EzCatDB: S00187
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DB codeS00187
CATH domainDomain 13.10.270.10 : Urate OxidaseCatalytic domain
E.C.1.7.3.3
CSA1uox
MACiEM0118

CATH domainRelated DB codes (homologues)
3.10.270.10 : Urate OxidaseD00541

Enzyme Name
UniProtKBKEGG

B8HFX6Q00511
Protein name
Uricaseurate oxidase
uric acid oxidase
uricase
uricase II
SynonymsUrate oxidase
EC 1.7.3.3
EC 1.7.3.3
Urate oxidase
RefSeqYP_002489258.1 (Protein)
NC_011886.1 (DNA/RNA sequence)

PfamPF01014 (Uricase)
[Graphical view]
PF01014 (Uricase)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00230Purine metabolism
MAP00232Caffeine metabolism

UniProtKB:Accession NumberB8HFX6Q00511
Entry nameB8HFX6_9MICCURIC_ASPFL
Activity
Urate + O(2) + H(2)O = 5-hydroxyisourate + H(2)O(2).
Subunit
Homotetramer.
Subcellular location
Peroxisome.
Cofactor


Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00366C00007C00001C11821C00027
CompoundUrateO2H2O5-HydroxyisourateH2O2
Typeamide group,aromatic ring (with nitrogen atoms)othersH2Oamide group,aromatic ring (with nitrogen atoms),imine groupothers
ChEBI62589
46823
46817
46814
46811
17775
27140
26689
15379
15377
18072
16240
PubChem1175
977
962
22247451
250388
784
22326046
             
1vaxAUnboundUnbound UnboundUnbound
1vaxBUnboundUnbound UnboundUnbound
1vaxCUnboundUnbound UnboundUnbound
1vaxDUnboundUnbound UnboundUnbound
1vaxEUnboundUnbound UnboundUnbound
1vaxFUnboundUnbound UnboundUnbound
1vaxGUnboundUnbound UnboundUnbound
1vaxHUnboundUnbound UnboundUnbound
1vayAAnalogue:AZAUnbound UnboundUnbound
1vayBAnalogue:AZAUnbound UnboundUnbound
1vayCAnalogue:AZAUnbound UnboundUnbound
1vayDAnalogue:AZAUnbound UnboundUnbound
1vayEAnalogue:AZAUnbound UnboundUnbound
1vayFAnalogue:AZAUnbound UnboundUnbound
1vayGAnalogue:AZAUnbound UnboundUnbound
1vayHAnalogue:AZAUnbound UnboundUnbound
1r4sAAnalogue:MUAUnbound UnboundUnbound
1r4uAAnalogue:OXCUnbound UnboundUnbound
1r51AAnalogue:AZAUnbound UnboundUnbound
1r56AUnboundUnbound UnboundUnbound
1r56BUnboundUnbound UnboundUnbound
1r56CUnboundUnbound UnboundUnbound
1r56DUnboundUnbound UnboundUnbound
1r56EUnboundUnbound UnboundUnbound
1r56FUnboundUnbound UnboundUnbound
1r56GUnboundUnbound UnboundUnbound
1r56HUnboundUnbound UnboundUnbound
1uoxAUnboundUnbound UnboundUnbound
1wrrAAnalogue:UNCUnbound UnboundUnbound
1ws2AAnalogue:URNUnbound UnboundUnbound
1ws2BAnalogue:URNUnbound UnboundUnbound
1ws2CAnalogue:URNUnbound UnboundUnbound
1ws2DAnalogue:URNUnbound UnboundUnbound
1ws3AAnalogue:URAUnbound UnboundUnbound
1ws3BAnalogue:URAUnbound UnboundUnbound
1ws3CAnalogue:URAUnbound UnboundUnbound
1ws3DAnalogue:URAUnbound UnboundUnbound
1xt4AAnalogue:GUNUnbound UnboundUnbound
1xxjAAnalogue:UNCUnbound UnboundUnbound
1xxjBAnalogue:UNCUnbound UnboundUnbound
1xxjCAnalogue:UNCUnbound UnboundUnbound
1xxjDAnalogue:UNCUnbound UnboundUnbound
1xy3AAnalogue:GUNUnbound UnboundUnbound
1xy3BAnalogue:GUNUnbound UnboundUnbound
1xy3CAnalogue:GUNUnbound UnboundUnbound
1xy3DAnalogue:GUNUnbound UnboundUnbound
1xy3EAnalogue:GUNUnbound UnboundUnbound
1xy3FAnalogue:GUNUnbound UnboundUnbound
1xy3GAnalogue:GUNUnbound UnboundUnbound
1xy3HAnalogue:GUNUnbound UnboundUnbound

Active-site residues
resource
Swiss-prot;Q00511 & literature [11], [18], [19]
pdbCatalytic residuesMain-chain involved in catalysis
          
1vaxALYS  22;THR  67;ARG 180;GLN 223;ASN 249
THR  67
1vaxBLYS  22;THR  67;ARG 180;GLN 223;ASN 249
THR  67
1vaxCLYS  22;THR  67;ARG 180;GLN 223;ASN 249
THR  67
1vaxDLYS  22;THR  67;ARG 180;GLN 223;ASN 249
THR  67
1vaxELYS  22;THR  67;ARG 180;GLN 223;ASN 249
THR  67
1vaxFLYS  22;THR  67;ARG 180;GLN 223;ASN 249
THR  67
1vaxGLYS  22;THR  67;ARG 180;GLN 223;ASN 249
THR  67
1vaxHLYS  22;THR  67;ARG 180;GLN 223;ASN 249
THR  67
1vayALYS  22;THR  67;ARG 180;GLN 223;ASN 249
THR  67
1vayBLYS  22;THR  67;ARG 180;GLN 223;ASN 249
THR  67
1vayCLYS  22;THR  67;ARG 180;GLN 223;ASN 249
THR  67
1vayDLYS  22;THR  67;ARG 180;GLN 223;ASN 249
THR  67
1vayELYS  22;THR  67;ARG 180;GLN 223;ASN 249
THR  67
1vayFLYS  22;THR  67;ARG 180;GLN 223;ASN 249
THR  67
1vayGLYS  22;THR  67;ARG 180;GLN 223;ASN 249
THR  67
1vayHLYS  22;THR  67;ARG 180;GLN 223;ASN 249
THR  67
1r4sALYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1r4uALYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1r51ALYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1r56ALYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1r56BLYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1r56CLYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1r56DLYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1r56ELYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1r56FLYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1r56GLYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1r56HLYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1uoxALYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1wrrALYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1ws2ALYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1ws2BLYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1ws2CLYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1ws2DLYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1ws3ALYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1ws3BLYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1ws3CLYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1ws3DLYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1xt4ALYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1xxjALYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1xxjBLYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1xxjCLYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1xxjDLYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1xy3ALYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1xy3BLYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1xy3CLYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1xy3DLYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1xy3ELYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1xy3FLYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1xy3GLYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57
1xy3HLYS  10;THR  57;ARG 176;GLN 228;ASN 254
THR  57

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[8]Fig.4, p.950-951
[9]Scheme 1
[18]Scheme 1, Fig.5, p.4097-4100
[19]p.460-462

references
[1]
PubMed ID5640165
JournalBiochim Biophys Acta
Year1968
Volume151
Pages63-9
AuthorsNose K, Arima K
TitleStudies on bacterial urate:oxygen oxidoreductase. II. Observations concerning the properties and components of the active site.
[2]
PubMed ID4696756
JournalBiochemistry
Year1973
Volume12
Pages1358-63
AuthorsPitts OM, Priest DG
TitleUricase reaction intermediate. Mechanism of borate and hydroxide ion catalysis.
[3]
PubMed ID4834240
JournalNature
Year1974
Volume249
Pages490-1
AuthorsNaparstek A, Romette JL, Kernevez JP, Thomas D
TitleMemory in enzyme membranes.
[4]
PubMed ID455938
JournalComput Biol Med
Year1979
Volume9
Pages145-53
AuthorsLam CF, Cross AP
TitleComparative study of parameter estimation procedures in enzymic kinetics.
[5]
PubMed ID7194181
JournalEnzyme
Year1981
Volume26
Pages49-53
AuthorsNishimura H, Matsushima A, Inada Y
TitleImproved modification of yeast uricase with polyethylene glycol, accompanied with nonimmunoreactivity towards anti-uricase serum and high enzymic activity.
[6]
PubMed ID9222322
JournalFEBS Lett
Year1981
Volume134
Pages50-2
AuthorsYoshida K, Nishimura H, Takahashi K, Matsushima A, Inada Y
TitleModification of amino groups in Candida utilis uricase with naphthoquinone disulfonic acid in relation to the enzymic activity.
[7]
PubMed ID9125493
JournalBiochemistry
Year1997
Volume36
Pages4731-8
AuthorsKahn K, Tipton PA
TitleKinetic mechanism and cofactor content of soybean root nodule urate oxidase.
[8]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
Medline ID98025064
PubMed ID9360612
JournalNat Struct Biol
Year1997
Volume4
Pages947-52
AuthorsColloc'h N, el Hajji M, Bachet B, L'Hermite G, Schiltz M, Prange T, Castro B, Mornon JP
TitleCrystal structure of the protein drug urate oxidase-inhibitor complex at 2.05 A resolution.
Related PDB1uox
Related UniProtKBQ00511
[9]
PubMed ID9709003
JournalBiochemistry
Year1998
Volume37
Pages11651-9
AuthorsKahn K, Tipton PA
TitleSpectroscopic characterization of intermediates in the urate oxidase reaction.
[10]
PubMed ID10361492
JournalAnal Chem
Year1999
Volume71
Pages1928-34
AuthorsNakaminami T, Ito S, Kuwabata S, Yoneyama H
TitleUricase-catalyzed oxidation of uric acid using an artificial electron acceptor and fabrication of amperometric uric acid sensors with use of a redox ladder polymer.
[11]
PubMed ID10227848
JournalJ Membr Biol
Year1999
Volume169
Pages13-27
AuthorsLeal-Pinto E, Cohen BE, Abramson RG
TitleFunctional analysis and molecular modeling of a cloned urate transporter/channel.
[12]
PubMed ID10737935
JournalProteins
Year2000
Volume39
Pages142-54
AuthorsColloc'h N, Poupon A, Mornon JP
TitleSequence and structural features of the T-fold, an original tunnelling building unit.
[13]
PubMed ID11856833
JournalActa Crystallogr D Biol Crystallogr
Year2002
Volume58
Pages472-9
AuthorsVivares D, Bonnete F
TitleX-ray scattering studies of Aspergillus flavus urate oxidase: towards a better understanding of PEG effects on the crystallization of large proteins.
[14]
PubMed ID12060597
JournalAm J Physiol Renal Physiol
Year2002
Volume283
PagesF150-63
AuthorsLeal-Pinto E, Cohen BE, Lipkowitz MS, Abramson RG
TitleFunctional analysis and molecular model of the human urate transporter/channel, hUAT.
[15]
PubMed ID12149119
JournalBiotechnol Appl Biochem
Year2002
Volume36
Pages21-31
AuthorsBayol A, Capdevielle J, Malazzi P, Buzy A, Claude Bonnet M, Colloc'h N, Mornon JP, Loyaux D, Ferrara P
TitleModification of a reactive cysteine explains differences between rasburicase and Uricozyme, a natural Aspergillus flavus uricase.
[16]
PubMed ID12208494
JournalFEBS Lett
Year2002
Volume526
Pages5-10
AuthorsColloc'h N, Mornon JP, Camadro JM
TitleTowards a new T-fold protein?: the coproporphyrinogen III oxidase sequence matches many structural features from urate oxidase.
[17]
PubMed ID12499547
JournalActa Crystallogr D Biol Crystallogr
Year2003
Volume59
Pages118-26
AuthorsGirard E, Stelter M, Anelli PL, Vicat J, Kahn R
TitleA new class of gadolinium complexes employed to obtain high-phasing-power heavy-atom derivatives: results from SAD experiments with hen egg-white lysozyme and urate oxidase from Aspergillus flavus.
[18]
PubMed ID12680763
JournalBiochemistry
Year2003
Volume42
Pages4094-100
AuthorsImhoff RD, Power NP, Borrok MJ, Tipton PA
TitleGeneral base catalysis in the urate oxidase reaction: evidence for a novel Thr-Lys catalytic diad.
[19]
CommentsX-ray crystallography
PubMed ID14993669
JournalActa Crystallogr D Biol Crystallogr
Year2004
Volume60
Pages453-62
AuthorsRetailleau P, Colloc'h N, Vivares D, Bonnete F, Castro B, El-Hajji M, Mornon JP, Monard G, Prange T
TitleComplexed and ligand-free high-resolution structures of urate oxidase (Uox) from Aspergillus flavus: a reassignment of the active-site binding mode.
Related PDB1r4s,1r4u,1r51,1r56
[20]
CommentsX-ray crystallography
PubMed ID15735331
JournalActa Crystallogr D Biol Crystallogr
Year2005
Volume61
Pages218-29
AuthorsRetailleau P, Colloc'h N, Vivares D, Bonnete F, Castro B, El Hajji M, Prange T
TitleUrate oxidase from Aspergillus flavus: new crystal-packing contacts in relation to the content of the active site.
Related PDB1wrr,1ws2,1ws3,1xt4,1xxj,1xy3

comments
This enzyme is enzyme is homologous to the counterpart enzyme from Bacillus sp. (D00541 in EzCatDB).
According to the literature [9], [18] & [19], this enzyme seems to catalyzes the following reactions:
(A) Oxygenation by O2
(B) Deoxygenation to release H2O2
(C) Additive double-bond deformation by H2O (or hydration)

createdupdated
2004-07-152009-04-08


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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