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Sequence of XDH_RAT

EC Number:1.1.3.22

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
xanthine oxidase
P22985
Rattus norvegicus
1331
146243
Reaction

General information:

Sequence
show sequence in normal format
>P22985|xanthine oxidase|EC 1.1.3.22|Rattus norvegicus|Swiss-Prot
MTADELVFFVNGKKVVEKNADPETTLLVYLRRKLGLCGTKLGCGEGGCGACTVMISKYDR
LQNKIVHFSVNACLAPICSLHHVAVTTVEGIGNTQKLHPVQERIARSHGSQCGFCTPGIV
MSMYTLLRNQPEPTVEEIENAFQGNLCRCTGYRPILQGFRTFAKDGGCCGGSGNNPNCCM
NQTKDQTVSLSPSLFNPEDFKPLDPTQEPIFPPELLRLKDTPQKKLRFEGERVTWIQAST
MEELLDLKAQHPDAKLVVGNTEIGIEMKFKNMLFPLIVCPAWIPELNSVVHGPEGISFGA
SCPLSLVESVLAEEIAKLPEQKTEVFRGVMEQLRWFAGKQVKSVASIGGNIITASPISDL
NPVFMASGAKLTLVSRGTRRTVRMDHTFFPGYRKTLLRPEEILLSIEIPYSKEGEFFSAF
KQASRREDDIAKVTSGMRVLFKPGTIEVQELSLCFGGMADRTISALKTTPKQLSKSWNEE
LLQSVCAGLAEELQLAPDAPGGMVEFRRTLTLSFFFKFYLTVLQKLGRADLEDMCGKLDP
TFASATLLFQKDPPANVQLFQEVPKDQSEEDMVGRPLPHLAANMQASGEAVYCDDIPRYE
NELSLRLVTSTRAHAKITSIDTSEAKKVPGFVCFLTAEDVPNSNATGLFNDETVFAKDEV
TCVGHIIGAVVADTPEHAQRAARGVKITYEDLPAIITIQDAINNNSFYGSEIKIEKGDLK
KGFSEADNVVSGELYIGGQEHFYLETNCTIAVPKGEAGEMELFVSTQNTMKTQSFVAKML
GVPDNRIVVRVKRMGGGFGGKETRSTVVSTALALAAHKTGRPVRCMLDRDEDMLITGGRH
PFLAKYKVGFMKTGTVVALEVAHFSNGGNTEDLSRSIMERALFHMDNAYKIPNIRGTGRI
CKTNLPSNTAFRGFGGPQGMLIAEYWMSEVAITCGLPAEEVRRKNMYKEGDLTHFNQKLE
GFTLPRCWDECIASSQYLARKREVEKFNRENCWKKRGLCIIPTKFGISFTLPFLNQGGAL
VHVYTDGSVLLTHGGTEMGQGLHTKMVQVASRALKIPTSKIHISETSTNTVPNTSPTAAS
ASADLNGQGVYEACQTILKRLEPFKKKKPTGPWEAWVMDAYTSAVSLSATGFYKTPNLGY
SFETNSGNPFHYFSYGVACSEVEIDCLTGDHKNLRTDIVMDVGSSLNPAIDIGQVEGAFV
QGLGLFTMEELHYSPEGSLHTRGPSTYKIPAFGSIPIEFRVSLLRDCPNKRAIYASKAVG
EPPLFLASSIFFAIKDAIRAARAQHGDNAKQLFQLDSPATPEKIRNACVDQFTTLCVTGV
PENCKSWSVRI
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
464464
Amaya Y.,Yamazaki K.,Sato M.,Noda K.,Nishino T.,Nishino T.
Proteolytic conversion of xanthine dehydrogenase from the NAD-dependent type to the O2-dependent type. Amino acid sequence of rat liver xanthine dehydrogenase and identification of the cleavage sites of the enzyme protein during irreversible conversion by trypsin.
J. Biol. Chem.
265
14170-14175
1990
464465
Chow C.W.,Clark M.,Rinaldo J.,Chalkley R.
Identification of the rat xanthine dehydrogenase/oxidase promoter.
Nucleic Acids Res.
22
1846-1854
1994
464466
Frederiks W.M.,Vreeling-Sindelarova H.
Ultrastructural localization of xanthine oxidoreductase activity in isolated rat liver cells.
Acta Histochem.
104
29-37
2002
464467
Nishino T.,Okamoto K.,Kawaguchi Y.,Hori H.,Matsumura T.,Eger B.T.,Pai E.F.,Nishino T.
Mechanism of the conversion of xanthine dehydrogenase to xanthine oxidase: identification of the two cysteine disulfide bonds and crystal structure of a non-convertible rat liver xanthine dehydrogenase mutant.
J. Biol. Chem.
280
24888-24894
2005
464468
Asai R.,Nishino T.,Matsumura T.,Okamoto K.,Igarashi K.,Pai E.F.,Nishino T.
Two mutations convert mammalian xanthine oxidoreductase to highly superoxide-productive xanthine oxidase.
J. Biochem.
141
525-534
2007