Skip to main content
Log in

Developmental regulation of phenylalanine hydroxylase activity in Drosophila melanogaster

  • Published:
Biochemical Genetics Aims and scope Submit manuscript

Abstract

Herein we demonstrate that Drosophila larvae possess a synthetic activity capable of converting phenylalanine to tyrosine. This system is readily extractable and displays many characteristics of phenylalanine hydroxylase systems described in other organisms, the most notable being that a tetrahydropteridine is required for full expression of activity. The level of phenylalanine hydroxylase activity present in the organism varies with the stage of development: from an undetected level of activity at the first larval instar, there is a rapid increase in phenylalanine hydroxylase activity which reaches a peak at the time of puparium formation, after which there is a rapid decrease again to an undetected level.

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

  • Belzecha, K., Laskowska, T., and Mochnacka, I. (1964). Hydroxylation of phenylalanine in insects and some vertebrates. Acta Biochem. Polon. 11191

    Google Scholar 

  • Bricteaux-Gregoire, S., Verly, W., and Florkin, M. (1956). Utilization of the carboxyl carbon of L-phenylalanine for the synthesis of the amino-acids of silk by Bombyx mori. Nature 1771237.

    Google Scholar 

  • Bublitz, C. (1969). A direct assay for liver phenylalanine hydroxylase. Biochim. Biophys. Acta 191249.

    Google Scholar 

  • Chen, P., and Hanimann, F. (1965). Ionenaustausch chromatographische Untersuchungen über die freien Aminosäuren und deren Derivate in Drosophila melanogaster. Z. Natureforsch. 20b307.

    Google Scholar 

  • Fan, C. L., and Brown, G. M. (1979). Partial purification and some properties of biopterin synthetase and dihydrobiopterin oxidase from Drosophila melanogaster. Biochem. Genet. 17351.

    Google Scholar 

  • Fukuda, T. (1956a). Biochemical studies on the formation of silk protein. III. The conversion of C14-labeled phenylalanine to tyrosine in the silkworm larva (Bombyx mori). J. Biochem. 43137.

    Google Scholar 

  • Fukuda, T. (1956b). Conversion of phenylalanine into tyrosine in the silk worm larva (Bombyx mori). Nature 177429.

    Google Scholar 

  • Kaufman, S. (1971). Phenylalanine hydroxylase (rat liver). Adv. Enzymol. 17603.

    Google Scholar 

  • Lowry, O., Rosenbrough, N., Farr, A., and Randall, R. (1951). Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193265.

    Google Scholar 

  • Mitchell, H. K. (1978). An apparatus for microinjection of Drosophila. In Ashburner, M., and Wright, T. R. F. (eds.), The Genetics and Biology of Drosophila, Vol 2A, Academic Press, New York, p. 150.

    Google Scholar 

  • Mitchell, H. K., and Mitchell, A. (1964). Mass culture and age selection in Drosophila. Drosophila Inform. Serv. 39135.

    Google Scholar 

  • Murdock, L., Hopkins, T., and Wirtz, R. (1970). Phenylalanine metabolism in cockroaches, Periplaneta americana: Tyrosine and benzoyl-β-glucoside biosynthesis. Comp. Biochem. Physiol. 36535.

    Google Scholar 

  • Tobler, J. E., Yim, J. J., Grell, E. H., and Jacobson, K. B. (1979). Developmental changes of sepiapterin synthetase activity associations with a variegated purple gene in Drosophila melanogaster. Biochem. Genet. 17197.

    Google Scholar 

  • Waalkes, T., and Udenfriend, S. (1957). A fluorometric method for the estimation of tyrosine in plasma and tissues. J. Lab. Clin. Med. 50733.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Geltosky, J.E., Mitchell, H.K. Developmental regulation of phenylalanine hydroxylase activity in Drosophila melanogaster . Biochem Genet 18, 781–791 (1980). https://doi.org/10.1007/BF00484593

Download citation

  • Received:

  • Revised:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00484593

Key words

Navigation