Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene.
Molecular cloning, tissue expression of human xanthine dehydrogenase.
Cloning and expression in vitro of human xanthine dehydrogenase/oxidase.
Identification of two mutations in human xanthine dehydrogenase gene responsible for classical type I xanthinuria.
XDH gene mutation is the underlying cause of classical xanthinuria: a second report.
Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry.
An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
Human xanthine oxidase changes its substrate specificity to aldehyde oxidase type upon mutation of amino acid residues in the active site: roles of active site residues in binding and activation of purine substrate.
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF MUTANT VAL-803 IN COMPLEX WITH FAD; 2FE-2S IRON-SULFUR CENTERS; SALICYLATE; MOLYBDOPTERIN AND CALCIUM IONS
Human milk xanthine dehydrogenase is incompletely converted to the oxidase form in the absence of proteolysis. A structural explanation.
X-RAY CRYSTALLOGRAPHY (3.59 ANGSTROMS) IN COMPLEX WITH FAD AND IRON-SULFUR CENTERS
Identification of a new point mutation in the human xanthine dehydrogenase gene responsible for a case of classical type I xanthinuria.
Mutational analysis of the xanthine dehydrogenase gene in a Turkish family with autosomal recessive classical xanthinuria.
The consensus coding sequences of human breast and colorectal cancers.
VARIANTS [LARGE SCALE ANALYSIS] PHE-763 AND GLY-791
Classical Xanthinuria in Nine Israeli Families and Two Isolated Cases from Germany: Molecular, Biochemical and Population Genetics Aspects.
VARIANTS XAN1 PHE-150; 478-TRP--VAL-1333 DEL; 722-LYS--VAL-1333 DEL AND 825-ARG--VAL-1333 DEL
Group enriched (breast, intestine, liver)
3 GO annotations based on evolutionary models
Expressed in jejunal mucosa and 126 other cell types or tissues
Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead
Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain
CO dehydrogenase flavoprotein, C-terminal domain
Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2
CO dehydrogenase flavoprotein C-terminal domain-like
CO dehydrogenase molybdoprotein N-domain-like
FAD-binding/transporter-associated domain-like
Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species. Has also low oxidase activity towards aldehydes (in vitro).
Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
Can be converted from the dehydrogenase form (D) to the oxidase form (O) irreversibly by proteolysis or reversibly through the oxidation of sulfhydryl groups.
Homodimer. Interacts with BTN1A1 (By similarity).
Subject to partial proteolysis; this alters the enzyme from the dehydrogenase form (D) to the oxidase form (O).
Contains sulfhydryl groups that are easily oxidized (in vitro); this alters the enzyme from the dehydrogenase form (D) to the oxidase form (O).
The disease is caused by variants affecting the gene represented in this entry.
Belongs to the xanthine dehydrogenase family.
In a breast cancer sample; somatic mutation.
Strongly decreased activity towards xanthine and hypoxanthine. Increased affinity and activity towards aromatic aldehydes.