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Amphibian Alcohol Dehydrogenase

Purification and Characterization of Classes I and III from Rana perezi

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 463))

Abstract

Alcohol dehydrogenase (ADH) catalyses the reversible interconversion of a variety of alcohols and their corresponding aldehydes and ketones, and is widely distributed in organisms. It has been detected in all animals, in plants, and eukaryotic and prokaryotic microorganisms. In vertebrates the ADH system is complex, with at least seven different enzymatic classes (Jörnvall and Höög, 1995, Kedishvili et al., 1997). The study in sub- mammal species is of interest to understand the relationship between the classes found in mammals and the evolutionary origins of the present structures. Moreover, since the enzyme exhibits a wide substrate specificity, the comparative study of the enzymes from distant species may provide valuable information on the function of the enzyme, and how it may change among groups of vertebrates to adapt to different physiological needs.

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References

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • Bradford, M. M., 1976, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72P, 248–254.

    Article  Google Scholar 

  • 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.

    Article  PubMed  CAS  Google Scholar 

  • Danielsson, O., Eklund, H., and Jörnvall, H., 1992, The major piscine liver alcohol dehydrogenase has class-mixed properties in relation to mammal alcohol dehydrogenases of class I and III, Biochemistry 31, 3751–3759.

    Article  PubMed  CAS  Google Scholar 

  • 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, 9247–9251.

    Article  PubMed  CAS  Google Scholar 

  • Danielsson, O., Shafqat, J., Estonius, M. and Jörnvall, H., 1994, Alcohol dehydrogenase class III contrasted to class I: Characterization of the cyclostome enzyme, the existence of multiple forms as for the human enzyme, and distant cross-species hybridization. Eur. J. Biochem. 225, 1081–1088.

    Article  PubMed  CAS  Google Scholar 

  • Danielsson, O., Shafqat, J., Estonius, M., El-Ahmad, M., and Jörnvall, H., 1996, Isozyme multiplicity with anomalous dimer patterns in a class III alcohol dehydrogenase. Effects on the activity and quaternary structure of residue exchanges at“nonfunctional”sites in a native protein, Biochemistry 35, 14561–14568.

    Article  PubMed  CAS  Google Scholar 

  • Estonius, M., Karlsson, C, Fox, E. A., Höög, J.-O., Holmquist, B., Vallée, B. L., Davidson, W. S. and Jörnvall, H., 1990, Avian alcohol dehydrogenase: The chicken liver enzyme. Primary structure, cDNA cloning, and relationships to other alcohol dehydrogenases, Eur. J. Biochem. 194, 593–602.

    Article  PubMed  CAS  Google Scholar 

  • Estonius, M., Hjelmqvist, L. and Jörnvall, H., 1994, Diversity of vertebrate class I alcohol dehydrogenase. Mammalian and non-mammalian enzyme functions correlated through the structure of a ratite enzyme, Eur. J. Biochem. 224, 373–378.

    Article  PubMed  CAS  Google Scholar 

  • 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 (ss-ADH) from human stomach. cDNA sequence and structure/function relationships, Eur. J. Biochem: 224 549–557.

    Article  PubMed  Google Scholar 

  • Fernández, M. R., Jörnvall, H., Moreno, A., Kaiser, R., and Parés, X., 1993, Cephalopod alcohol dehydrogenase: purification and enzymatic characterization, FEBS Lett. 328, 235–238.

    Article  Google Scholar 

  • Fernández, M. R., Biosca, J. A., Norin, A., Jörnvall, H., and Parés, X., 1995, Class III alcohol dehydrogenase from Saccharomyces cerevisiae: Structural and enzymatic features differ toward the human/mammalian forms in a manner consistent with functional needs in formaldehyde detoxication, FEBS Lett. 370, 23–26.

    Article  PubMed  Google Scholar 

  • Fernández, M. R., Biosca, J. A., Martinez, M. C., Achkor, H., Farrés, J., and Parés, X., 1997, Formaldehyde dehydrogenase from yeast and plant. Implications for the general functional and structural significance of class III alcohol dehydrogenase, Adv. Exp. Med. Biol 414, 373–381.

    Article  PubMed  Google Scholar 

  • Hjelmqvist, H., Metsis, M., Persson, H., Höög, J.-O., McLennan, J. and Jörnvall, H., 1995, Alcohol dehydrogenase of class I: kiwi liver enzyme, parallel evolution in separate vertebrate lines, and correlation withS rRNA patterns, FEBS Lett. 367, 306–310.

    Article  PubMed  CAS  Google Scholar 

  • Hjelmqvist, L., Shafqat, J., Siddiqi, A. R. and Jörnvall, H., 1996, Linking of isozyme and class variability patterns in the emergence of novel alcohol dehydrogenase functions: Characterization of isozymes in Uromastix hardwickii. Eur. J. Biochem. 236, 563–570.

    Article  CAS  Google Scholar 

  • Jörnvall, H., and Höög, J.-O., 1995, Nomenclature of alcohol dehydrogenases, Alcohol Alcohol 30, 153–161.

    PubMed  Google Scholar 

  • Julià, P., Parés, X., and Jörnvall, H., 1988, Rat liver alcohol dehydrogenase of class III. Primary structure, functional consequences and relationships to other alcohol dehydrogenases, Eur. J. Biochem. 172, 73–83.

    Article  PubMed  Google Scholar 

  • Kaiser, R., Nussrallah, B. A., Dam, R., Wagner, F. W., and Jörnvall, H., 1990, Avian alcohol dehydrogenase. Characterization of the quail enzyme, functional interpretations, and relationships to the different classes of mammalian alcohol dehydrogenase, Biochemistry 29, 8365–8371.

    Article  PubMed  CAS  Google Scholar 

  • Kedishvili, N. Y., Gough, W. H., Chernoff, E. A. G., Hurley, T. D., Stone, C. L., Bowman, K. D., Popov, K. M., Bosron, W. F., and Li, T.-K. (1997) cDNA sequence and catalytic properties of a chick embryo alcohol dehydrogenase that oxidizes retinol andβ,a-Hydroxysteroids, J. Biol. Chem. 272, 7494–7500.

    Article  PubMed  CAS  Google Scholar 

  • Moreno, A., and Parés, X., 1991, Purification and characterization of a new alcohol dehydrogenase from human stomach, J. Biol. Chem. 266, 1128–1133.

    PubMed  CAS  Google Scholar 

  • Moulis, J.-M., Holmquist, B., and Vallée, B. L., 1991, Hydrophobic anion activation of human liver χχ alcohol dehydrogenase, Biochemistry 30, 5743–5749.

    Article  PubMed  CAS  Google Scholar 

  • Nussrallah, B., Dam, R. and Wagner, F. W., 1989, Characterization of Coturnix quail liver alcohol dehydrogenase enzymes. Biochemistry 28, 6245–6251.

    Article  PubMed  CAS  Google Scholar 

  • Peralba, J. M., Cederlund, E., Crosas, B., Moreno, A., Julià, P., Martinez, S. E., Persson, B., Farrés, J., Parés, X., and Jörnvall, H., 1998, Structural and enzymatic properties of a gastric NADP(H)-dependent and retinal-active alcohol dehydrogenase (submitted).

    Google Scholar 

  • Persson, B., Bergman, T., Keung, W.-M., Waldenström, U., Holmquist, B., Vallée, B. L., and Jörnvall, H., 1993, Basic features of class I alcohol dehydrogenase. Variable and constant segments coordinated by inter-class and in-tra-class variability. Conclusions from characterization of the alligator enzyme, Eur. J. Biochem. 216, 49–56.

    Article  PubMed  CAS  Google Scholar 

  • Ramaswamy, S., El-Ahmad, M., Danielsson, O., Jörnvall, H., and Eklund, H., 1996, Crystal structure of cod liver class I alcohol dehydrogenase: Substrate pocket and structurally variable segments, Protein Science 5, 663–671.

    Article  PubMed  CAS  Google Scholar 

  • Wesolowski, M. H., and Lyerla, T. A., 1979, The developmental appearance of hexokinase and alcohol dehydrogenase in the Xenopus laevis, J. Exp. Zool. 210, 211–220.

    CAS  Google Scholar 

  • Wesolowski, M. H. and Lyerla, T. A., 1983, Alcohol dehydrogenase isozymes in the clawed frog, Xenopus laevis. Biochem. Genet. 21, 1003–1017.

    Article  CAS  Google Scholar 

  • Xie, P., Parsons, S. H., Speckhard, D. C., Bosron, WE, and Hurley T. D., 1997, X-ray structure of human class IV GG alcohol dehydrogenase. Structural basis for substrate specificity, J. Biol. Chem. 30, 18558–18563.

    Article  Google Scholar 

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© 1999 Springer Science+Business Media New York

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Peralba, J.M., Crosas, B., Martinez, S.E., Julià, P., Farrés, J., Parés, X. (1999). Amphibian Alcohol Dehydrogenase. In: Weiner, H., Maser, E., Crabb, D.W., Lindahl, R. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 7. Advances in Experimental Medicine and Biology, vol 463. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-4735-8_42

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  • DOI: https://doi.org/10.1007/978-1-4615-4735-8_42

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-7146-5

  • Online ISBN: 978-1-4615-4735-8

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