Sequence of XDH_BOVIN
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
General information:
Sequence
show sequence in normal format
>P80457|xanthine oxidase|EC 1.17.3.2|Bos taurus|Swiss-Prot
MTADELVFFVNGKKVVEKNADPETTLLAYLRRKLGLRGTKLGCGEGGCGACTVMLSKYDR
LQDKIIHFSANACLAPICTLHHVAVTTVEGIGSTKTRLHPVQERIAKSHGSQCGFCTPGI
VMSMYTLLRNQPEPTVEEIEDAFQGNLCRCTGYRPILQGFRTFAKNGGCCGGNGNNPNCC
MNQKKDHTVTLSPSLFNPEEFMPLDPTQEPIFPPELLRLKDVPPKQLRFEGERVTWIQAS
TLKELLDLKAQHPEAKLVVGNTEIGIEMKFKNQLFPMIICPAWIPELNAVEHGPEGISFG
AACALSSVEKTLLEAVAKLPTQKTEVFRGVLEQLRWFAGKQVKSVASLGGNIITASPISD
LNPVFMASGTKLTIVSRGTRRTVPMDHTFFPSYRKTLLGPEEILLSIEIPYSREDEFFSA
FKQASRREDDIAKVTCGMRVLFQPGSMQVKELALCYGGMADRTISALKTTQKQLSKFWNE
KLLQDVCAGLAEELSLSPDAPGGMIEFRRTLTLSFFFKFYLTVLKKLGKDSKDKCGKLDP
TYTSATLLFQKDPPANIQLFQEVPNGQSKEDTVGRPLPHLAAAMQASGEAVYCDDIPRYE
NELFLRLVTSTRAHAKIKSIDVSEAQKVPGFVCFLSADDIPGSNETGLFNDETVFAKDTV
TCVGHIIGAVVADTPEHAERAAHVVKVTYEDLPAIITIEDAIKNNSFYGSELKIEKGDLK
KGFSEADNVVSGELYIGGQDHFYLETHCTIAIPKGEEGEMELFVSTQNAMKTQSFVAKML
GVPVNRILVRVKRMGGGFGGKETRSTLVSVAVALAAYKTGHPVRCMLDRNEDMLITGGRH
PFLARYKVGFMKTGTIVALEVDHYSNAGNSRDLSHSIMERALFHMDNCYKIPNIRGTGRL
CKTNLSSNTAFRGFGGPQALFIAENWMSEVAVTCGLPAEEVRWKNMYKEGDLTHFNQRLE
GFSVPRCWDECLKSSQYYARKSEVDKFNKENCWKKRGLCIIPTKFGISFTVPFLNQAGAL
IHVYTDGSVLVSHGGTEMGQGLHTKMVQVASKALKIPISKIYISETSTNTVPNSSPTAAS
VSTDIYGQAVYEACQTILKRLEPFKKKNPDGSWEDWVMAAYQDRVSLSTTGFYRTPNLGY
SFETNSGNAFHYFTYGVACSEVEIDCLTGDHKNLRTDIVMDVGSSLNPAIDIGQVEGAFV
QGLGLFTLEELHYSPEGSLHTRGPSTYKIPAFGSIPTEFRVSLLRDCPNKKAIYASKAVG
EPPLFLGASVFFAIKDAIRAARAQHTNNNTKELFRLDSPATPEKIRNACVDKFTTLCVTG
APGNCKPWSLRV
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
641138
Berglund L.,Rasmussen J.T.,Andersen M.D.,Rasmussen M.S.,Petersen T.E.
Purification of the bovine xanthine oxidoreductase from milk fat globule membranes and cloning of complementary deoxyribonucleic acid.
J. Dairy Sci.
79
198-204
1996
641139
Terao M.,Kurosaki M.,Zanotta S.,Garattini E.
The xanthine oxidoreductase gene: structure and regulation.
Biochem. Soc. Trans.
25
791-796
1997
641140
Turner N.A.,Doyle W.A.,Ventom A.M.,Bray R.C.
Properties of rabbit liver aldehyde oxidase and the relationship of the enzyme to xanthine oxidase and dehydrogenase.
Eur. J. Biochem.
232
646-657
1995
641141
Battelli M.G.,Lorenzoni E.,Stripe F.
Milk xanthine oxidase type D (dehydrogenase) and type O (oxidase). Purification, interconversion and some properties.
Biochem. J.
131
191-198
1973
641142
Kuwabara Y.,Nishino T.,Okamoto K.,Matsumura T.,Eger B.T.,Pai E.F.,Nishino T.
Unique amino acids cluster for switching from the dehydrogenase to oxidase form of xanthine oxidoreductase.
Proc. Natl. Acad. Sci. U.S.A.
100
8170-8175
2003
641143
Enroth C.,Eger B.T.,Okamoto K.,Nishino T.,Nishino T.,Pai E.F.
Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion.
Proc. Natl. Acad. Sci. U.S.A.
97
10723-10728
2000
641144
Okamoto K.,Eger B.T.,Nishino T.,Kondo S.,Pai E.F.,Nishino T.
An extremely potent inhibitor of xanthine oxidoreductase. Crystal structure of the enzyme-inhibitor complex and mechanism of inhibition.
J. Biol. Chem.
278
1848-1855
2003
641145
Okamoto K.,Matsumoto K.,Hille R.,Eger B.T.,Pai E.F.,Nishino T.
The crystal structure of xanthine oxidoreductase during catalysis: implications for reaction mechanism and enzyme inhibition.
Proc. Natl. Acad. Sci. U.S.A.
101
7931-7936
2004
641146
Pauff J.M.,Cao H.,Hille R.
Substrate orientation and catalysis at the molybdenum site in xanthine oxidase: crystal structures in complex with xanthine and lumazine.
J. Biol. Chem.
284
8760-8767
2009
