Use of rosy mutant strains of Drosophila melanogaster to probe the structure and function of xanthine dehydrogenase.

doi:10.1042/bj2850507

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Article

Use of rosy mutant strains of Drosophila melanogaster to probe the structure and function of xanthine dehydrogenase.

The Biochemical journal - 15 Jul 1992

Hughes R K, Doyle W A, Chovnick A, Whittle J R, Burke J F, Bray R C

Abstract excerpt

The usefulness in structure/function studies of molybdenum-containing hydroxylases in work with rosy mutant strains of Drosophila melanogaster has been investigated. At least 23 such strains are available, each corresponding to a single known amino acid change in the xanthine dehydrogenase sequence. Sequence comparisons permit identification, with some certainty, of regions associated with the iron-sulphur...

Topics

Amino Acid Sequence
Animals
Binding Sites
Chromatography, Gel
Coenzymes
Drosophila melanogaster
Flavin-Adenine Dinucleotide
Iron-Sulfur Proteins
Metalloproteins
Molecular Sequence Data
Molybdenum

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Molybdenum Cofactors

Mutation

NAD

Pteridines

Sequence Alignment

Structure-Activity Relationship

Xanthine Dehydrogenase

Source

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Identifiers

PMID: 1637342
DOI: 10.1042/bj2850507
PMCID: PMC1132817

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1637342-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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