Abstract
Thirty amino acid substitutions are known in eight sets of isozymes or mutants of alcohol dehydrogenases. The replacements are at different positions in the subunits and affect many regions of the protein chains, which is consistent with the variability in properties of isozyme pairs. Correlations with functional consequences, chemical modifications and sub-forms are summarized.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsPreview
Unable to display preview. Download preview PDF.
References
Berger, D., M. Berger, and J.-P. von Wartburg, 1974, Structural studies of human-liver alcohol-dehydrogenase isoenzymes, Eur. J. Biochem., 50: 215.
Brändén, C.-I., 1977, in: “Alcohol and Aldehyde Metabolizing Systems,” Thurman, R.G., Williamson, J.R., Drott, H.R., and Chance, B., eds., Academic Press, New York.
Brändén, C.-I., H. Jörnvall, H. Eklund, and B. Furugren, 1975, in: “The Enzymes,” Boyer, P.D., ed., Academic Press, New York.
Cronholm, T., C. Larsén, J. Sjövall, H. Theorell, and A. Akeson, 1975, Steroid oxidoreductase activity of alcohol dehydrogenase from horse, rat and human liver, Acta Chem. Scand., B29: 571.
Eckfeldt, J., L. Mope, K. Takio, and T. Xonetani, 1976, Horse liver aldehyde dehydrogenase, J. Biol. Chem., 251: 236.
Eklund, H., B. Nordström, E. Zeppezauer, G. Söderlund, I. Ohlsson, T. Boiwe, B.-O. Soderberg, O. Tapia, C.-I. Brändén, and A. Akeson, 1976, Three-dimensional structure of horse-liver alcohol dehydrogenase at 2.4Å Resolution, J. Mol. Biol., 102: 27.
Jörnvall, H., 1970, Horse-liver alcohol dehydrogenase on the primary structures of the isoenzymes, Eur. J. Biochem., 16: 41.
Jörnvall, H., 1975, Acetylation of protein N-terminal amino groups. Structural observations on alpha-amino acetylated proteins, J. Theor. Biol., 55: 1.
Jörnvall, H., 1977a, in: “Pyridine Nucleotide-Dependent Dehydrogenases,” Sund, H., ed., Walter de Gruyter, Berlin and New York.
Jörnvall, H., 1977b, The primary structure of yeast alcohol dehydrogenase, Eur. J. Biochem., 72: 425.
Jörnvall, H., 1979, in: “Dehydrogenases Requiring Nicotinamide Coenzymes,” Jeffery, J., ed., Birkhäuser Verlag, Basel, in press.
Jörnvall, H., and R. Pietruszko, 1972, Structural studies of alcohol dehydrogenase from human liver, Eur. J. Biochem., 25: 283.
Jörnvall, H., L.G. Lange, III., J.F. Riordan, and B.L. Vallee, 1977, Identification of a reactive arginyl residue in horse liver alcohol dehydrogenase, Biochem. Biophys. Res. Commun., 77: 73.
Jörnvall, H., H. Eklund, and C.-I. Brandon, 1978, Subunit conformation of yeast alcohol dehydrogenase, J. Biol. Chem., 253: 8414.
Jörnvall, H., T. Fâirwell, P. Kratofil, and C. Wills, 1979, Differences in α-amino acetylation of isozymes of yeast alcohol dehydrogenase, FEES Lett., submitted.
Lange, L.G., III, J.F. Riordan, and B.L. Vallee, 1974, Functional arginyl residues as NADH binding sites of alcohol dehydrogenases, Biochem., 13: 4361.
Lange, L.G., III, J.F. Riordan, B.L. Vallee, and C.-I. Brändén, 1975, The role of arginyl tesidues in directing carboxylmethylation of horse liver alcohol dehydrogenase, Biochem., 14: 3497.
Li, T.-K., W.F. Bosron, W.P. Dafeldecker, L.G. Lange, and B.L. Vallee, 1977, Isolation of II-alcohol dehydrogenase of human liver: Is it a determinant of alcoholism?, Proc. Natl. Acad. Sci. USA, 74: 4378.
Palmiter, R.D., 1977, Prevention of NH2-terminal acetylation of proteins synthesized in cell-free systems, J. Biol. Chem., 252: 8781.
Schwartz, M.F., and H. Jörnvall, 1976, Structural analyses of mutant and wild-type alcohol dehydrogenases from Drosophila melanogaster, Eur. J. Biochem., 68: 159.
Smith, M., D.A. Hopkinson, and H. Harris, 1973, Studies on the properties of the human alcohol dehydrogenase isozymes determined by the different loci ADH1, ADH2, and ADH3, Ann. Hum. Genet., 37: 49.
von Wartburg, J.-P., J. Papenberg, and H. Aebi, 1965, An atypical human alcohol dehydrogenase, Can. J. Biochem., 43: 889.
Wills, C., 1976, Production of yeast alcohol dehydrogenase isoenzymes by selection, Nature, 261: 26.
Wills, C., and H. Jörnvall, 1979a, The two major isozymes of yeast alcohol dehydrogenase, Eur. J. Biochem., 99: 323.
Wills, C., and H. Jörnvall, 1979b, Amino acid substitutions in two functional mutants of yeast alcohol dehydrogenase, Nature, 279: 734.
Zeppezauer, E., H. Jörnvall, and I. Ohlsson, 1975, Carboxymethylation of horse-liver alcohol dehydrogenase in the crystalline state, Eur. J. Biochem., 58: 95.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1980 Springer Science+Business Media New York
About this chapter
Cite this chapter
Jörnvall, H. (1980). Isozymes of Alcohol Dehydrogenases. In: Thurman, R.G. (eds) Alcohol and Aldehyde Metabolizing Systems-IV. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-1419-7_8
Download citation
DOI: https://doi.org/10.1007/978-1-4757-1419-7_8
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4757-1421-0
Online ISBN: 978-1-4757-1419-7
eBook Packages: Springer Book Archive