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Distinctive Class Relationships Within Vertebrate Alcohol Dehydrogenases

  • Lars Hjelmqvist
  • Mats Estonius
  • Hans Jörnvall

Abstract

Mammalian alcohol dehydrogenases (ADH) constitute a well-studied enzyme system composed of sub-forms at different levels of multiplicity. The family has diverged into a number of different enzymes. At the next level (Fig. 1), fairly different forms (“classes”) of alcohol dehydrogenase, with distinct structural and enzymatic properties, occur. The subsequent level constitutes still more similar forms (“isozymes”) with gradual differences in properties and fewer residue exchanges.

Keywords

Gene Duplication Alcohol Dehydrogenase Variable Segment Subsequent Mutation Torpedo Electric Organ 
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.

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References

  1. 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
  2. Danielsson, O. and Jörnvall, H., 1992, “Enzymogenesis”: Classical liver alcohol dehydrogenase origin from the glutathione-dependent formaldehyde dehydrogenase line. Proc. Natl. Acad. Sci. USA 89:92479251.Google Scholar
  3. Danielsson, O., Atrian, S., Luque, T., Hjelmqvist, L., Gonzàlez-Duarte, R. and Jörnvall, H., 1994a, Fundamental molecular differences between alcohol dehydrogenase classes. Proc. Natl. Acad. Sci. USA 91: 49804984.Google Scholar
  4. Danielsson, O., Shafqat, J., Estonius, M., and Jörnvall, H., 1994b, Alcohol dehydrogenase class III contrasted to class I. Characterization of the cyclostome enzyme, existence of multiple forms as for the human enzyme, and distant cross-species hybridization, Eur. J. Biochem. 225: 1081–1088.PubMedCrossRefGoogle Scholar
  5. 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, Eue. J. Biochem. 193: 303–310.CrossRefGoogle Scholar
  6. El-Ahmad, M., Ramaswamy, S., Danielsson, O., Karlsson, C., Höög, J.-O., Eklund, H., and Jörnvall, H., 1995, Crystallizations of novel forms of alcohol dehydrogenase, in: Enzymology and Molecular Biology of Carbonyl Metabolism 5, Weiner, H., Holmes, R, and Flynn, T. G., eds, Plenum, New York, pp. 365–371.CrossRefGoogle Scholar
  7. Engeland, H., Höög, J.-O., Holmquist, B., Estonius, M., Jörnvall, H., and Vallee, B. L., 1993, Mutation of Arg-115 of human class III alcohol dehydrogenase, a binding site required for formaldehyde dehydrogenase activity and fatty acid activation, Proc. Natl. Acad. Sci. USA 90: 2491–2494.PubMedCrossRefGoogle Scholar
  8. Estonius, M., Höög, J.-O., Danielsson, O., and Jörnvall, H., 1994, Residues specific for class III alcohol dehydrogenase. Site-directed mutagenesis of the human enzyme. Biochemistry 33: 15080–15085.PubMedCrossRefGoogle Scholar
  9. 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 (aa-ADH) from human stomach. cDNA sequence and structure/function relationships. Eue. J. Biochem. 224: 549–557.CrossRefGoogle Scholar
  10. Höög, J.-O., Eklund, H., and Jörnvall, H., 1992, A single-residue exchange gives human recombinant (3(3 alcohol dehydrogenase yy isozyme properties, Eue. J. Biochem. 205: 519–526.CrossRefGoogle Scholar
  11. Jörnvall, H., Danielsson, O., Hjelmqvist, L., Persson, B., and Shafqat, J., 1995, The alcohol dehydrogenase system, in: Enzymology and Molecular Biology of Carbonyl Metabolism 5, Weiner, H., Holmes, R, and Flynn, T. G., eds, Plenum, New York, pp. 281–294.CrossRefGoogle Scholar
  12. Jörnvall, H. and Höög, J.-O., 1995, Nomenclature of alcohol dehydrogenases, Alcohol and Alcoholism, 30, 153–161.PubMedGoogle Scholar
  13. Kaiser, R., Holmquist, B., Vallee, B. L., and Jörnvall, H., 1989, Characterization of mammalian class III alcohol dehydrogenases, an enzyme less variable than the traditional liver enzyme of class I, Biochemistry 28: 8432–8438.PubMedCrossRefGoogle Scholar
  14. Koivusalo, M., Baumann, M., and Uotila, L., 1989, Evidence for the identity of glutathione-dependent formaldehyde dehydrogenase and class III alcohol dehydrogenase, FEBS Lett. 257: 105–109.PubMedCrossRefGoogle Scholar
  15. Parés, X., Cederlund, E., Moreno, A., Hjelmqvist, L., Farrés, J., and Jörnvall, H., 1994, Mammalian class IV alcohol dehydrogenase (stomach ADH): structure, origin and correlation with enzymology. Proc. Natl. Acad. Sci. USA 91: 1893–1897.PubMedCrossRefGoogle Scholar
  16. Persson, B., Zigler, J. S. Jr, and Jörnvall, H., 1994, A super-family of medium-chain dehydrogenases/reductases (MDR). Eur. J. Biochem. 226: 15–22.PubMedCrossRefGoogle Scholar
  17. Vallee, B. L. and Bazzone, T. J., 1983, Isozymes of human liver alcohol dehydrogenase, Isozymes 8: 219–244.PubMedGoogle Scholar
  18. Yang, Z. N., Davis, G. J., Hurley, T. D., Stone, C. L., Li, T.-K., and Bosron, W. F., 1993, Catalytic efficiency of human alcohol dehydrogenase for retinol oxidation and retinol reduction, Alcohol. Clin. Exp. Res. 17: 496.Google Scholar

Copyright information

© Springer Science+Business Media New York 1995

Authors and Affiliations

  • Lars Hjelmqvist
    • 1
  • Mats Estonius
    • 1
  • Hans Jörnvall
    • 1
  1. 1.Department of Medical Biochemistry and BiophysicsKarolinska InstitutetS-171 77 StockholmSweden

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