Urate Oxidase - Structure

Structure

Urate oxidase is mainly localised in the liver, where it forms a large electron-dense paracrystalline core in many peroxisomes. The enzyme exists as a tetramer of identical subunits, each containing a possible type 2 copper-binding site.

Urate oxidase is a homotetrameric enzyme containing four identical active sites situated at the interfaces between its four subunits. UO from A. flavus is made up of 301 residues and has a molecular weight of 33438 dalton. It is unique among the oxidases in that it does not require a metal atom or an organic co-factor for catalysis. Sequence analysis of several organisms has determined that there are 24 amino acids which are conserved, and of these, 15 are involved with the active site.

factor-independent urate hydroxylase
Identifiers
EC number 1.7.3.3
CAS number 9002-12-4
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures
Gene Ontology
Search
PMC articles
PubMed articles
NCBI Protein search
Uricase
Identifiers
Symbol Uricase
Pfam PF01014
InterPro IPR002042
PROSITE PDOC00315
SCOP 1uox
SUPERFAMILY 1uox
Available protein structures:
Pfam structures
PDB RCSB PDB; PDBe
PDBsum structure summary

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