Abstract
Enzymes are defined from their catalytic activity and generally they have a specific function in cell metabolism. Mammalian alcohol dehydrogenase (ADH) was early isolated and classified (Vallee and Bazzone, 1983) and the function was stated as either to metabolize ethanol into acetaldehyde or to produce ethanol. In the mammals and especially in humans a large number of different ADHs have been identified, as different enzymes (classes), as different isozymes and as allelic forms (Jörnvall et al., this volume). For the different classes, solely class III ADH, glutathione-dependent formaldehyde dehydrogenase, has a specific function in the turnover of formaldehyde (Uotila and Koivusalo, 1986). Class I ADH, the main ethanol metabolizing enzyme in the liver, probably has an additional function in the metabolism of steroids and bile acids (human class I γγ Marschall et al., 1998) The extrahepatically expressed class IV ADH has been ascribed a function in the turnover of retinoids (Duester, 1998)
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References
Bücher, T. (1970) In: Pyridine nucleotide dependent dehydrogenases (Sund, H., ed. ) Springer Verl
Consalvi, V., Mårdh, G. and Vallee, B. L. (1986) Human alcohol dehydrogenases and serotonin metabolism, Bio-chem. Biophys. Res. Commun. 139, 1009–1016.
Davis, G. J., Carr, L. G., Hurley, T. D., Li, T.-K. and Bosron, W. F. (1994) Comparative roles of histidine 51 in human βjβ, and threonine in ππ alcohol dehydrogenases, Arch. Biochem. Biophys. 311, 307–312.
Deetz, J. S., Luehr, C. A., Vallée, B. L. (1984) Human liver alcohol dehydrogenase isozymes: Reduction of aldehyde and ketones, Biochemistry 23, 6822–6828.
Ditlow, C. C., Holmquist, B., Morelock, M. M. and Vallée, B. L. (1984) Physical and enzymatic properties of a class II alcohol dehydrogenase isozyme of human liver: π-ADH, Biochemistry 23, 6363–6368.
Duester G. (1998) Alcohol dehydrogenase as a critical mediator of retinoic acid synthesis from vitamin A in the mouse embryo, J. Nutrition. 128,459S–462S.
Duester, G., Farrés, J., Felder, M. R., Holmes, R., Höög, J.-O., Parés, X., Plapp, B. V., Yin, S.-J. and Jörnvall, H. (1998) Recommended nomenclature for the vertebrate alcohol dehydrogenase gene family, Submitted to FEBSLett
Eklund, H., Plapp, B. V., Samama, J.-R and Bränden, C.-I. (1992) Binding of substrate in a ternary complex of horse liver alcohol dehydrogenase, J. Biol. Chem. 257, 14349–14358.
Estonius, M., Danielsson, O., Karlsson, G, 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., Svensson, S. and Höög, J.-O. (1996) Alcohol dehydrogenase in human tissues. Localisation of transcripts coding for five classes of the enzyme, FEBS Lett. 397, 338–342.
Hjelmqvist, L., Estonius, M. and Jörnvall, H. (1995) The vertebrate alcohol dehydrogenase system: Variable class II type form elucidates separate stages of enzymogenesis, Proc. Natl. Acad. Sci. USA 92, 10905–10909.
Höög, J.-O. (1995) Cloning and characterization of a novel rat alcohol dehydrogenase of class II type, FEBS Lett. 368, 445–448.
Höög, J.-O., von Bahr-Lindström, H., Hedén, L.-O., Holmquist, B., Larsson, K., Hempel, J., Vallée, 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 π subunit, Biochemistry 26, 1926–1932.
Höög, J.-O. and Svensson, S. (1997) Mammalian class II alcohol dehydrogenase-a highly variable enzyme, In: Enzymology and molecular biology of carbonyl metabolism 6 (Weiner, H., Lindahl, R., Crabb, D. W. and Flynn, T. G., eds. ) Plenum Press, pp 303–311.
Li, T.-K., Bosron, W. F., Dafeldecker, W. P., Lange, L. G. and Vallée, B. L. (1977) Isolation of II-alcohol dehydrogenase of human liver: Is it a determinant of alcoholism? Proc. Natl. Acad. Sci. USA 74, 4378–43
Marschall, H.-U., Oppermann, U. C. T., Svensson, S., Nordling, E., Persson, B., Höög, J.-O and Jörnvall, H. (1998) Human liver alcohol dehydrogenase γγ isozyme: the sole cytosolic 3β-hydroxysteroid dehydrogenase of iso-bile acids, Biochemistry, in press.
Maskos, Z. and Winston, G. W. (1994) Mechanism of p-nitrosophenol reduction catalyzed by horse liver and human π-alcohol dehydrogenase (ADH), J. Biol. Chem. 269, 31579–31584.
Mârdh, G., Dingely, A. L., Auld, D. S. and Vallée, B. L. (1986) Human class II (π) alcohol dehydrogenase has a re-dox-specific function in norepinephrine metabolism, Proc. Natl. Acad. Sci. USA 83, 8908–8912.
Mârdh, G., Auld, D. S. and Vallée, B. L. (1987) Thyroid hormones selectively modulate human alcohol dehydrogenase isozyme catalyzed ethanol metabolism, Biochemistry 26, 7585–7588.
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.
Sellin, S., Holmquist, B., Mannervik, B. and Vallée, B. L. (1990) Oxidation and reduction of 4-hydroxyalkenals catalyzed by isozymes of human alcohol dehydrogenase, Biochemistry 30, 2514–2518.
Svensson, S., Lundsjö, A., Cronholm, T. and Höög, J.-O. (1996) Aldehyde dismutase activity of human liver alcohol dehydrogenase, FEBS Lett. 394, 217–220.
Svensson, S., Hedberg, J. J. and Höög, J.-O. (1998) Structural and functional divergence of class II alcohol dehydrogenase. Cloning and characterization of rabbit liver isoforms of the enzyme, Eur. J. Biochem. 251, 236–243.
Uotila, L. and Koivusalo, M. (1989) Glutathione-dependent oxidoreductases:formaldehyde dehydrogenase, In: Glutathione: Chemical, biochemical and medical aspects, part A (Dolphin, D., Poulson, R. and Avramovic, O., eds. ) John Wiley and sons, pp. 517–551.
Vallée, B. L. and Bazzone, T. J. (1983) Isozymes of human liver alcohol dehydrogenase, Isozyme 8, 219–244.
Yang, Z. N., Davies, G. J., Hurley, T. D., Stone, C. L., Li, T.-K. and Bosron, WF. (1994) Catalytic efficiency of human alcohol dehydrogenases for retinol oxidation and retinal reduction, Alcohol Clin. Exp. Res. 18, 587–591.
Yang, Z. N., Bosron, W. F. and Hurley, T. D. (1997) Structure of human χχalcoh°l dehydrogenase: A glutathione-dependent formaldehyde dehydrogenase, J. Mol. Biol. 265, 330–343.
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Höög, JO., Svensson, S., Strömberg, P., Brandt, M. (1999). Class II 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_40
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DOI: https://doi.org/10.1007/978-1-4615-4735-8_40
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