| EC |
1.7.3.3 |
| Accepted name: |
factor-independent urate hydroxylase |
| Reaction: |
urate + O2 + H2O = 5-hydroxyisourate + H2O2 |
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For diagram of AMP catabolism, click here |
| Other name(s): |
uric acid oxidase; uricase; uricase II; urate oxidase |
| Systematic name: |
urate:oxygen oxidoreductase |
| Comments: |
This enzyme was previously thought to be a copper protein, but it is now known that the enzymes from soy bean (Glycine max), the mould Aspergillus flavus and Bacillus subtilis contains no copper nor any other transition-metal ion. The 5-hydroxyisourate formed decomposes spontaneously to form allantoin and CO2, although there is an enzyme-catalysed pathway in which EC 3.5.2.17, hydroxyisourate hydrolase, catalyses the first step. The enzyme is different from EC 1.14.13.113 (FAD-dependent urate hydroxylase). |
| Links to other databases: |
BRENDA, EAWAG-BBD, EXPASY, Gene, KEGG, MetaCyc, PDB, CAS registry number: 9002-12-4 |
| References: |
| 1. |
London, M. and Hudson, P.B. Purification and properties of solubilized uricase. Biochim. Biophys. Acta 21 (1956) 290–298. [DOI] [PMID: 13363909] |
| 2. |
Mahler, H.R., Hübscher, G. and Baum, H. Studies on uricase. I. Preparation, purification, and properties of a cuproprotein. J. Biol. Chem. 216 (1955) 625–641. [PMID: 13271340] |
| 3. |
Robbins, K.C., Barnett, E.L. and Grant, N.H. Partial purification of porcine liver uricase. J. Biol. Chem. 216 (1955) 27–35. [PMID: 13252004] |
| 4. |
Kahn, K. and Tipton, P.A. Spectroscopic characterization of intermediates in the urate oxidase reaction. Biochemistry 37 (1998) 11651–11659. [DOI] [PMID: 9709003] |
| 5. |
Colloc'h, N., el Hajji, M., Bachet, B., L'Hermite, G., Schiltz, M., Prange, T., Castro, B. and Mornon, J.-P. Crystal structure of the protein drug urate oxidase-inhibitor complex at 2.05 Å resolution. Nat. Struct. Biol. 4 (1997) 947–952. [PMID: 9360612] |
| 6. |
Imhoff, R.D., Power, N.P., Borrok, M.J. and Tipton, P.A. General base catalysis in the urate oxidase reaction: evidence for a novel Thr-Lys catalytic diad. Biochemistry 42 (2003) 4094–4100. [DOI] [PMID: 12680763] |
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| [EC 1.7.3.3 created 1961, modified 2002, modified 2005, modified 2010] |
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