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.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
Jörnvall, H. and Höög, J.-O., 1995, Nomenclature of alcohol dehydrogenases, Alcohol and Alcoholism, 30, 153–161.
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.
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.
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.
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.
Vallee, B. L. and Bazzone, T. J., 1983, Isozymes of human liver alcohol dehydrogenase, Isozymes 8: 219–244.
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.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1995 Springer Science+Business Media New York
About this chapter
Cite this chapter
Hjelmqvist, L., Estonius, M., Jörnvall, H. (1995). Distinctive Class Relationships Within Vertebrate Alcohol Dehydrogenases. In: Atassi, M.Z., Appella, E. (eds) Methods in Protein Structure Analysis. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1031-8_37
Download citation
DOI: https://doi.org/10.1007/978-1-4899-1031-8_37
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4899-1033-2
Online ISBN: 978-1-4899-1031-8
eBook Packages: Springer Book Archive