6533b830fe1ef96bd12970d2

RESEARCH PRODUCT

Genetic and biochemical characterization of little isoxanthopterin (lix), a gene controlling dihydropterin oxidase activity in Drosophila melanogaster.

Baltasar EscricheEugenio OrdoñoFrancisco J. SilvaJuan Ferré

subject

MaleX ChromosomeGenotypeMutantSubstrate Specificitychemistry.chemical_compoundDihydropterin oxidase activityDrosophilidaeGeneticsAnimalsPterinMolecular BiologyCrosses Geneticchemistry.chemical_classificationbiologyPteridinesStructural geneTemperatureChromosome Mappingbiology.organism_classificationEnzyme assayEnzymeDrosophila melanogasterchemistryBiochemistryMutationbiology.proteinFemaleDrosophila melanogasterOxidoreductases

description

Dihydropterin oxidase catalyses the oxidation of 7,8-dihydropteridines into their fully oxidized products, and is involved in the biosynthesis of isoxanthopterin. Fifteen Drosophila melanogaster mutants, selected for their low pterin and isoxanthopterin content, were assayed for dihydropterin oxidase activity. The activity was around 100% in most mutants tested, slightly reduced in red, g and dke, and undetectable in lix. In flies carrying various doses of the lix+ allele, a correlation was found between enzyme activity and the number of lix+ copies in the genome. The results suggest that lix is the structural gene for the dihydropterin oxidase enzyme. Isoxanthopterin was quantitated in strains carrying deficiencies for the region in which lix has been mapped by recombination. This allowed us to assign the lix locus to the 7D10-7171-2 segment of the X chromosome.

10.1007/bf00290656https://pubmed.ncbi.nlm.nih.gov/1745247