FB2025_01 , released February 20, 2025
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Citation
Schott, D.R., Baldwin, M.C., Finnerty, V. (1986). Molybdenum hydroxylases in Drosophila. III. Further characterization of the low xanthine dehydrogenase gene. Biochem. Genet. 24(): 509--527.
FlyBase ID
FBrf0043787
Publication Type
Research paper
Abstract
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.
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    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    Biochem. Genet.
    Title
    Biochemical Genetics
    Publication Year
    1967-
    ISBN/ISSN
    0006-2928
    Data From Reference