Molybdenum hydroxylases in Drosophila. III: Further characterization of the low xanthine dehydrogenase gene

The biochemical effects of several newly induced low xanthine dehydrogenase (lxd) mutations in Drosophila melanogaster were investigated. When homozygous, all lxd alleles simultaneously interrupt each of the molybdoenzyme activities to approximately the same levels: xanthine dehydrogenase, 25%; alde...

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Bibliographic Details
Published in:Biochemical genetics 1986-08, Vol.24 (7-8), p.509-527
Main Authors: SCHOTT, D. R, BALDWIN, M. C, FINNERTY, V
Format: Article
Language:English
Subjects:
Alleles
Animals
Biological and medical sciences
Classical genetics, quantitative genetics, hybrids
Coenzymes
Drosophila melanogaster - enzymology
Drosophila melanogaster - genetics
Ethyl Methanesulfonate - pharmacology
Fundamental and applied biological sciences. Psychology
Genes - drug effects
Genes - radiation effects
Genetic Complementation Test
Genetics of eukaryotes. Biological and molecular evolution
Genotype
Homozygote
Invertebrata
Ketone Oxidoreductases - genetics
Kinetics
Metalloproteins
Molybdenum - analysis
Mutation
Pteridines - analysis
Xanthine Dehydrogenase - genetics
Xanthine Dehydrogenase - metabolism
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Summary:The biochemical effects of several newly induced low xanthine dehydrogenase (lxd) mutations in Drosophila melanogaster were investigated. When homozygous, all lxd alleles simultaneously interrupt each of the molybdoenzyme activities to approximately the same levels: xanthine dehydrogenase, 25%; aldehyde oxidase, 12%; pyridoxal oxidase, 0%; and sulfite oxidase, 2% as compared to the wild type. In order to evaluate potentially small complementation or dosage effects, mutant stains were made coisogenic for 3R. These enzymes require a molybdenum cofactor, and lxd cofactor levels are also reduced to less than 10% of the wild type. These low levels of molybdoenzyme activities and cofactor activity are maintained throughout development from late larval to adult stages. The lxd alleles exhibit a dosage-dependent effect on molybdoenzyme activities, indicating that these mutants are leaky for wild-type function. In addition, cofactor activity is dependent upon the number of lxd+ genes present. The lxd mutation results in the production of more thermolabile XDH and AO enzyme activities, but this thermolability is not transferred with the cofactor to a reconstituted Neurospora molybdoenzyme. The lxd gene is localized to salivary region 68A4-9, 0.1 map unit distal to the superoxide dismutase (Sod) gene.
ISSN:0006-2928
1573-4927
DOI:10.1007/BF00504332