Abstract
Alcohol dehydrogenases and related enzymes constitute a large group of proteins belonging to several super-families, which also encompass many other enzyme activities. The enzymes, in turn, exhibit further multiplicity in the form of separate classes, separate isozymes, and different allelozymes. These overall relationships are exemplified in Table 1 and have been summarized recently (Jörnvall et al., 1992). The different levels of complexity reflect general principles of protein relationships. A feature observed in many families is the modular build-up of proteins, showing separate organizations but still individual units in common, and an extensive divergence. Another such feature is the frequent examples of insertions/deletions.
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References
Borrás, T., Persson, B. and Jörnvall, 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.
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.
Dickerson, R. E., 1971 The structure of cytochrome c and the rates of molecular evolution, J. Mol. Evol. 1:26.
Eklund, H., Nordstrom, B., Zeppezauer, E., Soderlund, G., Ohlsson, I., Boiwe, T., Soderberg, B.-O., Tapia, O., Branden, C.-I. and Akeson, A., 1976 Three-dimensional structure of horse liver alcohol dehydrogenase at 2.4 Å resolution, J. Mol. Biol. 102:27.
Eklund, H., Horjales, E., Jornvall, H., Branden, C. I. and Jeffery, J., 1985 Molecular aspects of functional differences between alcohol and sorbitol dehydrogenases, Biochemistry 24:8005.
Inoue, H., Sunagawa, M., Mori, A., Imai, C., Fukuda, M., Takagi, M. and Yano, K., 1989 Cloning and sequencing of the gene encoding the 72-kilodalton dehydorgenase subunit of alcohol dehydrogenase from Aceobacter aceti, J. Bacteriol. 171:3115.
Jeffery, J., Chester, J., Mills, C., Sadler, P. J. and Jörnvall, H., 1984 Sorbitol dehydrogenase is a zinc enzyme, EMBO J. 3:357.
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.
Jörnvall, H., Persson, B. and Jeffery, J., 1987 Characteristics of alcohol/polyol dehydrogenases. The zinc-containing long-chain alcohol dehydorgenases, Eur. J. Biochem. 167:195.
Jörnvall, H., Danielsson, O., Eklund, H., Hjelmqvist, L., Höög, J.-O., Pares, X. and Shafqat, J., 1992 Enzyme and isozyme developments within the medium-chain alcohol dehydorgenase family, in: Enzymology and Molecular Biology of Carbonyl Metabolism, Weiner, H., Flynn, T.G. and Crabb, D.W., eds., Plenum Press, in press.
Kaiser, R., Holmquist, B., Hempel, J., Vallee, B. L. and Jörnvall, H., 1988 Class III human liver alcohol dehydrogenase: a novel structural type equidistantly related to the class I and class II enzymes, Biochemistry 27:1132.
Krook, M., Ghosh, D., Stromberg, R., Carlquist, M. and Jörnvall, H., 1992 Native carbonyl reductase/NADP+-dependent prostaglandin dehydrogenase. Multiplicity and reductive alkylation in a short-chain dehydrogenase, Proc. Natl. Acad. Sci. USA, in press.
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 σσ-ADH reveals class IV to be variable and confirms the presence of a fifth mammalian alcohol dehydrogenase class, FEBS Lett. 30:69.
Persson, B., Krook, M. and Jörnvall, H., 1991 Characteristics of short-chain alcohol dehydrogenases and related enzymes, Eur. J. Biochem. 200:537.
Rouimi, P., Loomes, K. and Jörnvall, H., 1992 Comparative proteolysis of sorbitol and alcohol dehydrogenases, Eur. J. Biochem., in press.
Scopes, R. K., 1983 An iron-activiated alcohol dehydrigenase, FEBS Lett. 156:303.
Smith, E. L. and Margoliash, E., 1964 Evolution of cytocrome c, Fed. Proc. 23:1243.
Smith, M., Hopkinson, D. A. and Harris, H., 1971 Developmental changes and polymorphism in human alcohol dehydrogenase, Ann. Hum. Genet. 34:251.
Schwartz, M. F. and Jörnvall, H., 1976 Structural analyses of mutant and wild-type alcohol dehydrogenases from Drosophila melanogaster, Eur. J. Biochem. 68:159.
Thatcher, D.R. and Sawyer, L., 1980 Secondary-structure prediction from the sequence of Drosophila melanogaster (fruitfly) alcohol dehydrogenase, Biochem. J. 187:884.
Vallee, B. L. and Bazzone, T. J., 1983 Isozymes of human liver alcohol dehydrogenases, Isozymes: Curr. Top. Biol. Med. Res. 8:219.
Williamson, V. M. and Paquin, C. E., 1987 Homology of Saccharomyces cerevisiae ADH4 to an iron-activated alcohol dehydrogenase form Zymonomas mibilis, Mol. Gen. Genet. 209:374.
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Jörnvall, H., Danielsson, O., Höög, JO., Persson, B. (1993). Alcohol Dehydrogenases: Patterns of Protein Evolution. In: Imahori, K., Sakiyama, F. (eds) Methods in Protein Sequence Analysis. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-1603-7_36
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DOI: https://doi.org/10.1007/978-1-4899-1603-7_36
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