Sequence of XDH_HUMAN
EC Number:1.17.1.4
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
xanthine + NAD+ + H2O = urate + NADH + H+
Other sequences found for EC No. 1.17.1.4
EC Number:1.17.1.4
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
xanthine + NAD+ + H2O = urate + NADH + H+
Other sequences found for EC No. 1.17.1.4
EC Number:1.17.3.2
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
xanthine + H2O + O2 = urate + H2O2
Other sequences found for EC No. 1.17.3.2
EC Number:1.17.3.2
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
xanthine + H2O + O2 = urate + H2O2
Other sequences found for EC No. 1.17.3.2
General information:
Sequence
0 MTADKLVFFV NGRKVVEKNA DPETTLLAYL RRKLGLSGTK LGCGEGGCGA CTVMLSKYDR
60 LQNKIVHFSA NACLAPICSL HHVAVTTVEG IGSTKTRLHP VQERIAKSHG SQCGFCTPGI
120 VMSMYTLLRN QPEPTMEEIE NAFQGNLCRC TGYRPILQGF RTFARDGGCC GGDGNNPNCC
180 MNQKKDHSVS LSPSLFKPEE FTPLDPTQEP IFPPELLRLK DTPRKQLRFE GERVTWIQAS
240 TLKELLDLKA QHPDAKLVVG NTEIGIEMKF KNMLFPMIVC PAWIPELNSV EHGPDGISFG
300 AACPLSIVEK TLVDAVAKLP AQKTEVFRGV LEQLRWFAGK QVKSVASVGG NIITASPISD
360 LNPVFMASGA KLTLVSRGTR RTVQMDHTFF PGYRKTLLSP EEILLSIEIP YSREGEYFSA
420 FKQASRREDD IAKVTSGMRV LFKPGTTEVQ ELALCYGGMA NRTISALKTT QRQLSKLWKE
480 ELLQDVCAGL AEELHLPPDA PGGMVDFRCT LTLSFFFKFY LTVLQKLGQE NLEDKCGKLD
540 PTFASATLLF QKDPPADVQL FQEVPKGQSE EDMVGRPLPH LAADMQASGE AVYCDDIPRY
600 ENELSLRLVT STRAHAKIKS IDTSEAKKVP GFVCFISADD VPGSNITGIC NDETVFAKDK
660 VTCVGHIIGA VVADTPEHTQ RAAQGVKITY EELPAIITIE DAIKNNSFYG PELKIEKGDL
720 KKGFSEADNV VSGEIYIGGQ EHFYLETHCT IAVPKGEAGE MELFVSTQNT MKTQSFVAKM
780 LGVPANRIVV RVKRMGGGFG GKETRSTVVS TAVALAAYKT GRPVRCMLDR DEDMLITGGR
840 HPFLARYKVG FMKTGTVVAL EVDHFSNVGN TQDLSQSIME RALFHMDNCY KIPNIRGTGR
900 LCKTNLPSNT AFRGFGGPQG MLIAECWMSE VAVTCGMPAE EVRRKNLYKE GDLTHFNQKL
960 EGFTLPRCWE ECLASSQYHA RKSEVDKFNK ENCWKKRGLC IIPTKFGISF TVPFLNQAGA
1020 LLHVYTDGSV LLTHGGTEMG QGLHTKMVQV ASRALKIPTS KIYISETSTN TVPNTSPTAA
1080 SVSADLNGQA VYAACQTILK RLEPYKKKNP SGSWEDWVTA AYMDTVSLSA TGFYRTPNLG
1140 YSFETNSGNP FHYFSYGVAC SEVEIDCLTG DHKNLRTDIV MDVGSSLNPA IDIGQVEGAF
1200 VQGLGLFTLE ELHYSPEGSL HTRGPSTYKI PAFGSIPIEF RVSLLRDCPN KKAIYASKAV
1260 GEPPLFLAAS IFFAIKDAIR AARAQHTGNN VKELFRLDSP ATPEKIRNAC VDKFTTLCVT
1320 GVPENCKPWS VRV
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
251220
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
251222
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
251223
Xu P.,Huecksteadt T.P.,Harrison R.,Hoidal J.R.
Biochem. Biophys. Res. Commun.
215
429-429
1995
251224
Saksela M.,Raivio K.O.
Cloning and expression in vitro of human xanthine dehydrogenase/oxidase.
Biochem. J.
315
235-239
1996
251226
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
251227
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
251228
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
251229
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
251230
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
251232
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
251233
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
251234
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
