ2 subunits of human liver alcohol dehydrogenase. cDNA structures, two amino acid replacements, and compatibility with changes in the enzymatic properties, Eur. J. Biochem. 159, 215–218.PubMedCrossRefGoogle Scholar
  11. Hurley, T.D., Edenberg, H.J., and Bosron, W.F. (1990) Expression and kinetic characterization of variants of human β1β1 alcohol dehydrogenase containing substitutions at amino acid 47, J. Biol. Chem. 265, 16366–16372.PubMedGoogle Scholar
  12. Hurley, T.D., Bosron, W.F., Hamilton, J.A., and Amzel, L.M. (1991) Structure of human β1βl alcohol dehydrogenase: Catalytic effects of non-active-site substitutions, Proc. Natl. Acad. Sci. USA 88, 8149–8153.PubMedCrossRefGoogle Scholar
  13. Jörnvall, H., Persson, B., and Jörnvall, H. (1993) Variability patterns of dehydrogenases versus peptide hormones and proteases/antiproteases, FEBS Lett. 335, 69–72.PubMedCrossRefGoogle Scholar
  14. Julià, P., Farrés, J., and Parés, X. (1987) Characterization of three isoenzymes of rat alcohol dehydrogenase. Tissue distribution and physical and enzymatic properties, Eur. J. Biochem. 162, 179–189.PubMedCrossRefGoogle Scholar
  15. Kedishvili, N.Y., Stone, C.L., Thomasson, H.R., Carr, L.G., Edenberg, H.J., Bosron, W.F., and Li, T.-K. (1994) Alcohol. Clin. Exp. Res. 18, 16A.Google Scholar
  16. Koivusalo, M., Baumann, M., and Uotila, L. (1989) FEBS Lett. 257, 105–109.PubMedCrossRefGoogle Scholar
  17. Moreno, A. and Parés, X. (1991) Purification and characterization of a new alcohol dehydrogenase from human stomach, J. Biol. Chem. 266, 1128–1133.PubMedGoogle Scholar
  18. Moreno, A., Parés, A., Ortiz, J., Enriquez, J., and Parés, X. (1994) Alcohol dehydrogenase from human stomach. Variability in normal mucosa and effect of age, gender, ADH3 phenotype and gastric region, Alcohol Alcohol., in press.Google Scholar
  19. Parés, X., Moreno, A., Cederlund, E., Höög, J.-O., and Jörnvall, H. (1990) Class IV mammalian alcohol dehydrogenase. Structural data of the rat stomach enzyme reveal a new class well separated from those already characterized, FEBS Lett. 277, 115–118.PubMedCrossRefGoogle Scholar
  20. Parés, X., Cederlund, E., Moreno, A., Saubi, N., Höög, J.-O., and Jörnvall, H. (1992) Class IV alcohol dehydrogenase (the gastric enzyme). Structural analysis of human σσ-ADH reveals class IV to be variable and confirms the presence of a fifth mammalian alcohol dehydrogenase class, FEBS Lett. 303, 69–72.PubMedCrossRefGoogle Scholar
  21. Parés, X., Cederlund, E., Moreno, A., Hjelmqvist, L., Farrés, J., and Jörnvall, H. (1994) Mammalian class IV alcohol dehydrogenase (stomach alcohol dehydrogenase): Structure, origin, and correlation with enzymology, Proc. Natl. Acad. Sci. USA 91, 1893–1897.PubMedCrossRefGoogle Scholar
  22. Parés, X. and Farrés, J. (1995) Alcohol and aldehyde dehydrogenases in the gastrointestinal tract, in Ethanol and the Gastrointestinal Tract: Mechanisms in Disease (Preedy, V.R. and Watson, R.R., eds.) CRC Press, in press.Google Scholar
  23. Satre, M.A., Agombi-Knight, M., and Duester, G. (1994) The complete structure of human class IV alcohol dehydrogenase (retinol dehydrogenase) determined from the ADH7 gene, J. Biol. Chem. 269, 15606–15612.PubMedGoogle Scholar
  24. Stone, C.L., Thomasson, H.R., Bosron, W.F., and Li, T.-K. (1993) Purification and partial amino acid sequence of a high-activity human stomach alcohol dehydrogenase, Alcohol. Clin. Exp. Res. 17, 911–918.PubMedCrossRefGoogle Scholar
  25. Vallee, B.L. and Bazzone, T.J. (1983) Isozymes of human liver alcohol dehydrogenase, Isozymes: Curr. Top. Biol. Med. Res. 8, 219–244.Google Scholar
  26. Yang, Z.N., Davis, G.J., Hurley, T.D., Stone, C.L., Li, T.-K., and Bosron, W.F. (1994) Catalytic efficiency of human alcohol dehydrogenases for retinol oxidation and retinal reduction, Alcohol. Clin. Exp. Res. 17, 496.Google Scholar
  27. Yasunami, M., Chen, C.-S., and Yoshida, A. (1991) A human alcohol dehydrogenase gene (ADH 6) encoding an additional class of isozyme, Proc. Natl. Acad. Sci. USA 88, 7610–7614.PubMedCrossRefGoogle Scholar
  28. Yin, S.-J., Wang, M.-F., Liao, C.-S., Chen, C-M., and Wu, C.-W. (1990) Identification of a human stomach alcohol dehydrogenase with distinctive kinetic properties, Biochem. Int. 22, 829–835.PubMedGoogle Scholar
  29. Yin, S.-J., Vagelopoulos, N., Wang, S.-L., and Jörnvall, H. (1991) Structural features of stomach aldehyde dehydrogenase distinguish dimeric aldehyde dehydrogenase as a ‘variable’ enzyme. ‘Variable’ and ‘constant’ enzymes within the alcohol and aldehyde dehydrogenase families, FEBS Lett. 283, 85–88.PubMedCrossRefGoogle Scholar
  30. Yokoyama, H., Baraona, E., and Lieber, C.S. (1994) Molecular cloning of cDNA of human class IV ADH. Submission to the GenBank database (accession number L33179).Google Scholar
  31. Zheng, Y.-W., Bey, M., Liu, H., and Felder, M.R. (1993) Molecular basis of the alcohol dehydrogenase-negative deer mouse. Evidence for deletion of the gene for class I enzyme and identification of a possible new enzyme class, J. Biol. Chem. 268, 24933–24939.PubMedGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1995

Authors and Affiliations

  • Jaume Farrés
    • 1
  • Alberto Moreno
    • 1
  • Bernat Crosas
    • 1
  • Ella Cederlund
    • 2
  • Abdellah Allali-Hassani
    • 1
  • Josep M. Peralba
    • 1
  • Lars Hjelmqvist
    • 2
  • Hans Jörnvall
    • 2
  • Xavier Parés
    • 1
  1. 1.Department of Biochemistry and Molecular Biology, Faculty of SciencesUniversitat Autònoma de BarcelonaBellateraSpain
  2. 2.Department of Medical Biochemistry and BiophysicsKarolinska InstitutetStockholmSweden

Personalised recommendations