Skip to main content

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 372))

Abstract

Alcohol dehydrogenases of different types are common enzymes in nature. Two of these families, the medium-chain dehydrogenase/reductase family, MDR, and the shortchain dehydrogenase/reductase family, SDR, are well studied and known since long, but have experienced a recent “explosion” of new knowledge, extension and importance. The MDR family includes the classical zinc-containing liver alcohol dehydrogenases encompassing the classes of human liver alcohol dehydrogenase, while the SDR family includes the Drosophila alcohol dehydrogenase, which has shorter subunits, no similar metal requirements, other sub-domain arrangements with different structural relationships, and other subunit interactions.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 39.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 54.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Bauer, A.J., Rayment, I., Frey, P.A. and Holden, H.M., 1992, The molecular structure of UDP-galactose 4-epimerase from Escherichia coli determined at 2.5 Å resolution. Proteins 12:372–381.

    Article  CAS  PubMed  Google Scholar 

  • Bonnichsen, R.K. and Wassén, A.M., 1948, Crystalline alcohol dehydrogenase from horse liver. Arch. Biochem. Biophys. 18:361–363.

    CAS  Google Scholar 

  • Borrás, X, Persson, B. and Jömvall, H., 1989, Eye lens ζ-crystallin relationships to the family of “long-chain” alcohol/polyol dehydrogenases. Protein trimming and conservation of stable parts. Biochemistry 28:6133–6139.

    Article  PubMed  Google Scholar 

  • Brändén, C.-I., Jörnvall, H., Eklund, H. and Furugren, B., 1975, Alcohol dehydrogenases. In The Enzymes, 3rd ed., Vol. 11, Academic Press, pp. 103-190.

    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  CAS  PubMed  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  CAS  PubMed  Google Scholar 

  • Danielsson, O., Eklund, H. and Jörnvall, H., 1992, The major piscine liver alcohol dehydrogenase hasclassmixed properties in relation to mammalian alcohol dehydrogenases of classes I and III. Biochemistry 31:3751–3759.

    Article  CAS  PubMed  Google Scholar 

  • 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 91:4980–4984.

    Article  CAS  PubMed  Google Scholar 

  • Danielsson, O., Shafqat, J., Estonius, M. and Jörnvall, H., 1994b, Alcohol dehydrogenase, class III contrasted to class I: characterization of the Cyclostome enzyme, multiplicity like for the human form, and distant cross-species hybridization. Eur. J. Biochem., in press.

    Google Scholar 

  • Duester, G., 1994a, Retinoids and the alcohol dehydrogenase gene family. In Toward a Molecular Basis of Alcohol Use and Abuse (Jansson, B., Jörnvall, H., Rydberg, U., Terenius, L., and Vallee, B.L., eds.) Birkhäuser Verlag, Basel, pp. 279–290.

    Chapter  Google Scholar 

  • Duester, G., 1994b, Class I and Class IV alcohol dehydrogenase (retinol dehydrogenase) gene expression in mouse embryos. This vol., in press.

    Google Scholar 

  • Eklund, H., Nordström, B., Zeppezauer, E., Söderlund, G., Ohlsson, I., Boiwe, T., Söderberg, B.-O., Tapia, O., Brändén, C.-I. and Åkeson, Å., 1976, Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4 Å resolution. J. Mol. Biol. 102:27–59.

    Article  CAS  PubMed  Google Scholar 

  • 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.

    Article  CAS  PubMed  Google Scholar 

  • El-Ahmad, M., Ramaswamy, S., Danielsson, O., Karlsson, C., Estonius, M., Höög, J.-O., Eklund, H. and Jörnvall, H., 1994, Crystallizations of novel forms of alcohol dehydrogenase. This vol., in press.

    Google Scholar 

  • 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.

    Article  CAS  PubMed  Google Scholar 

  • Estonius, M., Höög, J.-O., Danielsson, O. and Jörnvall, H., 1994, Residues specific for class III alcohol dehydrogenase. Biochemistry, submitted.

    Google Scholar 

  • Farrés, J., Moreno, A., Crosas, B., Peralba, J.M., Allali-Hassani, A., Hjelmqvist, L., Jörnvall, H. andParés, X., 1994a, Human stomach class IV alcohol dehydrogenase: cDNA sequence and primary structure correlations with enzymatic properties. Eur. J. Biochem. in press.

    Google Scholar 

  • Farrés, J., Moreno, A., Crosas, B., Cederlund, E., Allali-Hassani, A., Peralba, J.M., Hjelmqvist, L., Jörnvall, H. and Parés, X., 1994b, Human and rat class IV alcohol dehydrogenases. Correlations of primary structures with enzymatic properties. This vol., in press.

    Google Scholar 

  • Felsenstein, J., 1985, Confidence limits on phylogenies: an approach using the bootstrap. Evolution 39:783–791.

    Article  Google Scholar 

  • Ghosh, D., Weeks, C.M., Grochulski, P., Duax, W.L., Erman, M., Rimsay, R.L. and Orr, J.C., 1991, Three-dimensional structure of holo 3α, 20β-hydroxysteroid dehydrogenase: A member of a short-chain dehydrogenase family. Proc. Natl. Acad. Sci. USA. 88:10064–10068.

    Article  CAS  PubMed  Google Scholar 

  • Hjelmqvist, L., Shafqat, J., Siddiqi, A.R. and Jörnvall, H., 1994, The vertebrate alcohol dehydrogenasesystem. Gene duplications traced by isozyme heterogeneity of the reptilian class I enzyme from Uromastix hardwickii. Eur. J. Biochem., submitted.

    Google Scholar 

  • Holm, L., Sander, C. and Murzin, A., 1994, Three sisters, different names. Nature Structural Biology 1:146–147.

    Article  CAS  PubMed  Google Scholar 

  • Höög, J.-O., Eklund, H. and Jörnvall, H., 1992, A single-residue exchange gives human recombinant ßß alcohol dehydrogenase γγ isozyme properties. Eur. J. Biochem. 213:31–38.

    Article  Google Scholar 

  • Hurley, T.D., Bosron, W.F., Hamilton, J.A. and Amzel, L.M., 1991, Structure of β1βl alcoholdehydrogenase: catalytic effects of non-active site substitutions. Proc. Natl. Acad. Sci. USA 88, 8149–8153.

    Article  CAS  PubMed  Google Scholar 

  • Inoue, T., Sunagawa, M., Mori, A., Imai, C., Fukuda, M., Takagi, M. and Yano., 1989, Cloning and sequencing of the gene encoding the 72-kilodalton dehydrogenase subunit of alcohol dehydrogenase from Acetobacter aceti. J. Bacteriol. 171:3115–3122

    CAS  PubMed Central  PubMed  Google Scholar 

  • Jörnvall, H. and Höög, J.-O., 1994, Nomenclature of alcohol dehydrogenases. Alcohol and Alcoholism, in press.

    Google Scholar 

  • Jörnvall, H., Eklund, H. and Brändén, C.-I., 1978, Subunit conformation of yeast alcohol dehydrogenase. J. Biol. Chem. 253:8414–8419.

    PubMed  Google Scholar 

  • Jörnvall, H., Persson, M. and Jeffery, J., 1981, Alcohol and polyol dehydrogenases are both divided into two protein types, and structural properties cross-relate the different enzyme activities within each type. Proc. Natl. Acad. Sci. USA 78:4226–4230.

    Article  PubMed  Google Scholar 

  • Jörnvall, H., Danielsson, O., Eklund, H., Hjelmqvist, L., Höög, J.-O., Parés, X. and Shafqat, J., 1993a, Enzyme and isozyme developments within the medium-chain alcohol dehydrogenase family. In Enzymology and Molecular Biology of Carbonyl Metabolism 4 (Weiner, H., ed.), Plenum, New York, pp. 533–544.

    Chapter  Google Scholar 

  • Jörnvall, H., Persson, B., Du Bois, G.C., Lavers, G.C., Chen, J.H., Gonzalez, P., Rao, P.V. and Zigler, Jr., J.S., 1993b, ζ-crystallin versus other members of the alcohol dehydrogenase super-family. Variability as a functional characteristic. FEBS Lett. 322:240–244.

    Article  PubMed  Google Scholar 

  • Krook, M., Marekov, L. and Jörnvall, H., 1990, Purification and structural characterization of placental NAD+-inked 15-hydroxyprostaglandin dehydrogenase. The primary structure reveals the enzyme to belong to the short-chain alcohol dehydrogenase family. Biochemistry 29:738–743.

    Article  CAS  PubMed  Google Scholar 

  • Krook, M., Ghosh, D., Strömberg, R., Carlquist, M. and Jörnvall, H., 1993, Carboxyethyllysine in a protein: Native carbonyl reductase/NADP+-dependent prostaglandin dehydrogenase. Proc. Natl. Acad. Sci. USA 90:502–506.

    Article  CAS  PubMed  Google Scholar 

  • Luque, T., Atrian, S., Danielsson, O., Jörnvall, H. and Gonzàlez-Duarte, R., 1994, Structure of the Drosophila melanogaster glutathione-dependent formaldehyde dehydrogenase/octanol dehydrogenase gene (class III alcohol dehydrogenase). Evolutionary pathway of the alcohol dehydrogenase genes. Eur. J. Biochem., in press.

    Google Scholar 

  • Marekov, L., Krook, M. and Jörnvall, H., 1990, Prokaryotic 20β-hydroxysteroid dehydrogenase is an enzyme of the “short-chain, non-metalloenzyme” alcohol dehydrogenase type. FEBS Lett. 266:51–54.

    Article  CAS  PubMed  Google Scholar 

  • McKinley-McKee, J.S., Winberg, J.-O. and Pettersson, G., 1991, Mechanism of action of Drosophila melanogaster alcohol dehydrogenase. Biochem. Internat. 25:879–885.

    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.

    CAS  PubMed  Google Scholar 

  • 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.

    Article  PubMed  Google Scholar 

  • Peltoketo, H., Isomaa, V., Mäentausta, O. and Vihko, R., 1988, Complete amino acid sequence of human placental 17β-hydroxysteroid dehydrogenase deduced from cDNA. FEBS Lett. 239:73–77.

    Article  CAS  PubMed  Google Scholar 

  • Persson, B., Krook, M. and Jörnvall, H., 1991, Characteristics of short-chain alcohol dehydrogenses and related enzymes. Eur. J. Biochem. 200:537–543.

    Article  CAS  PubMed  Google Scholar 

  • Persson, B., Hallborn, J., Walfridsson, M., Hahn-Hägerdal, B., Keränen, S., Penttilä, M. and Jörnvall, H., 1993a, Dual relationships of xylitol and alcohol dehydrogenases in families of two protein types. FEBS Lett. 324:9–14.

    Article  CAS  PubMed  Google Scholar 

  • Persson, B., Bergman, T., Keung, W.M., Waldenström, U., Holmquist, B., Vallee, B.L. and Jörnvall, H., 1993b, 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.

    Article  CAS  PubMed  Google Scholar 

  • Persson, B., Krook, M. and Jörnvall, H., 1994a, Short-chain dehydrogenases/reductases. This vol., in press.

    Google Scholar 

  • Persson, B., Zigler, Jr., J.S. and Jörnvall, H., 1994b, A super-family of medium-chain dehydrogenasesAreductases (MDR): sub-lines including ζ-crystallin, alcohol and polyol dehydrogenases, quinone oxidore-ductases, enoyl reductases, VAT-1 and further proteins. Eur. J. Biochem., in press.

    Google Scholar 

  • Ramaswamy, S., El-Ahmad, M., Danielsson, O., Jörnvall, H. and Eklund, H., 1994, Crystallization and crystallographic investigations of cod alcohol dehydrogenase class I and class III enzymes. FEBS Lett. 350:122–124.

    Article  CAS  PubMed  Google Scholar 

  • Rao, P.V. and Zigler, J.S., Jr, 1991, ζ-crystallin from guinea pig lens is capable of functioning catalytically as an oxidoreductase. Arch. Biochem. Biophys. 284:181–185.

    Article  CAS  PubMed  Google Scholar 

  • Rao, P.V, Krishna, C.M. and Zigler, J.S., Jr, 1992, Identification and characterization of the enzymatic activity of zeta-crystallin from guinea-pig lens. A novel NADPH:quinone oxidoreductase. J. Biol. Chem. 267:96–102.

    CAS  PubMed  Google Scholar 

  • Satre, M.A., îgombi…-Knight, M. and Duester, G., 1994, The complete structure of human class IV alcohol dehydrogenase (retinol dehydrogenase) determined from the ADH7 gene. J. Biol. Chem. 269:15606–15612.

    CAS  PubMed  Google Scholar 

  • Scopes, R.K., 1983, An iron-activated alcohol dehydrogenase. FEBS Lett. 156:303–306.

    Article  CAS  PubMed  Google Scholar 

  • Vallee, B.L. and Bazzone, T.J., 1983, Isozymes of human liver alcohol dehydrogenases. Isozymes: Cum Top. Biol. Med. Res. 8:219–244.

    CAS  Google Scholar 

  • van Ophem, P.W., Van Beeumen, J and Duine, J.A., 1992, NAD-linked, factor-dependent formaldehy dedehy-drogenase or trimeric, zinc-containing, long-chain alcohol dehydrogenase from Amycolatopsis methanolica. Eur. J. Biochem., 206:511–518.

    Article  PubMed  Google Scholar 

  • Varughese, K.I., Skinner, M.M., Whiteley, J.M., Matthews, D.A. and Xuong, N.H., 1992, Crystal structure of rat liver dihydropteridine reductase. Proc. Natl. Acad. Sci. USA. 89:6080–6084.

    Article  CAS  PubMed  Google Scholar 

  • Wermuth, B., Bohren, K.M. and Ernst, E., 1993, Autocatalytic modification of human carbonyl reductase by 2-oxocarboxylic acids. FEBS Lett. 335, 151–154.

    Article  CAS  PubMed  Google Scholar 

  • Williamson, V.M. and Paquin, C.E., 1987, Homology of Saccharmomyces cerevisiae ADH4 to an iron-activated alcohol dehydrogenase from Zymomonas mobilis. Mol. Gen. Genet. 209:374–381.

    Article  CAS  Google Scholar 

  • Yin, S.-J., Vagelopoulos, N., Wang, S.-L. and Jörnvall, H., 1991, Structural features of stomach aldehyde dehydrogenase distinguish dimeric aldehyde dehydrogenase as a “variable” enzyme. “Variable” and “constant” enzymes within the alcohol and aldehyde dehydrogenase families. FEBS Lett. 283:85–88.

    Article  CAS  PubMed  Google Scholar 

  • Zheng, Y.-W., Bey, M., Liu, H. and Felder, M.R., 1993, Molecular basis of the alcohol dehydrogenase-negative deer mouse. J. Biol. Chem. 268:24933–24939.

    CAS  PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1995 Springer Science+Business Media New York

About this chapter

Cite this chapter

Jörnvall, H., Danielsson, O., Hjelmqvist, L., Persson, B., Shafqat, J. (1995). The Alcohol Dehydrogenase System. 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_34

Download citation

  • DOI: https://doi.org/10.1007/978-1-4615-1965-2_34

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-5808-4

  • Online ISBN: 978-1-4615-1965-2

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics