Abstract
The enzyme guanosine triphosphate cyclohydrolase (GTP cyclohydrolase), which in bacteria is known to be the first enzyme in the biosynthetic pathway for the synthesis of pteridines, has been discovered in extracts of Drosophila melanogaster. Most of the enzyme (80%) is located in the head of the adult fly. An analysis of enzyme activity during development in Drosophila has revealed the presence of a relatively small peak of activity at pupariation and a much larger peak that appears at about the time of eclosion. Enzyme activity declines rapidly as the fly ages. Analyses for the production of the typical pteridine pigments of Drosophila have indicated that the small peak of GTP cyclohydrolase activity evident at pupariation coincides with the appearance of isoxanthopterin, sepiapterin, and pterin, and the larger peak at eclosion roughly corresponds to the accumulation of drosopterin as well as to the appearance in larger amounts of pterin and sepiapterin. These observations strongly suggest that in Drosophila, like bacteria, GTP cyclohydrolase is involved in the biosynthesis of pteridines. Analyses of a variety of zeste mutants of Drosophila melanogaster have shown that these mutants all contain GTP cyclohydrolase equal approximately to the amount found in the wild-type fly. These observations do not support the suggestions made by Rasmusson et al. (1973) that zeste is the structural locus for GTP cyclohydrolase.
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References
Brown, G. M. (1971). The biosynthesis of pteridines. In Advances in Enzymology, Vol. 35, Academic Press, New York, pp. 35–77.
Burg, A. W., and Brown, G. M. (1968). The biosynthesis of folic acid. VIII. Purification and properties of the enzyme that catalyzes the production of formate from carbon atom 8 of guanosine triphosphate. J. Biol. Chem. 2432349.
Dickinson, W. J., and Sullivan, D. T. (1975). Gene-Enzyme Systems in Drosophila, Springer-Verlag, New York.
Fan, C. L., and Brown, G. M. (1976). Partial purification and properties of guanosine triphosphate cyclohydrolase from Drosophila melanogaster. Biochem. Genet. 14259.
Fukushima, T., and Shiota, T. (1972). Pterins in human urine. J. Biol. Chem. 2474549.
Gans, M. (1953). Etude genetique et physiologique du mutant z de Drosophila melanogaster. Bull. Biol. Fran. Belg. Suppl. 381.
Gregg, T. G., and Smucker, L. A. (1965). Pteridines and gene homologies in the eye color mutants of Drosophila hydei and Drosophila melanogaster. Genetics 521023.
Grell, E. H. (1962). The dose effect of ma-l + and ry + on xanthine dehydrogenase activity in Drosophila melanogaster. Z. Vererb. 93371.
Hadorn, E. (1958). Contribution to the physiological and biochemical genetics of pteridines and pigments in insects. 19th Int. Cong. Genet. 1337.
Hadorn, E., and Mitchell, H. K. (1951). Properties of mutants of Drosophila melanogaster and changes during development as revealed by paper chromatography. Proc. Natl. Acad. Sci. 37650.
Harmsen, R. (1966). Identification of fluorescing and u.v. absorbing substances in Pieris brassicae L. J. Insect Physiol. 1223.
Hodgetts, R. B. (1975). The response of dopa decarboxylase activity to variations in gene dosage in Drosophila: A possible location of the structural gene. Genetics 7945.
Lewis, E. G. (1960). A new standard food medium. Drosophila Inform. Serv. 34117.
Lindsley, D. L., and Grell, E. H. (1968). Genetic Variations of Drosophila melanogaster, Carnegie Institution of Washington Publication No. 627.
Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951). Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193265.
Nöthiger, R. (1970). Sucrose density separation—A method for collecting large numbers of Drosophila larvae. Drosophila Inform. Serv. 45177.
O'Brien, S. J., and Gethmann, R. C. (1973). Segmental aneuploidy as a probe for structural genes in Drosophila: Mitochondrial membrane enzymes. Genetics 75155.
Rasmusson, B., Montell, I., and Ohring, L. (1973). In vivo and in vitro studies of GTP-cyclohydrolase activity in some different eye color mutants of Drosophila melanogaster. Genetics 74:s225.
Sullivan, D. T., Kitos, R. J., and Sullivan, M. C. (1973). Developmental and genetic studies on kynurenine hydroxylase from Drosophila melanogaster. Genetics 75651.
Yen, T. T. T., and Glassman, E. (1965). Electrophoretic variants of xanthine dehydrogenase in Drosophila melanogaster. Genetics 52977.
Ziegler, I. (1961). Genetic aspects of ommachrome and pterin pigments. Advan. Genet. 10349.
Ziegler, I., and Harmsen, R. (1969). The biology of pteridines in insects. Advan. Insect Physiol. 6139.
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This work was supported by research grants from the National Institutes of Health (AM03442) and the National Science Foundation (GB33929).
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Fan, C.L., Hall, L.M., Skrinska, A.J. et al. Correlation of guanosine triphosphate cyclohydrolase activity and the synthesis of pterins in Drosophila melanogaster . Biochem Genet 14, 271–280 (1976). https://doi.org/10.1007/BF00484766
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DOI: https://doi.org/10.1007/BF00484766