Abstract
The number of mammalian alcohol dehydrogenases (ADHs) has increased in recent years, with six classes currently being defined according to structural differences (Jörnvall & Höög, 1984; cf. Jörnvall et al., this volume). In the rat, a widely used model in studies on the metabolism of alcohol, three distinct forms have been characterized (Julià et al., 1987), while the human ADHs have been grouped earlier into three classes according to kinetic and electrophoretic properties (Vallee & Bazzone, 1983).
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References
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.
Chen, C.-S. and Yoshida, A., 1991, Enzymatic properties of the protein encoded by newly cloned human alcohol dehydrogenase ADH6 gene, Biochem. Biophys. Res. Commun. 181:743–747.
Danielsson, O., Eklund, H., and Jörnvall, H., 1993, The major piscine liver alcohol dehydrogenase has class-mixed properties in relation to mammalian alcohol dehydrogenases of classes I and III, Biochemistry 31:3751–3759.
Eklund, H., Nordström, B., Zeppezauer, E., Söderlund, G., Ohlsson, L, Boiwe, T., Söderberg, B.-O., horse liver alcohol dehydrogenase at 2.4 Å resolution, J. Mol. Biol. 102:27–59.
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.
Engeland, K., 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.
Estonius, M., Danielsson, O., Karlsson, C., Persson, H., Jörnvall, H., and Höög, J.-O., 1993, Distribution of alcohol and sorbitol dehydrogenases: Assessment of mRNAs in rat tissues, Eur. J. Biochem. 215:497–503.
Estonius, M., Höög, J.-O., Danielsson, O., and Jörnvall, H., 1994, Residues specific for class III alcohol dehydrogenase. Class transition and S-hydroxymethylglutathione binding. Site-directed mutagenesis of the human enzyme, Biochemistry, in press.
Hurley, T.D., Bosron, W.F., Hamilton, J.A., and Amzel, L.M., 1991, Structure of human b1b1 alcohol dehydrogenase: catalytic effects of non-active site substitutions, Proc. Natl. Acad. Sci. USA 88:8149–8154.
Hurley, T. and Bosron, W.F., 1992, Human alcohol dehydrogenase: dependence of secondary alcohol oxidation on the amino acids at positions 93 and 94, Biochem. Biophys. Res. Commun. 183:93–99.
Höög, J.-O., 1990, Mammalian class II alcohol dehydrogenase: Species and class comparisons at genomic and protein levels, in: Enzymology and Molecular Biology of Carbonyl Metabolism 3. Edited by H. Weiner, B. Wermuth, and D.W. Crabb, Plenum Press, New York, pp. 285–292.
Höög, J.-O., von Bahr-Lindström, H., Hedén, L.-O., Holmquist, B., Larsson, K., Hempel, J., Vallee, B.L., and Jörnvall, H., 1987, Structure of the class II enzyme of human liver alcohol dehydrogenase. Combined cDNA and protein sequence determination of the p-subunit, Biochemistry 26:1926–1932.
Höög, J.-O., Karlsson, C., Eklund, H., Shapiro, R., and Jörnvall, H., 1993, Site-directed mutagenesis of mammalian alcohol and sorbitol dehydrogenases map functional differences within the enzyme family, in: Enzymology and Molecular Biology of Carbonyl Metabolism 4. Edited by H. Weiner, D.W. Crabb, and T.G. Flynn, Plenum Press, New York, pp. 439–450.
Julia, P., Farrés, J., and Parés, X., 1987, Characterization of three isozymes of rat alcohol dehydrogenase. Tissue distribution and enzymatic properties, Eur. J. Biochem. 162:179–189.
Jörnvall, H. and Höög, J.-O, 1994, Nomenclature of alcohol dehydrogenases, Alcohol and Alcoholism, in press.
Jörnvall, H., Persson, B., and Jeffery, J., 1987, Characteristics of alcohol/polyol dehydrogenases. The zinc-containing long-chain alcohol dehydrogenases, Eur. J. Biochem. 167:195–201.
Jörnvall, H., von Bahr-Lindström, H., and Höög, J.-O., 1989, Alcohol dehydrogenases — structure, in: Human Metabolism of Alcohol vol. 2. Edited by R.D. Batt and K.E. Crow, CRC press, Boca Raton pp.43–64.
Koivusalo, M., Baumann, M., and Uotila, L., 1989, Evidence for the identity of glutathione-dependent formaldehyde and class III alcohol dehydrogenase, FEBS Lett. 257:105–109.
Li, T.-K., Bosron, W.F., Dafeldecker, W.P., Lange, L.G., and Vallee, B.L., 1977, Isolation of P-alcohol dehydrogenase of human liver: Is it a determinant of alcoholism? Proc. Natl. Acad. Sci. USA 74:4378–4381.
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.
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 ss-ADH reveals class IV to be variable and confirms the prescence of a fifth mammalian alcohol dehydrogenase class, FEBS Lett. 303:69–72.
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.
Persson, B., Bergman, T., Keung, W.M., Waldenström, U., Holmquist, B., Vallee, B.L., and Jörnvall, H., 1993, Basic features of class-I alcohol dehydrogenase: variable and constant segments coordinated by inter-class and intra-class variability. Conclusions from characterization of the alligator enzyme, Eur. J. Biochem. 216:49–56.
Sambrook, J., Fritsch, E.F., and Maniatis, T., 1989, in: Molecular Cloning: a laboratory manual, Cold Spring Harbor Laboratory, Cold Spring Harbor, New York.
Sanger, F., Nicklen, S., and Coulson, A.R., 1977, DNA sequencing with chain termination inhibitors, Proc. Natl. Acad. Sci. USA 74:5463–5467.
Sellin, S., Holmquist, B., Mannervik, B., and Vallee, B.L., 1991, Oxidation and reduction of 4-hydroxyalkenals catalyzed by isozymes of human alcohol dehydrogenase, Biochemistry 30:2514–2518.
Taylor, J.W., Ott, J., and Eckstein, F., 1985, The rapid generation of oligonucleotide-directed mutations at high frequency using phosphorothioate-modified DNA, Nucleic Acids Res. 13:8765–8785.
Uotila, L. and Koivusalo, M., 1989, Glutathione-dependent oxidoreductases: Formaldehyde dehydrogenase, in: Coenzymes and Cofactors, Glutathione. Chemical, Biochemical and Medical Aspects, vol III, part A. Edited by D. Dolphin et al, John Wiley & Sons, New York pp. 517–551.
Vallee, B.L. and Bazzone, T.J., 1983, Isozymes of human liver alcohol dehydrogenase, Isozymes 8:219–244.
Yasunami, C.C., Chen, C.-S., and Yoshida, A., 1991, A human alcohol dehydrogenase gene (ADH6) encoding an additional class of isozyme, Proc. Natl Acad. Sci. USA 88:7610–7614.
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.
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Höög, JO., Brandt, M. (1995). Mammalian Class VI Alcohol Dehydrogenase. In: Weiner, H., Holmes, R.S., Wermuth, B. (eds) Enzymology and Molecular Biology of Carbonyl Metabolism 5. Advances in Experimental Medicine and Biology, vol 372. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1965-2_43
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DOI: https://doi.org/10.1007/978-1-4615-1965-2_43
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