Molecular and General Genetics MGG

, Volume 180, Issue 2, pp 455–462 | Cite as

Preliminary characterization and physical properties of pyridoxal oxidase activity from Drosophila melanogaster

  • E. W. Hanly


a method of extracting pyridoxal oxidase (PO) activity from D. melanogaster adults is described. in crude extracts, this method allows the activity to remain stable for an extended period of time so that subsequent work on the enzyme can be carried out. The extraction procedure, the constituents of the buffer, and the assay conditions are given. Under these conditions, there is an increase, in specific activity of PO during the first 4 to 8 h following extraction when the extract is held at 4° C. Optimum pH, substrate concentration, and ionic strength are given. In all of these cases the maximum activity points are not chosen since at those values, the lability of the activity is increased. Enzyme activity is also increased by short periods at 55°C. The basis for the increased activity, either upon heating or upon standing at 4°C, is not understood. These and other results are discussed considering the possibility that the structural loci for pyridoxal oxidase and aldehyde oxidase might have arisen as a duplication from an ancestral gene.


Enzyme Enzyme Activity Aldehyde Ionic Strength Crude Extract 
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  1. Andres RY (1976) Aldehyde oxidase and xanthine dehydrogenase from wild type Drosophila melanogaster and immunology cross-reacting material from ma-l mutants. Eur J Biochem 62: 591–600Google Scholar
  2. Beckman L, Johnson FM (1964) Esterase variations in Drosophila melanogaster. Hereditas 51:221–230Google Scholar
  3. Bentley MM, Williamson JW (1979) A new mutant affecting aldehyde oxidase in Drosophila melanogaster. Naturforsch 34c:304–305Google Scholar
  4. Bray RC (1976) Molybdenum iron-sulfur flavin hydroxylases and related enzymes. In: Boyer P (ed) The Enzymes, vol XII, part B. Academic Press, Inc., San FranciscoGoogle Scholar
  5. Browder LW, Williamson JH (1976) The effects of cinnamon on xanthine dehydrogenase, aldehyde oxidase and pyridoxal oxidase activity during development in Drosophila melanogaster. Dev Biol 53:241–249Google Scholar
  6. Chovnick A, Gelbart W, McCarron M, Osmond B, Candido DPM, Baillie DL (1976) Organization of the rosy locus in Drosophila melanogaster: evidence for a control element adjacent to the xanthine dehydrogenase structural element. Genetics 84:233–255Google Scholar
  7. Collins JF, Glassman E (1969) A third locus (lpo) affecting pyridoxal oxidase in Drosophila melanogaster. Genetics 61:833–839Google Scholar
  8. Collins JF, Duke EJ, Glassman E (1971) Multiple molecular forms of xanthine dehydrogenase and related enzymes. IV. The relationship of aldehyde oxidase to xanthine dehydrogenase. Biochem Genet 5:1–13Google Scholar
  9. David J, Boquet C, Van Herrewege J, Fouillet P, Arens MF (1978) Alcohol metabolism in Drosophila melanogaster: Uselessness of the most active aldehyde oxidase produced by the aldox locus. Biochem Genet 16:203–211Google Scholar
  10. Dickinson WJ (1970) The genetics of aldehyde oxidase in Drosophila melanogaster. Genetics 66:487–496Google Scholar
  11. Dickinson WJ (1971) Aldehyde oxidase in Drosophila melanogaster: A system, for genetic studies in developmental regulation. Dev Biol 26:77–86Google Scholar
  12. Dickinson WJ (1975) A genetic locus affecting the developmental expression of an enzyme in Drosophila melanogaster. Dev Biol 42:131–140Google Scholar
  13. Dickinson WJ, Sullivan DT (1975) Gene enzyme systems in Drosophila. Springer Verlag, New YorkGoogle Scholar
  14. Dickinson WJ, Weisbrod E (1976) Gene regulation in Drosophila: Independent expression of closely linked, related structural loci. Biochem Genet 14:709–721Google Scholar
  15. Doane WW (1969) Amylase variants in Drosophila melanogaster: Linkage studies and characterization of enzyme extracts. J Exp Zool 171:321–342Google Scholar
  16. Finnerty V (1976) Genetic units of Drosophila — simple cistrons. In: Novitski E, Ashburner M (eds) The Genetics and biology of Drosophila vol 1b. Academic Press, Inc, New York, p. 721–765Google Scholar
  17. Forrest HS, Hanly EW, Lagowski JM (1961a) Biochemical differences between the mutants rosy-2 and maroon-like of Drosophila melanogaster. Genetics 46:1455–1463Google Scholar
  18. Forrest HS, Hanly EW, Lagowski JM (1961b) 2,4-Dihydroxypteridine as an intermediate in the enzymically catalyzed oxidation of 4-hydroxypteridine. Biochim Biophys Acta 50:596–598Google Scholar
  19. Glassman E, Mitchell HK (1959) Mutants in Drosophila melanogaster deficient in xanthine dehydrogenase. Genetics 44:153–162Google Scholar
  20. Hanly EW (1964) A quantitative assay for the oxidase activity associated with xanthine dehydrogenase. Dros Inform Serv 39:82–83Google Scholar
  21. Lindsley DL, Grell EH (1968) Genetic Variations of Drosophila melanogaster. Carnegie Institution of Washington, Inc, Oak RidgeGoogle Scholar
  22. Lowry OH, Rosenbrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193:265–275Google Scholar
  23. MacIntyre RJ, O'Brien SJ (1976) Interacting gene-enzyme systems in Drosophila. Annu Rev Genet 10:281–318Google Scholar
  24. Patterson JT, Stone WS (1952) Evolution in the genus Drosophila. MacMillan Co, New YorkGoogle Scholar
  25. Reiner JM (1959) Behavior of enzyme systems. Burgess Publishing Co, MinneapolisGoogle Scholar
  26. Scazzocchio C (1974) The genetic determination of molybdoflavoenzymes in Aspergillus nidulans. In: PCH Mitchell (ed) Proc Climax First Int Conf on Chemistry and Uses of Molybdenum, Univ of Reading, England, Sept 1973. Climax Molybdenum Co, Ltd; LondonGoogle Scholar
  27. Throckmorton LH (1977) Drosophila systematics and biochemical evolution. Annu Rev Ecol Syst 8:235–254Google Scholar
  28. Warner CK, Watts DT, Finnerty V (1980) Molybdenum hydroxylases in Drosophila. I. Preliminary studies of pyridoxal oxidase. Mol Gen Genet 180:449–453Google Scholar

Copyright information

© Springer-Verlag 1980

Authors and Affiliations

  • E. W. Hanly
    • 1
  1. 1.Dept. of BiologyUniversity of UtahSalt Lake CityUSA

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