Abstract
Zinc-containing medium-chain alcohol dehydrogenases/reductases (MDR) are ubiquitous (Danielsson et al., 1994), constituting a group of enzymes with great multiplicity. Natural variants of the family serve to illustrate functional properties, but can also serve as tools for studying evolution of novel forms. Formation of families, enzymes, classes and isozymes reflects these aspects. Class III/glutathione-dependent formaldehyde dehydrogenase, with its constant properties in vertebrates (Jörnvall and Höög, 1995; Hjelmqvist et al., 1995), invertebrates (Danielsson et al., 1994; Kaiser et al., 1993), plants (Shafqat et al., 1996; Martinez et al., 1996), fungi (Sasnaukas et al., 1992; Fernandez et al., 1995), prokaryotes (Gutheil et al., 1992; Ras et al., 1995), and archaeons (Ammendola, 1992) has a distant origin. Class I, with ethanol dehydrogenase activity, has a duplicatory origin from class III (Daniels son and Jörnvall, 1992; Jörnvall, 1994), as has also the ethanol active ADH in plants (Shafqat et al., 1996). Different regions of the molecules have been assessed for various functional and structural properties, like binding of substrate and coenzyme (Eklund, 1984; Hurley, 1991), metals (Eklund et al., 1976), other subunits (Persson et al., 1993; Danielsson et al., 1994), and further aspects.
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References
Ammendola, S., Raia, CA., Caruso, C., Camardella, L., D’Auria, S., Rosa, M. D. and Rossi, M. (1992) Thermo-stable NAD+-dependent alcohol dehydrogenase from Sulfolobus solfataricus: gene and protein sequence determination and relationship to other alcohol dehydrogenases. Biochemistry, 12514–12523.
Blattner, F. R, plunkett, G., Block, CA., Perna, N. T., Burland, V, Riley, M., Colladovides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Krikpatric, H. A., Goeden, M. A., Rose, DJ., Mau, B., and Shao, Y. (1997) The complete genome sequence of Escherichia coli K-12. Science,-1471
Borrâs, T., Persson, B. and Jörnvall, H. (1989) Eye lens ς-crystallin relationships to the family of“long-chain”al-cohol/polyol dehydrogenases. Protein trimming and conservation of stable parts. Biochemistry 28,6133–6139.
Danielsson, O., Atrian, S., Luque, T., Hjelmqvist, L., Gonzéz-Duarte, R. and Jörnvall, H. (1994) Fundamental molecular differences between alcohol dehydrogenase classes. Proc. Natl. Acad. Sci. USA, 91, 4980–4984.
Danielsson, O., Eklund, H. and Jörnvall, H. (1992) Major piscine liver alcohol dehydrogenase has class-mixed properties in relation to mammalian alcohol dehydrogenases of classes I and III. Biochemistry 31, 3751–3759.
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.
Eklund, H., Nordström, B., Zeppezaner, E., Söderlund, G., Ohlsson, L, Boiwe, T., Söderberg, B-O., Tapia, O., Bränden, C-I. and ákeson, υ. (1976) Three dimensional structure of horse liver alcohol dehydrogenase at 2. 4Å resolution. J. Mol. Biol. 102,27–59.
Eklund, H., Samama, J.-R and Jones, T. A. (1984) Crystallographic investigations of nicotinamide adenine dinu-cleotide binding to horse liver alcohol dehydrogenase. Biochemistry 23, 5982–5996.
Felsenstein, J. (1985) Confidence limits on phylogenies: An approach using the bootstrap. Evolution. 39, 783–789.
Fernández, M. R., Biosca, J. A., Norin, A., Jörnvall, H. and Parés, X. (1995) Class III alcohol dehydrogenase from Saccharomyces cerevisiae: Structural and enzymatic features differ towards the human/mammalian forms in a manner consistent with functional needs in formaldehyde detoxication. FEBS Lett. 370, 23–26.
Gutheil, W. G., Holmquist, B. and Vallée, B. L. (1992) Purification, characterization, and partial sequence of the glutathione-dependent formaldehyde dehydrogenase from Escherichia coli: a class III alcohol dehydrogenase. Biochemistry 31,475–481.
Hjelmqvist, L., Shafqat, J., Siddiqi, A. R. and Jörnvall, H. (1995) Alcohol dehydrogenase öf class HI: consistent patterns of structural and functional conservation in relation to class I and other proteins. FEBS Lett. 373, 212–216.
Höög, J.-O., Weis, M., Hedén, L.-O., Zeppezauer, M., Jörnvall, H. and von Bahr-Lindström, H. (1987) Expression in Escherichia coli of active human alcohol dehydrogenase lacking N-terminal acetylation. Biosci. Rep. 7, 969–974.
Hurley, T. D., Bosron, W. F., Hamilton, J. A. and Amzel, L. M. (1991) Structure of human β,β, alcohol dehydrogenase: catalytic effects of non-active-site substitutions. Proc. Natl. Acad. Sci. USA. 88, 8149–8153.
Jörnvall, H. (1994) The alcohol dehydrogenase system. In: Toward a Molecular Basis of Alcohol Use and Abuse (Jansson, B., Jörnvall, H., Rydberg, U., Terenius, L. and Vallée, B. L. eds) pp. 221–229, Birkhäuser, Basel.
Jörnvall, H. and Höög, J.-O. (1995) Nomenclature of alcohol dehydrogenases. Alcohol and Alcoholism 30, 153–161.
Jörnvall, H., Shafqat, J., El-ahmad, M., Hjelmqvist, L., Persson, B. and Danielsson, O. (1996) Alcohol dehydrogenase variability: Evolutionary and functional conclusions from characterization of further variants. Enzy-mology and molecular Biology of Carbonyl Metabolism 6. Edited by Weiner et al. Plenum press, New York. 281–289
Kaiser, R., Fernândez, M. R., Parés, X. and Jörnvall, H. (1993). Origin of the human alcohol dehydrogenase system: Implications from the structure and properties of the octopus protein. Proc. Natl. Acad. Sci. USA, 90, 11222–11226
Keshav, K. F., Yomano, L. P., An, H. and Ingram, L. O. (1990) Cloning of the Zymomonas mobilis structural gene encoding alcohol dehydrogenase I (adhA): sequence comparison and expression in Escherichia coli. J. Bacteriol. 172,2491–2497.
Luque, T., Hjelmqvist, L., Marfany, G., Danielsson, O., El-Ahmad, M., Persson, B., Jörnvall, H. and Gonzéz-Duarte, R. (1998) Sorbitol dehydrogenase of Drosophila: gene, protein and expression data show a two-gene system. J. Biol. Chem., submitted.
Martinez, M. C., Achkor, H., Persson, B., Fernandez, M. R., Shafqat, J., Farrés, J., Jörnvall, H. and Parés, X. (1996) Arabidopsis formaldehyde dehydrogenase. Eur. J. Biochem. 241, 849–857.
Norin, A., van Ophem, P. W., Piersma, S., Duine, J. A. and Jörnvall, H. (1997) Factor-dependent formaldehyde dehydrogenase: A prokaryotic enzyme linking different eukaryotic dehydrogenase lines. EUT. J. Biochem. 248,282–289.
Persson, B., Bergman, T., Keung, W. M., Waldenström, U., Holmqvist, B. and Jörnvall, H. (1993) Basic features of class I alcohol dehydrogenase: variable and constant segments coordinating by inter-class and intra-class variability. Conclusions from characterization of alligator enzyme. EUT. J. Biochem. 216,49–56.
Ras, J., Van Ophem, P. W., Reijnders, W. N. M., Van Spanning, R. J. M., Duine, J. A., Stouthamer, A. H. and Harms, N. (1995) Isolation, sequencing, and mutagenesis of the gene encoding NAD-and glutathione-dependent formaldehyde dehydrogenase (GD-FALDH) from Paracoccus denitrificans, in which GD-FALDH is essential for methylotrophic growth. J. Bacteriol. 177, 247–251.
Sasnaukas, K., Jomantiené, R., Januska, A., Lebediené, E., Lebedys, J. and Janulaitis, A. (1992) Cloning and analysis of a Candida maltosa gene which confers resistance to formaldehyde in Saccharomyces cere-visiae. Gene 122, 207–211.
Shafqat, J., El-Ahmad, M, Danielsson, O., Martinez, M. C., Persson, B., Parés, X. and Jörnvall, H. (1996) Pea formaldehyde-active class III alcohol dehydrogenase: Common derivation of the plant and animal forms but not of the corresponding ethanol-active forms (classes I and P). Proc. Natl. Acad. Sci. USA, 93, 5595–5599.
Shafqat, J., Höög, J-O., Hjelmqvist, L., Oppermann, U., Ibanez, C. and Jörnvall, H. (1998) An ethanol-active and ethanol-inducible E. coli alcohol dehydrogenase. Structural and enzymatic relationships to the eukaryotic protein forms. Eur. J. Biochem. submitted.
Thompson, J. D., Higgins, D. G. and Gibson, T. J. (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acid Res. 22, 4673–4680.
Wagner, F. W., Burger, A. R. and Vallée, B. L. (1983) Kinetic properties of human liver alcohol dehydrogenase: oxidation of alcohols by class I isoenzymes. Biochemistry 22, 1857–1863.
Wills, C, Kratofil, P., Londo, D. and Martin, T. (1981) Characterization of the two alcohol dehydrogenases of Zy-momonas mobilis. Arch. Biochem. Biophys. 210, 775–785.
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Shafqat, J., Höög, JO., Hjelmqvist, L., Oppermann, U., Ibanez, C., Jörnvall, H. (1999). Studies on Variants of Alcohol Dehydrogenases and its Domains. 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_35
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DOI: https://doi.org/10.1007/978-1-4615-4735-8_35
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