DB code: S00187

CATH domain 3.10.270.10 : Urate Oxidase Catalytic domain
E.C. 1.7.3.3
CSA 1uox
M-CSA 1uox
MACiE M0118

CATH domain Related DB codes (homologues)
3.10.270.10 : Urate Oxidase D00541

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
B8HFX6
Urate oxidase
EC 1.7.3.3
YP_002489258.1 (Protein)
NC_011886.1 (DNA/RNA sequence)
PF01014 (Uricase)
[Graphical View]
Q00511 Uricase
EC 1.7.3.3
Urate oxidase
PF01014 (Uricase)
[Graphical View]

KEGG enzyme name
urate oxidase
uric acid oxidase
uricase
uricase II

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
B8HFX6 B8HFX6_9MICC
Q00511 URIC_ASPFL Urate + O(2) + H(2)O = 5-hydroxyisourate + H(2)O(2). Homotetramer. Peroxisome.

KEGG Pathways
Map code Pathways E.C.
MAP00230 Purine metabolism
MAP00232 Caffeine metabolism

Compound table
Substrates Products Intermediates
KEGG-id C00366 C00007 C00001 C11821 C00027
E.C.
Compound Urate O2 H2O 5-Hydroxyisourate H2O2
Type amide group,aromatic ring (with nitrogen atoms) others H2O amide group,aromatic ring (with nitrogen atoms),imine group others
ChEBI 17775
46811
46814
46817
46823
62589
17775
46811
46814
46817
46823
62589
15379
26689
27140
15379
26689
27140
15377
15377
18072
18072
16240
16240
PubChem 1175
1175
977
977
22247451
962
22247451
962
250388
250388
22326046
784
22326046
784
1vaxA Unbound Unbound Unbound Unbound
1vaxB Unbound Unbound Unbound Unbound
1vaxC Unbound Unbound Unbound Unbound
1vaxD Unbound Unbound Unbound Unbound
1vaxE Unbound Unbound Unbound Unbound
1vaxF Unbound Unbound Unbound Unbound
1vaxG Unbound Unbound Unbound Unbound
1vaxH Unbound Unbound Unbound Unbound
1vayA Analogue:AZA Unbound Unbound Unbound
1vayB Analogue:AZA Unbound Unbound Unbound
1vayC Analogue:AZA Unbound Unbound Unbound
1vayD Analogue:AZA Unbound Unbound Unbound
1vayE Analogue:AZA Unbound Unbound Unbound
1vayF Analogue:AZA Unbound Unbound Unbound
1vayG Analogue:AZA Unbound Unbound Unbound
1vayH Analogue:AZA Unbound Unbound Unbound
1r4sA Analogue:MUA Unbound Unbound Unbound
1r4uA Analogue:OXC Unbound Unbound Unbound
1r51A Analogue:AZA Unbound Unbound Unbound
1r56A Unbound Unbound Unbound Unbound
1r56B Unbound Unbound Unbound Unbound
1r56C Unbound Unbound Unbound Unbound
1r56D Unbound Unbound Unbound Unbound
1r56E Unbound Unbound Unbound Unbound
1r56F Unbound Unbound Unbound Unbound
1r56G Unbound Unbound Unbound Unbound
1r56H Unbound Unbound Unbound Unbound
1uoxA Unbound Unbound Unbound Unbound
1wrrA Analogue:UNC Unbound Unbound Unbound
1ws2A Analogue:URN Unbound Unbound Unbound
1ws2B Analogue:URN Unbound Unbound Unbound
1ws2C Analogue:URN Unbound Unbound Unbound
1ws2D Analogue:URN Unbound Unbound Unbound
1ws3A Analogue:URA Unbound Unbound Unbound
1ws3B Analogue:URA Unbound Unbound Unbound
1ws3C Analogue:URA Unbound Unbound Unbound
1ws3D Analogue:URA Unbound Unbound Unbound
1xt4A Analogue:GUN Unbound Unbound Unbound
1xxjA Analogue:UNC Unbound Unbound Unbound
1xxjB Analogue:UNC Unbound Unbound Unbound
1xxjC Analogue:UNC Unbound Unbound Unbound
1xxjD Analogue:UNC Unbound Unbound Unbound
1xy3A Analogue:GUN Unbound Unbound Unbound
1xy3B Analogue:GUN Unbound Unbound Unbound
1xy3C Analogue:GUN Unbound Unbound Unbound
1xy3D Analogue:GUN Unbound Unbound Unbound
1xy3E Analogue:GUN Unbound Unbound Unbound
1xy3F Analogue:GUN Unbound Unbound Unbound
1xy3G Analogue:GUN Unbound Unbound Unbound
1xy3H Analogue:GUN Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;Q00511 & literature [11], [18], [19]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1vaxA LYS 22;THR 67;ARG 180;GLN 223;ASN 249 THR 67
1vaxB LYS 22;THR 67;ARG 180;GLN 223;ASN 249 THR 67
1vaxC LYS 22;THR 67;ARG 180;GLN 223;ASN 249 THR 67
1vaxD LYS 22;THR 67;ARG 180;GLN 223;ASN 249 THR 67
1vaxE LYS 22;THR 67;ARG 180;GLN 223;ASN 249 THR 67
1vaxF LYS 22;THR 67;ARG 180;GLN 223;ASN 249 THR 67
1vaxG LYS 22;THR 67;ARG 180;GLN 223;ASN 249 THR 67
1vaxH LYS 22;THR 67;ARG 180;GLN 223;ASN 249 THR 67
1vayA LYS 22;THR 67;ARG 180;GLN 223;ASN 249 THR 67
1vayB LYS 22;THR 67;ARG 180;GLN 223;ASN 249 THR 67
1vayC LYS 22;THR 67;ARG 180;GLN 223;ASN 249 THR 67
1vayD LYS 22;THR 67;ARG 180;GLN 223;ASN 249 THR 67
1vayE LYS 22;THR 67;ARG 180;GLN 223;ASN 249 THR 67
1vayF LYS 22;THR 67;ARG 180;GLN 223;ASN 249 THR 67
1vayG LYS 22;THR 67;ARG 180;GLN 223;ASN 249 THR 67
1vayH LYS 22;THR 67;ARG 180;GLN 223;ASN 249 THR 67
1r4sA LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1r4uA LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1r51A LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1r56A LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1r56B LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1r56C LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1r56D LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1r56E LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1r56F LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1r56G LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1r56H LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1uoxA LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1wrrA LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1ws2A LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1ws2B LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1ws2C LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1ws2D LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1ws3A LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1ws3B LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1ws3C LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1ws3D LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1xt4A LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1xxjA LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1xxjB LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1xxjC LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1xxjD LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1xy3A LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1xy3B LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1xy3C LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1xy3D LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1xy3E LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1xy3F LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1xy3G LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57
1xy3H LYS 10;THR 57;ARG 176;GLN 228;ASN 254 THR 57

References for Catalytic Mechanism
References Sections No. 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]
Resource
Comments
Medline ID
PubMed ID 5640165
Journal Biochim Biophys Acta
Year 1968
Volume 151
Pages 63-9
Authors Nose K, Arima K
Title Studies on bacterial urate:oxygen oxidoreductase. II. Observations concerning the properties and components of the active site.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 4696756
Journal Biochemistry
Year 1973
Volume 12
Pages 1358-63
Authors Pitts OM, Priest DG
Title Uricase reaction intermediate. Mechanism of borate and hydroxide ion catalysis.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 4834240
Journal Nature
Year 1974
Volume 249
Pages 490-1
Authors Naparstek A, Romette JL, Kernevez JP, Thomas D
Title Memory in enzyme membranes.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 455938
Journal Comput Biol Med
Year 1979
Volume 9
Pages 145-53
Authors Lam CF, Cross AP
Title Comparative study of parameter estimation procedures in enzymic kinetics.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 7194181
Journal Enzyme
Year 1981
Volume 26
Pages 49-53
Authors Nishimura H, Matsushima A, Inada Y
Title Improved modification of yeast uricase with polyethylene glycol, accompanied with nonimmunoreactivity towards anti-uricase serum and high enzymic activity.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 9222322
Journal FEBS Lett
Year 1981
Volume 134
Pages 50-2
Authors Yoshida K, Nishimura H, Takahashi K, Matsushima A, Inada Y
Title Modification of amino groups in Candida utilis uricase with naphthoquinone disulfonic acid in relation to the enzymic activity.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 9125493
Journal Biochemistry
Year 1997
Volume 36
Pages 4731-8
Authors Kahn K, Tipton PA
Title Kinetic mechanism and cofactor content of soybean root nodule urate oxidase.
Related PDB
Related UniProtKB
[8]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS)
Medline ID 98025064
PubMed ID 9360612
Journal Nat Struct Biol
Year 1997
Volume 4
Pages 947-52
Authors Colloc'h N, el Hajji M, Bachet B, L'Hermite G, Schiltz M, Prange T, Castro B, Mornon JP
Title Crystal structure of the protein drug urate oxidase-inhibitor complex at 2.05 A resolution.
Related PDB 1uox
Related UniProtKB Q00511
[9]
Resource
Comments
Medline ID
PubMed ID 9709003
Journal Biochemistry
Year 1998
Volume 37
Pages 11651-9
Authors Kahn K, Tipton PA
Title Spectroscopic characterization of intermediates in the urate oxidase reaction.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 10361492
Journal Anal Chem
Year 1999
Volume 71
Pages 1928-34
Authors Nakaminami T, Ito S, Kuwabata S, Yoneyama H
Title Uricase-catalyzed oxidation of uric acid using an artificial electron acceptor and fabrication of amperometric uric acid sensors with use of a redox ladder polymer.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 10227848
Journal J Membr Biol
Year 1999
Volume 169
Pages 13-27
Authors Leal-Pinto E, Cohen BE, Abramson RG
Title Functional analysis and molecular modeling of a cloned urate transporter/channel.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 10737935
Journal Proteins
Year 2000
Volume 39
Pages 142-54
Authors Colloc'h N, Poupon A, Mornon JP
Title Sequence and structural features of the T-fold, an original tunnelling building unit.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 11856833
Journal Acta Crystallogr D Biol Crystallogr
Year 2002
Volume 58
Pages 472-9
Authors Vivares D, Bonnete F
Title X-ray scattering studies of Aspergillus flavus urate oxidase: towards a better understanding of PEG effects on the crystallization of large proteins.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 12060597
Journal Am J Physiol Renal Physiol
Year 2002
Volume 283
Pages F150-63
Authors Leal-Pinto E, Cohen BE, Lipkowitz MS, Abramson RG
Title Functional analysis and molecular model of the human urate transporter/channel, hUAT.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 12149119
Journal Biotechnol Appl Biochem
Year 2002
Volume 36
Pages 21-31
Authors Bayol A, Capdevielle J, Malazzi P, Buzy A, Claude Bonnet M, Colloc'h N, Mornon JP, Loyaux D, Ferrara P
Title Modification of a reactive cysteine explains differences between rasburicase and Uricozyme, a natural Aspergillus flavus uricase.
Related PDB
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 12208494
Journal FEBS Lett
Year 2002
Volume 526
Pages 5-10
Authors Colloc'h N, Mornon JP, Camadro JM
Title Towards a new T-fold protein?: the coproporphyrinogen III oxidase sequence matches many structural features from urate oxidase.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 12499547
Journal Acta Crystallogr D Biol Crystallogr
Year 2003
Volume 59
Pages 118-26
Authors Girard E, Stelter M, Anelli PL, Vicat J, Kahn R
Title A 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.
Related PDB
Related UniProtKB
[18]
Resource
Comments
Medline ID
PubMed ID 12680763
Journal Biochemistry
Year 2003
Volume 42
Pages 4094-100
Authors Imhoff RD, Power NP, Borrok MJ, Tipton PA
Title General base catalysis in the urate oxidase reaction: evidence for a novel Thr-Lys catalytic diad.
Related PDB
Related UniProtKB
[19]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 14993669
Journal Acta Crystallogr D Biol Crystallogr
Year 2004
Volume 60
Pages 453-62
Authors Retailleau P, Colloc'h N, Vivares D, Bonnete F, Castro B, El-Hajji M, Mornon JP, Monard G, Prange T
Title Complexed and ligand-free high-resolution structures of urate oxidase (Uox) from Aspergillus flavus: a reassignment of the active-site binding mode.
Related PDB 1r4s 1r4u 1r51 1r56
Related UniProtKB
[20]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 15735331
Journal Acta Crystallogr D Biol Crystallogr
Year 2005
Volume 61
Pages 218-29
Authors Retailleau P, Colloc'h N, Vivares D, Bonnete F, Castro B, El Hajji M, Prange T
Title Urate oxidase from Aspergillus flavus: new crystal-packing contacts in relation to the content of the active site.
Related PDB 1wrr 1ws2 1ws3 1xt4 1xxj 1xy3
Related UniProtKB

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)

Created Updated
2004-07-15 2009-04-08