Sequence of XDH_BOVIN
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 MTADELVFFV NGKKVVEKNA DPETTLLAYL RRKLGLRGTK LGCGEGGCGA CTVMLSKYDR
60 LQDKIIHFSA NACLAPICTL HHVAVTTVEG IGSTKTRLHP VQERIAKSHG SQCGFCTPGI
120 VMSMYTLLRN QPEPTVEEIE DAFQGNLCRC TGYRPILQGF RTFAKNGGCC GGNGNNPNCC
180 MNQKKDHTVT LSPSLFNPEE FMPLDPTQEP IFPPELLRLK DVPPKQLRFE GERVTWIQAS
240 TLKELLDLKA QHPEAKLVVG NTEIGIEMKF KNQLFPMIIC PAWIPELNAV EHGPEGISFG
300 AACALSSVEK TLLEAVAKLP TQKTEVFRGV LEQLRWFAGK QVKSVASLGG NIITASPISD
360 LNPVFMASGT KLTIVSRGTR RTVPMDHTFF PSYRKTLLGP EEILLSIEIP YSREDEFFSA
420 FKQASRREDD IAKVTCGMRV LFQPGSMQVK ELALCYGGMA DRTISALKTT QKQLSKFWNE
480 KLLQDVCAGL AEELSLSPDA PGGMIEFRRT LTLSFFFKFY LTVLKKLGKD SKDKCGKLDP
540 TYTSATLLFQ KDPPANIQLF QEVPNGQSKE DTVGRPLPHL AAAMQASGEA VYCDDIPRYE
600 NELFLRLVTS TRAHAKIKSI DVSEAQKVPG FVCFLSADDI PGSNETGLFN DETVFAKDTV
660 TCVGHIIGAV VADTPEHAER AAHVVKVTYE DLPAIITIED AIKNNSFYGS ELKIEKGDLK
720 KGFSEADNVV SGELYIGGQD HFYLETHCTI AIPKGEEGEM ELFVSTQNAM KTQSFVAKML
780 GVPVNRILVR VKRMGGGFGG KETRSTLVSV AVALAAYKTG HPVRCMLDRN EDMLITGGRH
840 PFLARYKVGF MKTGTIVALE VDHYSNAGNS RDLSHSIMER ALFHMDNCYK IPNIRGTGRL
900 CKTNLSSNTA FRGFGGPQAL FIAENWMSEV AVTCGLPAEE VRWKNMYKEG DLTHFNQRLE
960 GFSVPRCWDE CLKSSQYYAR KSEVDKFNKE NCWKKRGLCI IPTKFGISFT VPFLNQAGAL
1020 IHVYTDGSVL VSHGGTEMGQ GLHTKMVQVA SKALKIPISK IYISETSTNT VPNSSPTAAS
1080 VSTDIYGQAV YEACQTILKR LEPFKKKNPD GSWEDWVMAA YQDRVSLSTT GFYRTPNLGY
1140 SFETNSGNAF HYFTYGVACS EVEIDCLTGD HKNLRTDIVM DVGSSLNPAI DIGQVEGAFV
1200 QGLGLFTLEE LHYSPEGSLH TRGPSTYKIP AFGSIPTEFR VSLLRDCPNK KAIYASKAVG
1260 EPPLFLGASV FFAIKDAIRA ARAQHTNNNT KELFRLDSPA TPEKIRNACV DKFTTLCVTG
1320 APGNCKPWSL RV
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
118591
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
118592
Terao M.,Kurosaki M.,Zanotta S.,Garattini E.
The xanthine oxidoreductase gene: structure and regulation.
Biochem. Soc. Trans.
25
791-796
1997
118593
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
118594
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
118595
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
118596
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
118597
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
118598
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
118599
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
