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Xanthine dehydrogenase/oxidase [Includes: Xanthine dehydrogenase (XD) (EC 1.17.1.4); Xanthine oxidase (XO) (EC 1.17.3.2) (Xanthine oxidoreductase) (XOR)]

 XDH_HUMAN               Reviewed;        1333 AA.
P47989; Q16681; Q16712; Q4PJ16;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
22-NOV-2017, entry version 184.
RecName: Full=Xanthine dehydrogenase/oxidase;
Includes:
RecName: Full=Xanthine dehydrogenase;
Short=XD;
EC=1.17.1.4 {ECO:0000269|PubMed:8670112};
Includes:
RecName: Full=Xanthine oxidase;
Short=XO;
EC=1.17.3.2 {ECO:0000269|PubMed:17301077, ECO:0000269|PubMed:8670112};
AltName: Full=Xanthine oxidoreductase;
Short=XOR;
Name=XDH; Synonyms=XDHA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=8224915; DOI=10.1016/0378-1119(93)90652-J;
Ichida K., Amaya Y., Noda K., Minoshima S., Hosoya T., Sakai O.,
Shimizu N., Nishino T.;
"Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase):
structural analysis of the protein and chromosomal location of the
gene.";
Gene 133:279-284(1993).
[2]
SEQUENCE REVISION TO 191; 231 AND 1150.
Ichida K.;
Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ARG-172.
TISSUE=Liver;
PubMed=8135849; DOI=10.1006/bbrc.1994.1328;
Xu P., Huecksteadt T.P., Harrison R., Hoidal J.R.;
"Molecular cloning, tissue expression of human xanthine
dehydrogenase.";
Biochem. Biophys. Res. Commun. 199:998-1004(1994).
[4]
ERRATUM.
PubMed=7575623; DOI=10.1006/bbrc.1995.2482;
Xu P., Huecksteadt T.P., Harrison R., Hoidal J.R.;
Biochem. Biophys. Res. Commun. 215:429-429(1995).
[5]
NUCLEOTIDE SEQUENCE [MRNA], AND CATALYTIC ACTIVITY.
TISSUE=Small intestine;
PubMed=8670112; DOI=10.1042/bj3150235;
Saksela M., Raivio K.O.;
"Cloning and expression in vitro of human xanthine
dehydrogenase/oxidase.";
Biochem. J. 315:235-239(1996).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-133; ARG-172;
MET-235; MET-395; SER-555; ALA-584; GLN-607; ASN-617; ILE-623;
VAL-646; VAL-703; MET-910; LEU-1091; THR-1109; CYS-1176 AND TRP-1296.
NIEHS SNPs program;
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
[7]
INVOLVEMENT IN XAN1, AND VARIANT ARG-1150.
PubMed=9153281; DOI=10.1172/JCI119421;
Ichida K., Amaya Y., Kamatani N., Nishino T., Hosoya T., Sakai O.;
"Identification of two mutations in human xanthine dehydrogenase gene
responsible for classical type I xanthinuria.";
J. Clin. Invest. 99:2391-2397(1997).
[8]
INVOLVEMENT IN XAN1.
PubMed=10844591; DOI=10.1046/j.1523-1755.2000.00082.x;
Levartovsky D., Lagziel A., Sperling O., Liberman U., Yaron M.,
Hosoya T., Ichida K., Peretz H.;
"XDH gene mutation is the underlying cause of classical xanthinuria: a
second report.";
Kidney Int. 57:2215-2220(2000).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1074.
TISSUE=Milk;
PubMed=18780401; DOI=10.1002/pmic.200701057;
Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.;
"Identification of N-linked glycoproteins in human milk by hydrophilic
interaction liquid chromatography and mass spectrometry.";
Proteomics 8:3833-3847(2008).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF MUTANT VAL-803 IN COMPLEX
WITH FAD; 2FE-2S IRON-SULFUR CENTERS; SALICYLATE; MOLYBDOPTERIN AND
CALCIUM IONS, COFACTOR, CATALYTIC ACTIVITY, FUNCTION, AND SUBUNIT.
PubMed=17301077; DOI=10.1093/jb/mvm053;
Yamaguchi Y., Matsumura T., Ichida K., Okamoto K., Nishino T.;
"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.";
J. Biochem. 141:513-524(2007).
[12]
X-RAY CRYSTALLOGRAPHY (3.59 ANGSTROMS) IN COMPLEX WITH FAD AND
IRON-SULFUR CENTERS, TISSUE SPECIFICITY, ENZYME REGULATION, AND
DISULFIDE BONDS.
Pearson A.R., Godber B.L.J., Eisenthal R., Taylor G.L., Harrison R.;
"Human milk xanthine dehydrogenase is incompletely converted to the
oxidase form in the absence of proteolysis. A structural
explanation.";
Submitted (FEB-2009) to the PDB data bank.
[13]
VARIANT XAN1 CYS-149.
PubMed=11379872; DOI=10.1007/s004390100477;
Sakamoto N., Yamamoto T., Moriwaki Y., Teranishi T., Toyoda M.,
Onishi Y., Kuroda S., Sakaguchi K., Fujisawa T., Maeda M., Hada T.;
"Identification of a new point mutation in the human xanthine
dehydrogenase gene responsible for a case of classical type I
xanthinuria.";
Hum. Genet. 108:279-283(2001).
[14]
INVOLVEMENT IN XAN1.
PubMed=14551354; DOI=10.1093/ndt/gfg385;
Gok F., Ichida K., Topaloglu R.;
"Mutational analysis of the xanthine dehydrogenase gene in a Turkish
family with autosomal recessive classical xanthinuria.";
Nephrol. Dial. Transplant. 18:2278-2283(2003).
[15]
VARIANTS [LARGE SCALE ANALYSIS] PHE-763 AND GLY-791.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: 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). {ECO:0000269|PubMed:17301077}.
-!- CATALYTIC ACTIVITY: Xanthine + NAD(+) + H(2)O = urate + NADH.
{ECO:0000269|PubMed:8670112}.
-!- CATALYTIC ACTIVITY: Hypoxanthine + NAD(+) + H(2)O = xanthine +
NADH. {ECO:0000269|PubMed:8670112}.
-!- CATALYTIC ACTIVITY: Xanthine + H(2)O + O(2) = urate + H(2)O(2).
{ECO:0000269|PubMed:17301077, ECO:0000269|PubMed:8670112}.
-!- COFACTOR:
Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
Evidence={ECO:0000269|PubMed:17301077};
Note=Binds 2 [2Fe-2S] clusters. {ECO:0000269|PubMed:17301077};
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000269|PubMed:17301077};
-!- COFACTOR:
Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
Evidence={ECO:0000269|PubMed:17301077};
Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
{ECO:0000269|PubMed:17301077};
-!- ENZYME REGULATION: Can be converted from the dehydrogenase form
(D) to the oxidase form (O) irreversibly by proteolysis or
reversibly through the oxidation of sulfhydryl groups.
{ECO:0000250}.
-!- SUBUNIT: Homodimer. Interacts with BTN1A1 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Peroxisome
{ECO:0000250}. Secreted.
-!- TISSUE SPECIFICITY: Detected in milk (at protein level).
{ECO:0000269|Ref.12}.
-!- PTM: Subject to partial proteolysis; this alters the enzyme from
the dehydrogenase form (D) to the oxidase form (O). {ECO:0000250}.
-!- PTM: Contains sulfhydryl groups that are easily oxidized (in
vitro); this alters the enzyme from the dehydrogenase form (D) to
the oxidase form (O). {ECO:0000250}.
-!- DISEASE: Xanthinuria 1 (XAN1) [MIM:278300]: A disorder
characterized by excretion of very large amounts of xanthine in
the urine and a tendency to form xanthine stones. Uric acid is
strikingly diminished in serum and urine. XAN1 is due to isolated
xanthine dehydrogenase deficiency. Patients can metabolize
allopurinol. {ECO:0000269|PubMed:10844591,
ECO:0000269|PubMed:11379872, ECO:0000269|PubMed:14551354,
ECO:0000269|PubMed:9153281}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/xdh/";
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EMBL; D11456; BAA02013.2; -; mRNA.
EMBL; U06117; AAA75287.1; -; mRNA.
EMBL; U39487; AAB08399.1; -; mRNA.
EMBL; DQ089481; AAY68219.1; -; Genomic_DNA.
CCDS; CCDS1775.1; -.
PIR; S66573; XOHUDH.
RefSeq; NP_000370.2; NM_000379.3.
UniGene; Hs.250; -.
PDB; 2CKJ; X-ray; 3.59 A; A/B/C/D=2-1333.
PDB; 2E1Q; X-ray; 2.60 A; A/B/C/D=1-1333.
PDBsum; 2CKJ; -.
PDBsum; 2E1Q; -.
ProteinModelPortal; P47989; -.
SMR; P47989; -.
BioGrid; 113335; 3.
CORUM; P47989; -.
IntAct; P47989; 3.
STRING; 9606.ENSP00000368727; -.
BindingDB; P47989; -.
ChEMBL; CHEMBL1929; -.
DrugBank; DB00041; Aldesleukin.
DrugBank; DB00437; Allopurinol.
DrugBank; DB00993; Azathioprine.
DrugBank; DB00958; Carboplatin.
DrugBank; DB01136; Carvedilol.
DrugBank; DB00856; Chlorphenesin.
DrugBank; DB00515; Cisplatin.
DrugBank; DB00694; Daunorubicin.
DrugBank; DB00746; Deferoxamine.
DrugBank; DB03328; dioxothiomolybdenum(VI) ion.
DrugBank; DB00997; Doxorubicin.
DrugBank; DB03516; Eniluracil.
DrugBank; DB04854; Febuxostat.
DrugBank; DB03147; Flavin adenine dinucleotide.
DrugBank; DB04335; Inosine.
DrugBank; DB00583; L-Carnitine.
DrugBank; DB00170; Menadione.
DrugBank; DB01033; Mercaptopurine.
DrugBank; DB00157; NADH.
DrugBank; DB00336; Nitrofural.
DrugBank; DB05262; Oxypurinol.
DrugBank; DB01168; Procarbazine.
DrugBank; DB00339; Pyrazinamide.
DrugBank; DB00127; Spermine.
DrugBank; DB00831; Trifluoperazine.
DrugBank; DB03841; Y-700.
GuidetoPHARMACOLOGY; 2646; -.
iPTMnet; P47989; -.
PhosphoSitePlus; P47989; -.
BioMuta; XDH; -.
DMDM; 2506326; -.
EPD; P47989; -.
MaxQB; P47989; -.
PaxDb; P47989; -.
PeptideAtlas; P47989; -.
PRIDE; P47989; -.
DNASU; 7498; -.
Ensembl; ENST00000379416; ENSP00000368727; ENSG00000158125.
GeneID; 7498; -.
KEGG; hsa:7498; -.
UCSC; uc002rnv.2; human.
CTD; 7498; -.
DisGeNET; 7498; -.
EuPathDB; HostDB:ENSG00000158125.9; -.
GeneCards; XDH; -.
H-InvDB; HIX0117690; -.
HGNC; HGNC:12805; XDH.
HPA; HPA062641; -.
HPA; HPA069323; -.
MalaCards; XDH; -.
MIM; 278300; phenotype.
MIM; 607633; gene.
neXtProt; NX_P47989; -.
OpenTargets; ENSG00000158125; -.
Orphanet; 93601; Xanthinuria type I.
PharmGKB; PA37404; -.
eggNOG; KOG0430; Eukaryota.
eggNOG; COG4630; LUCA.
eggNOG; COG4631; LUCA.
GeneTree; ENSGT00390000003772; -.
HOGENOM; HOG000191197; -.
HOVERGEN; HBG004182; -.
InParanoid; P47989; -.
KO; K00106; -.
OMA; KPEDGEM; -.
OrthoDB; EOG091G01AW; -.
PhylomeDB; P47989; -.
TreeFam; TF353036; -.
BioCyc; MetaCyc:HS08270-MONOMER; -.
BRENDA; 1.17.1.4; 2681.
Reactome; R-HSA-74259; Purine catabolism.
Reactome; R-HSA-8851680; Butyrophilin (BTN) family interactions.
SABIO-RK; P47989; -.
ChiTaRS; XDH; human.
EvolutionaryTrace; P47989; -.
GeneWiki; Xanthine_dehydrogenase; -.
GenomeRNAi; 7498; -.
PRO; PR:P47989; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000158125; -.
CleanEx; HS_XDH; -.
Genevisible; P47989; HS.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
GO; GO:0016529; C:sarcoplasmic reticulum; IEA:Ensembl.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IDA:UniProtKB.
GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IDA:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0043546; F:molybdopterin cofactor binding; IDA:UniProtKB.
GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
GO; GO:0016903; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors; IBA:GO_Central.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0004854; F:xanthine dehydrogenase activity; IDA:UniProtKB.
GO; GO:0004855; F:xanthine oxidase activity; IDA:UniProtKB.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:UniProtKB.
GO; GO:0007595; P:lactation; IEA:Ensembl.
GO; GO:0045602; P:negative regulation of endothelial cell differentiation; IDA:UniProtKB.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IDA:UniProtKB.
GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IDA:UniProtKB.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:UniProtKB.
GO; GO:1900747; P:negative regulation of vascular endothelial growth factor signaling pathway; IDA:UniProtKB.
GO; GO:2001213; P:negative regulation of vasculogenesis; IDA:UniProtKB.
GO; GO:1900745; P:positive regulation of p38MAPK cascade; IDA:UniProtKB.
GO; GO:2000379; P:positive regulation of reactive oxygen species metabolic process; IDA:UniProtKB.
GO; GO:0006195; P:purine nucleotide catabolic process; TAS:Reactome.
GO; GO:0009115; P:xanthine catabolic process; IDA:UniProtKB.
Gene3D; 1.10.150.120; -; 1.
Gene3D; 3.10.20.30; -; 1.
Gene3D; 3.30.365.10; -; 4.
Gene3D; 3.30.43.10; -; 1.
Gene3D; 3.30.465.10; -; 1.
Gene3D; 3.90.1170.50; -; 1.
InterPro; IPR002888; 2Fe-2S-bd.
InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
InterPro; IPR006058; 2Fe2S_fd_BS.
InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
InterPro; IPR016208; Ald_Oxase/xanthine_DH.
InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
InterPro; IPR012675; Beta-grasp_dom_sf.
InterPro; IPR005107; CO_DH_flav_C.
InterPro; IPR036683; CO_DH_flav_C_dom_sf.
InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2.
InterPro; IPR016166; FAD-bd_2.
InterPro; IPR036318; FAD-bd_2-like_sf.
InterPro; IPR016167; FAD-bd_2_sub1.
InterPro; IPR002346; Mopterin_DH_FAD-bd.
InterPro; IPR022407; OxRdtase_Mopterin_BS.
InterPro; IPR014307; Xanthine_DH_ssu.
Pfam; PF01315; Ald_Xan_dh_C; 1.
Pfam; PF02738; Ald_Xan_dh_C2; 1.
Pfam; PF03450; CO_deh_flav_C; 1.
Pfam; PF00941; FAD_binding_5; 1.
Pfam; PF00111; Fer2; 1.
Pfam; PF01799; Fer2_2; 1.
PIRSF; PIRSF000127; Xanthine_DH; 1.
SMART; SM01008; Ald_Xan_dh_C; 1.
SMART; SM01092; CO_deh_flav_C; 1.
SUPFAM; SSF47741; SSF47741; 1.
SUPFAM; SSF54292; SSF54292; 1.
SUPFAM; SSF54665; SSF54665; 1.
SUPFAM; SSF55447; SSF55447; 1.
SUPFAM; SSF56003; SSF56003; 1.
SUPFAM; SSF56176; SSF56176; 1.
TIGRFAMs; TIGR02963; xanthine_xdhA; 1.
PROSITE; PS00197; 2FE2S_FER_1; 1.
PROSITE; PS51085; 2FE2S_FER_2; 1.
PROSITE; PS51387; FAD_PCMH; 1.
PROSITE; PS00559; MOLYBDOPTERIN_EUK; 1.
1: Evidence at protein level;
2Fe-2S; 3D-structure; Complete proteome; Cytoplasm; Disease mutation;
Disulfide bond; FAD; Flavoprotein; Glycoprotein; Iron; Iron-sulfur;
Metal-binding; Molybdenum; NAD; Oxidoreductase; Peroxisome;
Polymorphism; Reference proteome; Secreted.
CHAIN 1 1333 Xanthine dehydrogenase/oxidase.
/FTId=PRO_0000166084.
DOMAIN 4 91 2Fe-2S ferredoxin-type.
{ECO:0000255|PROSITE-ProRule:PRU00465}.
DOMAIN 229 414 FAD-binding PCMH-type.
{ECO:0000255|PROSITE-ProRule:PRU00718}.
NP_BIND 257 264 FAD. {ECO:0000269|PubMed:17301077,
ECO:0000269|Ref.12}.
NP_BIND 347 351 FAD. {ECO:0000269|PubMed:17301077,
ECO:0000269|Ref.12}.
ACT_SITE 1262 1262 Proton acceptor.
METAL 43 43 Iron-sulfur (2Fe-2S) 1.
METAL 48 48 Iron-sulfur (2Fe-2S) 1.
METAL 51 51 Iron-sulfur (2Fe-2S) 1.
METAL 73 73 Iron-sulfur (2Fe-2S) 1.
METAL 113 113 Iron-sulfur (2Fe-2S) 2.
METAL 116 116 Iron-sulfur (2Fe-2S) 2.
METAL 148 148 Iron-sulfur (2Fe-2S) 2.
METAL 150 150 Iron-sulfur (2Fe-2S) 2.
METAL 768 768 Molybdenum.
METAL 799 799 Molybdenum; via carbonyl oxygen.
METAL 913 913 Molybdenum; via amide nitrogen.
METAL 1080 1080 Molybdenum; via amide nitrogen.
BINDING 337 337 FAD. {ECO:0000269|PubMed:17301077,
ECO:0000269|Ref.12}.
BINDING 360 360 FAD. {ECO:0000269|PubMed:17301077,
ECO:0000269|Ref.12}.
BINDING 404 404 FAD; via amide nitrogen and carbonyl
oxygen. {ECO:0000250}.
BINDING 422 422 FAD. {ECO:0000269|PubMed:17301077,
ECO:0000269|Ref.12}.
BINDING 803 803 Substrate. {ECO:0000250}.
BINDING 881 881 Substrate.
BINDING 915 915 Substrate. {ECO:0000250}.
BINDING 1011 1011 Substrate.
CARBOHYD 1074 1074 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:18780401}.
DISULFID 509 1318 In oxidase form. {ECO:0000269|Ref.12}.
DISULFID 536 993 In oxidase form. {ECO:0000269|Ref.12}.
VARIANT 133 133 E -> K (in dbSNP:rs45447191).
{ECO:0000269|Ref.6}.
/FTId=VAR_023976.
VARIANT 149 149 R -> C (in XAN1; dbSNP:rs72549369).
{ECO:0000269|PubMed:11379872}.
/FTId=VAR_045900.
VARIANT 172 172 G -> R (in dbSNP:rs45523133).
{ECO:0000269|PubMed:8135849,
ECO:0000269|Ref.6}.
/FTId=VAR_023977.
VARIANT 235 235 T -> M (in dbSNP:rs45469499).
{ECO:0000269|Ref.6}.
/FTId=VAR_023978.
VARIANT 395 395 K -> M (in dbSNP:rs34929837).
{ECO:0000269|Ref.6}.
/FTId=VAR_023979.
VARIANT 555 555 P -> S (in dbSNP:rs45577338).
{ECO:0000269|Ref.6}.
/FTId=VAR_023980.
VARIANT 584 584 D -> A (in dbSNP:rs45491693).
{ECO:0000269|Ref.6}.
/FTId=VAR_023981.
VARIANT 607 607 R -> Q (in dbSNP:rs45442092).
{ECO:0000269|Ref.6}.
/FTId=VAR_023982.
VARIANT 617 617 K -> N (in dbSNP:rs45442398).
{ECO:0000269|Ref.6}.
/FTId=VAR_023983.
VARIANT 623 623 T -> I (in dbSNP:rs45448694).
{ECO:0000269|Ref.6}.
/FTId=VAR_023984.
VARIANT 646 646 I -> V (in dbSNP:rs17323225).
{ECO:0000269|Ref.6}.
/FTId=VAR_023985.
VARIANT 703 703 I -> V (in dbSNP:rs17011368).
{ECO:0000269|Ref.6}.
/FTId=VAR_023986.
VARIANT 763 763 L -> F (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035899.
VARIANT 791 791 R -> G (in a breast cancer sample;
somatic mutation; dbSNP:rs775646772).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035900.
VARIANT 910 910 T -> M (in dbSNP:rs669884).
{ECO:0000269|Ref.6}.
/FTId=VAR_023987.
VARIANT 1091 1091 V -> L (in dbSNP:rs45619033).
{ECO:0000269|Ref.6}.
/FTId=VAR_023988.
VARIANT 1109 1109 N -> T (in dbSNP:rs45547640).
{ECO:0000269|Ref.6}.
/FTId=VAR_023989.
VARIANT 1150 1150 P -> R (in dbSNP:rs1042036).
{ECO:0000269|PubMed:9153281}.
/FTId=VAR_045901.
VARIANT 1176 1176 R -> C (in dbSNP:rs45624433).
{ECO:0000269|Ref.6}.
/FTId=VAR_023990.
VARIANT 1296 1296 R -> W (in dbSNP:rs45564939).
{ECO:0000269|Ref.6}.
/FTId=VAR_023991.
MUTAGEN 803 803 E->V: Strongly decreased activity towards
xanthine and hypoxanthine. Increased
affinity and activity towards aromatic
aldehydes.
MUTAGEN 881 881 R->M: Abolishes xanthine oxidase
activity.
CONFLICT 259 259 V -> E (in Ref. 3; AAA75287).
{ECO:0000305}.
CONFLICT 333 334 QL -> HV (in Ref. 3; AAA75287).
{ECO:0000305}.
CONFLICT 495 495 H -> Q (in Ref. 3; AAA75287).
{ECO:0000305}.
CONFLICT 515 517 FFF -> LLL (in Ref. 3; AAA75287).
{ECO:0000305}.
STRAND 6 10 {ECO:0000244|PDB:2E1Q}.
STRAND 13 17 {ECO:0000244|PDB:2E1Q}.
HELIX 26 32 {ECO:0000244|PDB:2E1Q}.
STRAND 44 48 {ECO:0000244|PDB:2E1Q}.
STRAND 52 59 {ECO:0000244|PDB:2E1Q}.
TURN 60 63 {ECO:0000244|PDB:2E1Q}.
STRAND 64 71 {ECO:0000244|PDB:2E1Q}.
TURN 72 74 {ECO:0000244|PDB:2E1Q}.
HELIX 77 79 {ECO:0000244|PDB:2E1Q}.
STRAND 84 86 {ECO:0000244|PDB:2E1Q}.
HELIX 88 90 {ECO:0000244|PDB:2E1Q}.
HELIX 100 107 {ECO:0000244|PDB:2E1Q}.
HELIX 117 130 {ECO:0000244|PDB:2E1Q}.
HELIX 136 141 {ECO:0000244|PDB:2E1Q}.
TURN 142 145 {ECO:0000244|PDB:2E1Q}.
STRAND 149 151 {ECO:0000244|PDB:2E1Q}.
HELIX 154 160 {ECO:0000244|PDB:2E1Q}.
HELIX 161 163 {ECO:0000244|PDB:2E1Q}.
HELIX 198 200 {ECO:0000244|PDB:2E1Q}.
HELIX 206 208 {ECO:0000244|PDB:2E1Q}.
HELIX 214 218 {ECO:0000244|PDB:2E1Q}.
STRAND 227 230 {ECO:0000244|PDB:2E1Q}.
STRAND 235 238 {ECO:0000244|PDB:2E1Q}.
HELIX 242 251 {ECO:0000244|PDB:2E1Q}.
HELIX 264 270 {ECO:0000244|PDB:2E1Q}.
STRAND 276 280 {ECO:0000244|PDB:2E1Q}.
HELIX 285 288 {ECO:0000244|PDB:2E1Q}.
STRAND 290 292 {ECO:0000244|PDB:2E1Q}.
STRAND 294 300 {ECO:0000244|PDB:2E1Q}.
HELIX 305 318 {ECO:0000244|PDB:2E1Q}.
HELIX 321 323 {ECO:0000244|PDB:2E1Q}.
HELIX 325 335 {ECO:0000244|PDB:2E1Q}.
HELIX 340 345 {ECO:0000244|PDB:2E1Q}.
HELIX 348 354 {ECO:0000244|PDB:2E1Q}.
HELIX 362 367 {ECO:0000244|PDB:2E1Q}.
STRAND 371 375 {ECO:0000244|PDB:2E1Q}.
STRAND 380 384 {ECO:0000244|PDB:2E1Q}.
HELIX 387 389 {ECO:0000244|PDB:2E1Q}.
STRAND 403 410 {ECO:0000244|PDB:2E1Q}.
STRAND 416 423 {ECO:0000244|PDB:2E1Q}.
STRAND 425 429 {ECO:0000244|PDB:2E1Q}.
STRAND 433 442 {ECO:0000244|PDB:2E1Q}.
STRAND 448 465 {ECO:0000244|PDB:2E1Q}.
HELIX 467 471 {ECO:0000244|PDB:2E1Q}.
TURN 472 475 {ECO:0000244|PDB:2E1Q}.
STRAND 477 479 {ECO:0000244|PDB:2E1Q}.
HELIX 480 493 {ECO:0000244|PDB:2E1Q}.
HELIX 505 529 {ECO:0000244|PDB:2E1Q}.
TURN 541 543 {ECO:0000244|PDB:2E1Q}.
HELIX 544 547 {ECO:0000244|PDB:2E1Q}.
STRAND 556 560 {ECO:0000244|PDB:2E1Q}.
HELIX 583 587 {ECO:0000244|PDB:2E1Q}.
HELIX 594 596 {ECO:0000244|PDB:2E1Q}.
STRAND 604 610 {ECO:0000244|PDB:2E1Q}.
STRAND 612 622 {ECO:0000244|PDB:2E1Q}.
HELIX 626 628 {ECO:0000244|PDB:2E1Q}.
STRAND 632 637 {ECO:0000244|PDB:2E1Q}.
HELIX 638 640 {ECO:0000244|PDB:2E1Q}.
STRAND 645 648 {ECO:0000244|PDB:2E1Q}.
STRAND 653 656 {ECO:0000244|PDB:2E1Q}.
STRAND 659 661 {ECO:0000244|PDB:2E1Q}.
STRAND 667 675 {ECO:0000244|PDB:2E1Q}.
HELIX 676 684 {ECO:0000244|PDB:2E1Q}.
STRAND 687 692 {ECO:0000244|PDB:2E1Q}.
HELIX 699 705 {ECO:0000244|PDB:2E1Q}.
STRAND 708 718 {ECO:0000244|PDB:2E1Q}.
HELIX 720 726 {ECO:0000244|PDB:2E1Q}.
STRAND 728 737 {ECO:0000244|PDB:2E1Q}.
STRAND 749 754 {ECO:0000244|PDB:2E1Q}.
STRAND 761 765 {ECO:0000244|PDB:2E1Q}.
HELIX 770 781 {ECO:0000244|PDB:2E1Q}.
HELIX 785 787 {ECO:0000244|PDB:2E1Q}.
STRAND 788 793 {ECO:0000244|PDB:2E1Q}.
TURN 799 802 {ECO:0000244|PDB:2E1Q}.
HELIX 807 820 {ECO:0000244|PDB:2E1Q}.
STRAND 824 827 {ECO:0000244|PDB:2E1Q}.
HELIX 830 837 {ECO:0000244|PDB:2E1Q}.
STRAND 843 851 {ECO:0000244|PDB:2E1Q}.
STRAND 857 871 {ECO:0000244|PDB:2E1Q}.
HELIX 875 884 {ECO:0000244|PDB:2E1Q}.
STRAND 893 903 {ECO:0000244|PDB:2E1Q}.
TURN 913 916 {ECO:0000244|PDB:2E1Q}.
HELIX 917 935 {ECO:0000244|PDB:2E1Q}.
HELIX 939 945 {ECO:0000244|PDB:2E1Q}.
HELIX 965 976 {ECO:0000244|PDB:2E1Q}.
HELIX 978 991 {ECO:0000244|PDB:2E1Q}.
STRAND 993 1009 {ECO:0000244|PDB:2E1Q}.
HELIX 1013 1015 {ECO:0000244|PDB:2E1Q}.
STRAND 1017 1024 {ECO:0000244|PDB:2E1Q}.
STRAND 1030 1035 {ECO:0000244|PDB:2E1Q}.
STRAND 1039 1041 {ECO:0000244|PDB:2E1Q}.
HELIX 1043 1055 {ECO:0000244|PDB:2E1Q}.
HELIX 1059 1061 {ECO:0000244|PDB:2E1Q}.
TURN 1069 1071 {ECO:0000244|PDB:2E1Q}.
HELIX 1083 1108 {ECO:0000244|PDB:2E1Q}.
HELIX 1114 1123 {ECO:0000244|PDB:2E1Q}.
STRAND 1129 1135 {ECO:0000244|PDB:2E1Q}.
TURN 1143 1146 {ECO:0000244|PDB:2E1Q}.
STRAND 1152 1166 {ECO:0000244|PDB:2E1Q}.
TURN 1167 1169 {ECO:0000244|PDB:2E1Q}.
STRAND 1172 1182 {ECO:0000244|PDB:2E1Q}.
HELIX 1189 1208 {ECO:0000244|PDB:2E1Q}.
TURN 1225 1227 {ECO:0000244|PDB:2E1Q}.
HELIX 1233 1235 {ECO:0000244|PDB:2E1Q}.
STRAND 1238 1244 {ECO:0000244|PDB:2E1Q}.
HELIX 1254 1256 {ECO:0000244|PDB:2E1Q}.
HELIX 1263 1268 {ECO:0000244|PDB:2E1Q}.
HELIX 1269 1286 {ECO:0000244|PDB:2E1Q}.
HELIX 1303 1309 {ECO:0000244|PDB:2E1Q}.
HELIX 1315 1317 {ECO:0000244|PDB:2E1Q}.
SEQUENCE 1333 AA; 146424 MW; 806FF2C7413F84C5 CRC64;
MTADKLVFFV NGRKVVEKNA DPETTLLAYL RRKLGLSGTK LGCGEGGCGA CTVMLSKYDR
LQNKIVHFSA NACLAPICSL HHVAVTTVEG IGSTKTRLHP VQERIAKSHG SQCGFCTPGI
VMSMYTLLRN QPEPTMEEIE NAFQGNLCRC TGYRPILQGF RTFARDGGCC GGDGNNPNCC
MNQKKDHSVS LSPSLFKPEE FTPLDPTQEP IFPPELLRLK DTPRKQLRFE GERVTWIQAS
TLKELLDLKA QHPDAKLVVG NTEIGIEMKF KNMLFPMIVC PAWIPELNSV EHGPDGISFG
AACPLSIVEK TLVDAVAKLP AQKTEVFRGV LEQLRWFAGK QVKSVASVGG NIITASPISD
LNPVFMASGA KLTLVSRGTR RTVQMDHTFF PGYRKTLLSP EEILLSIEIP YSREGEYFSA
FKQASRREDD IAKVTSGMRV LFKPGTTEVQ ELALCYGGMA NRTISALKTT QRQLSKLWKE
ELLQDVCAGL AEELHLPPDA PGGMVDFRCT LTLSFFFKFY LTVLQKLGQE NLEDKCGKLD
PTFASATLLF QKDPPADVQL FQEVPKGQSE EDMVGRPLPH LAADMQASGE AVYCDDIPRY
ENELSLRLVT STRAHAKIKS IDTSEAKKVP GFVCFISADD VPGSNITGIC NDETVFAKDK
VTCVGHIIGA VVADTPEHTQ RAAQGVKITY EELPAIITIE DAIKNNSFYG PELKIEKGDL
KKGFSEADNV VSGEIYIGGQ EHFYLETHCT IAVPKGEAGE MELFVSTQNT MKTQSFVAKM
LGVPANRIVV RVKRMGGGFG GKETRSTVVS TAVALAAYKT GRPVRCMLDR DEDMLITGGR
HPFLARYKVG FMKTGTVVAL EVDHFSNVGN TQDLSQSIME RALFHMDNCY KIPNIRGTGR
LCKTNLPSNT AFRGFGGPQG MLIAECWMSE VAVTCGMPAE EVRRKNLYKE GDLTHFNQKL
EGFTLPRCWE ECLASSQYHA RKSEVDKFNK ENCWKKRGLC IIPTKFGISF TVPFLNQAGA
LLHVYTDGSV LLTHGGTEMG QGLHTKMVQV ASRALKIPTS KIYISETSTN TVPNTSPTAA
SVSADLNGQA VYAACQTILK RLEPYKKKNP SGSWEDWVTA AYMDTVSLSA TGFYRTPNLG
YSFETNSGNP FHYFSYGVAC SEVEIDCLTG DHKNLRTDIV MDVGSSLNPA IDIGQVEGAF
VQGLGLFTLE ELHYSPEGSL HTRGPSTYKI PAFGSIPIEF RVSLLRDCPN KKAIYASKAV
GEPPLFLAAS IFFAIKDAIR AARAQHTGNN VKELFRLDSP ATPEKIRNAC VDKFTTLCVT
GVPENCKPWS VRV


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