Sequence of XDH_RAT
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 DPETTLLVYL RRKLGLCGTK LGCGEGGCGA CTVMISKYDR
60 LQNKIVHFSV NACLAPICSL HHVAVTTVEG IGNTQKLHPV QERIARSHGS QCGFCTPGIV
120 MSMYTLLRNQ PEPTVEEIEN AFQGNLCRCT GYRPILQGFR TFAKDGGCCG GSGNNPNCCM
180 NQTKDQTVSL SPSLFNPEDF KPLDPTQEPI FPPELLRLKD TPQKKLRFEG ERVTWIQAST
240 MEELLDLKAQ HPDAKLVVGN TEIGIEMKFK NMLFPLIVCP AWIPELNSVV HGPEGISFGA
300 SCPLSLVESV LAEEIAKLPE QKTEVFRGVM EQLRWFAGKQ VKSVASIGGN IITASPISDL
360 NPVFMASGAK LTLVSRGTRR TVRMDHTFFP GYRKTLLRPE EILLSIEIPY SKEGEFFSAF
420 KQASRREDDI AKVTSGMRVL FKPGTIEVQE LSLCFGGMAD RTISALKTTP KQLSKSWNEE
480 LLQSVCAGLA EELQLAPDAP GGMVEFRRTL TLSFFFKFYL TVLQKLGRAD LEDMCGKLDP
540 TFASATLLFQ KDPPANVQLF QEVPKDQSEE DMVGRPLPHL AANMQASGEA VYCDDIPRYE
600 NELSLRLVTS TRAHAKITSI DTSEAKKVPG FVCFLTAEDV PNSNATGLFN DETVFAKDEV
660 TCVGHIIGAV VADTPEHAQR AARGVKITYE DLPAIITIQD AINNNSFYGS EIKIEKGDLK
720 KGFSEADNVV SGELYIGGQE HFYLETNCTI AVPKGEAGEM ELFVSTQNTM KTQSFVAKML
780 GVPDNRIVVR VKRMGGGFGG KETRSTVVST ALALAAHKTG RPVRCMLDRD EDMLITGGRH
840 PFLAKYKVGF MKTGTVVALE VAHFSNGGNT EDLSRSIMER ALFHMDNAYK IPNIRGTGRI
900 CKTNLPSNTA FRGFGGPQGM LIAEYWMSEV AITCGLPAEE VRRKNMYKEG DLTHFNQKLE
960 GFTLPRCWDE CIASSQYLAR KREVEKFNRE NCWKKRGLCI IPTKFGISFT LPFLNQGGAL
1020 VHVYTDGSVL LTHGGTEMGQ GLHTKMVQVA SRALKIPTSK IHISETSTNT VPNTSPTAAS
1080 ASADLNGQGV YEACQTILKR LEPFKKKKPT GPWEAWVMDA YTSAVSLSAT GFYKTPNLGY
1140 SFETNSGNPF HYFSYGVACS EVEIDCLTGD HKNLRTDIVM DVGSSLNPAI DIGQVEGAFV
1200 QGLGLFTMEE LHYSPEGSLH TRGPSTYKIP AFGSIPIEFR VSLLRDCPNK RAIYASKAVG
1260 EPPLFLASSI FFAIKDAIRA ARAQHGDNAK QLFQLDSPAT PEKIRNACVD QFTTLCVTGV
1320 PENCKSWSVR I
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
251250
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
251251
Chow C.W.,Clark M.,Rinaldo J.,Chalkley R.
Identification of the rat xanthine dehydrogenase/oxidase promoter.
Nucleic Acids Res.
22
1846-1854
1994
251252
Frederiks W.M.,Vreeling-Sindelarova H.
Ultrastructural localization of xanthine oxidoreductase activity in isolated rat liver cells.
Acta Histochem.
104
29-37
2002
251253
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
251254
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
