Abstract
The toxicity of the first eight primary alcohols and of four secondary alcohols was compared in a wild-type strain (having active ADH) and an ADH-negative mutant. Differences between lc 50 measured in the two strains allowed an evaluation of the biological activity of the enzyme. In vitro, ADH is mainly active on secondary alcohols, while in vivo its main role is the detoxification and metabolism of ethanol. These observations suggest that originally ADH was involved in unknown metabolic pathways and that its utilization in ethanol metabolism could be a recent event.
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References
Bari-Kolata, G. (1975). Evolution of DNA: Changes in gene regulation. Science 189446.
Birley, A. J., and Barnes, B. W. (1973). Genetical variation for enzyme activity in a population of Drosophila melanogaster. I. Extent of the variation for alcohol dehydrogenase activity. Heredity 31413.
Briscoe, D. A., Robertson, A., and Malpica, J. M. (1975). Dominance at the ADH locus in response of adult Drosophila melanogaster to environmental alcohol. Nature 255148.
Clarke, B. (1975). The contribution of ecological genetics to evolutionary theory: Detecting the direct effects of natural selection on particular polymorphic loci. Genetics 79101.
David, J., and Bocquet, C. (1974). L'adaptation génétique à l'éthanol: Un paramètre important dans l'évolution des races géographiques de Drosophila melanogaster. Compt. Rend. Acad. Sci. Paris 2791385.
David, J., and Bocquet, C. (1975). Latitudinal adaptation of two Drosophila sibling species: Similarities and differences. Nature 257588.
David, J., and Bocquet, C. (1976a). Genetic tolerance to ethanol in Drosophila melanogaster: Increase by selection and analysis of correlated responses. Genetica (in press).
David, J., and Bocquet, C. (1976b). Compared toxicities of different alcohols for two Drosophila sibling species, D. melanogaster and D. simulans. Comp. Physiol. Biochem. 54C71.
David, J., and Clavel, M. F. (1965). Interaction entre le génotype et le milieu d'élevage: Conséquences sur les caractéristiques du développement de la Drosophile. Bull. Biol. Fr. Belg. 99369.
David, J., Fouillet, P., and Arens, M. F. (1974). Comparison de la sensibilité à l'alcool éthylique de six espèces de Drosophila du sous groupe melanogaster. Arch. Zool. Exp. Gen. 115401.
Day, T., Hillier, P. C., and Clarke, B. (1974). Properties of genetically polymorphic isozymes of alcohol dehydrogenase in Drosophila melanogaster. Biochem. Genet. 11141.
Grell, E. H., Jacobson, K. B., and Murphy, J. H. (1968). Alteration of genetic material for analysis of alcohol dehydrogenase isozymes of Drosophila melanogaster. Ann. N.Y. Acad. Sci. 151441.
Libion-Mannaert, M., Delcour, J., Deltombe-Lietaert, M. C., Lenelle-Montfort, N., and Elens, A. (1976). Ethanol as a food for Drosophila melanogaster: Influence of the ebony gene. Experientia 3222.
McKenzie, J. A., and Parsons, P. A. (1972). Alcohol tolerance: An ecological parameter in the relative success of Drosophila melanogaster and D. simulans. Oecologia 10373.
McKenzie, J. A., and Parsons, P. A. (1974). Microdifferentiation in a natural population of Drosophila melanogaster to alcohol in the environment. Genetics 77385.
O'Donnell, J., Gerace, L., Leister, F., and Sofer, W. (1975). Chemical selection of mutants that affect alcohol dehydrogenase in Drosophila. II. Use of 1-pentyne-3-ol. Genetics 7973.
Pipkin, S. B., and Hewitt, N. E. (1972). Variation of alcohol dehydrogenase levels in Drosophila species hybrids. J. Hered. 63267.
Pipkin, S. B., Potter, J. H., Lubega, S., and Springer, E. (1975). Further studies on alcohol dehydrogenase polymorphism in Mexican strains of Drosophila melanogaster. In Markert, C. L. (ed.), Isozymes, Vol. 4, Academic Press, New York, p. 547.
Sieber, F., Fox, D. J., and Ursprung, H. (1972). Properties of octanol dehydrogenase from Drosophila. FEBS Letters 26274.
Sofer, W. H., and Hatkoff, M. A. (1972). Chemical selection of alcohol dehydrogenase negative mutants in Drosophila. Genetics 72545.
Ursprung, M., and Leone, J. (1965). Alcohol dehydrogenase: A polymorphism in D. melanogaster. J. Exp. Zool. 160147.
Van Delden, W., Kamping, A., and Van Dijk, M. (1975). Selection at the alcohol dehydrogenase locus in Drosophila melanogaster. Experientia 31418.
Van Herrewege, J., and David, J. (1974). Utilisation de l'alcool éthylique dans le métabolisme énergétique d'un insecte: Influence sur la durée de survie des adultes de Drosophila melanogaster. Compt. Rend. Acad. Sci. Paris 279335.
Vigue, C. L., and Johnson, F. M. (1973). Isozyme variability in species of the genus Drosophila. VI. Frequency-property-environment relationships of allelic alcohol dehydrogenases in D. melanogaster. Biochem. Genet. 9213.
Vigue, C., and Sofer, W. (1976). Chemical selection of mutants that affect ADH activity in Drosophila. III. Effects of ethanol. Biochem. Genet. 14127.
Ward, R. D., and Hebert, P. D. N. (1972). Variability of alcohol dehydrogenase activity in a natural population of Drosophila melanogaster. Nature 236243.
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David, J.R., Bocquet, C., Arens, MF. et al. Biological role of alcohol dehydrogenase in the tolerance of Drosophila melanogaster to aliphatic alcohols: Utilization of an ADH-null mutant. Biochem Genet 14, 989–997 (1976). https://doi.org/10.1007/BF00485131
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DOI: https://doi.org/10.1007/BF00485131