Skip to main content
Log in

The involvement of alcohol dehydrogenase and aldehyde dehydrogenase in alcohol/aldehyde metabolism in Drosophila melanogaster

  • Published:
Genetica Aims and scope Submit manuscript

Abstract

In this study we have examined the roles of alcohol dehydrogenase, aldehyde oxidase, and aldehyde dehydrogenase in the adaptation of Drosophila melanogaster to alcohol environments. Fifteen strains were characterized for genetic variation at the above loci by protein electrophoresis. Levels of in vitro enzyme activity were also determined. The strains examined showed considerable variation in enzyme activity for all three gene-enzyme systems. Each enzyme was also characterized for coenzyme requirements, effect of inhibitors, subcellular location, and tissue specific expression. A subset of the strains was chosen to assess the physiological role of each gene-enzyme system in alcohol and aldehyde metabolism. These strains were characterized for both the ability to utilize alcohols and aldehydes as carbon sources as well as the capacity to detoxify such substrates. The results of the above analyses demonstrate the importance of both alcohol dehydrogenase and aldehyde dehydrogenase in the in vivo metabolism of alcohols and aldehydes.

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

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Anderson, S. & McDonald, J., 1981a. Effect of environmental alcohol on in vivo properties of Drosophila alcohol dehydrogenase. Biochem. Genet. 19: 420–428.

    Google Scholar 

  • Anderson, S. & McDonald, J., 1981b. Changes in the levels of alcohol dehydrogenase during the development of Drosophila melanogaster. Can. J. of Genet. and Cyt. 23: 305–313.

    Google Scholar 

  • Anderson, S. & McDonald, J., 1983. Biochemical and molecular analysis of naturally occuring Adh variants in Drosophila melanogaster. Proc. Natl. Acad. Sci. 80: 4798–4802.

    Google Scholar 

  • Anderson, S., Santos, M. & McDonald, J., 1981. Selection at the Adh locus: Adult survivorship in response to ethanol. Experientia 37: 463–464.

    Google Scholar 

  • Atrian, S. & Gonzalez-Duarte, R., 1985. An aldo-keto reductase activity in Drosophila melanogaster and Drosophila hydei: A possible function in alcohol metabolism. Comp. Biochem. Physiol. 81B: 949–952.

    Google Scholar 

  • Chambers, G. K., 1988. The Drosophila alcohol dehydrogenase gene-enzyme system. Adv. Genet. 25: 39–106.

    Google Scholar 

  • Cypher, J. J., Tedesco, J. L., Courtright, J. B. & Kumarin, A. K., 1982. Tissue-specific and substrate-specific detection of aldehyde and pyridoxal oxidase in larval and imaginal tissues of Drosophila melanogaster. Biochem. Genet. 20: 315–332.

    Google Scholar 

  • Daly, K. & Clarke, B., 1981. Selection associated with the alcohol dehydrogenase locus in Drosophila melanogaster: Differential survival of adults maintained on low concentrations of ethanol. Heredity 46: 219–226.

    Google Scholar 

  • David, J., Bocquet, C., Van Herrewege, J., Fouillet, P. & Arens, M., 1978. Alcohol metabolism in Drosophila: Uselessness of the most active aldehyde oxidase produced by the Aldox locus. Biochem. Genet. 16: 203–211.

    Google Scholar 

  • David, J. R., Daly, K. & Van Herrewege, J., 1984. Acetaldehyde utilization and tolerance in Drosophila adults lacking alcohol dehydrogenase or aldehyde oxidase. Biochem. Genet. 22: 1015–1029.

    Google Scholar 

  • Eisses, K. Th., Schooner, W. G. E. J., Aben, W., Scharloo, W. & Thorig, G. E. W., 1985. Dual function of the alcohol dehydrogenase of Drosophila melanogaster: Ethanol and acetaldehyde oxidation by two allozymes ADH-71k and ADH-F. Mol. Gen. Genet. 199: 76–81.

    Google Scholar 

  • Garcin, F., Cote, J., Radouco-Thomas, S., Kasienczuk, D., Chawla, S. & Radouco-Thomas, C., 1983. Acetaldehyde oxidation in Drosophila melanogaster and Drosophila simulans: Evidence for the presence of an NAD+-dependendent dehydrogenase. Comp. Biochem. Phys. 75B: 205–210.

    Google Scholar 

  • Garcin, F., Larochelle, C., Lau You Hin, G. & Cote, J., 1985. Acetaldehyde oxidation in Drosophila null-mutants for alcohol dehydrogenase. Experientia 41: 946–948.

    Google Scholar 

  • Heinstra, P. W. H., Eisses, K. Th., Schooner, W. G. E. J., Aben, W., DeWinter, A. J., Van Der Horst, D. J., Van Marrewijk, W. J., Beenakkers, A. M. Th., Scharloo, W. & Thorig, G. E. W., 1983. A dual function of alcohol dehydrogenase in Drosophila. Genetica 60: 129–137.

    Google Scholar 

  • Heinstra, P. W. H., Geer, B. W., Sykers, D. & Langevin, M., 1989. The metabolism of ethanol derived acetaldehyde by alcohol dehydrogenase (E.C. 1.1.1.1) and aldehyde dehydrogenase (E.C. 1.2.1.3.) in Drosophila melanogaster larvae. Biochem. J. 259: 791–797.

    Google Scholar 

  • Hsu, L. C., Tani, K., Fujiyoshi, T., Kurachi, K. & Yoshida, A., 1985. Cloning of cDNAs for human aldehyde dehydrogenase 1 and 2. Proc. Natl. Acad. Sci. 82: 3771–3775.

    Google Scholar 

  • McDonald, J., Anderson, S. & Santos, M., 1980. Biochemical differences between the products of the Adh locus in Drosophila. Genetics 95: 1013–1022.

    Google Scholar 

  • McDonald, J. F. & Ayala, F. J., 1978. Genetic and biochemical basis of enzyme activity variation in natural populations. I. Alcohol dehydrogenase in Drosophila melanogaster. Genetics 89: 371–388.

    Google Scholar 

  • O'Brien, S. J. & MacIntyre, R. J., 1972. The alpha glycerophosphate cycle in Drosophila melanogaster. I. Biochemical and developmental aspects. Biochem. Genet. 7: 141–161.

    Google Scholar 

  • Sofer, W. H. & Hatkoff, M. A., 1972. Chemical selection of alcohol dehydrogenase mutants in Drosophila. Genetics 72: 545–549.

    Google Scholar 

  • Tsutsumi, M., Takade, A., Takase, S. & Sugata, K., 1988. Hepatic aldehyde dehydrogenase isoenzymes: Differences with respect to species. Alcohol 5: 33–38.

    Google Scholar 

  • Van Delden, W., 1982. The alcohol dehydrogenase polymorphism in Drosophila melanogaster. In: Evolutionary Biology (Hecht, M., Wallace, B., and Prance, G. eds.) v 15. pp. 187–222. Plenum Press, London and New York.

    Google Scholar 

  • Weiner, H., 1979. Aldehyde dehydrogenase: Mechanism of action and possible physiological role. In: Biochemistry and Pharmacology of Ethanol (Majchrowicz, E. and Noble, E. eds) pp 107–124. Plenum Press. London and New York.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Anderson, S.M., Barnett, S.E. The involvement of alcohol dehydrogenase and aldehyde dehydrogenase in alcohol/aldehyde metabolism in Drosophila melanogaster . Genetica 83, 99–106 (1991). https://doi.org/10.1007/BF00058526

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00058526

Keywords

Navigation