| EC |
4.1.1.97 |
| Accepted name: |
2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase |
| Reaction: |
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate = (S)-allantoin + CO2 |
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For diagram of AMP catabolism, click here |
| Glossary: |
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate = 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline |
| Other name(s): |
OHCU decarboxylase; hpxQ (gene name); PRHOXNB (gene name) |
| Systematic name: |
5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate carboxy-lyase [(S)-allantoin-forming] |
| Comments: |
This enzyme is part of the pathway from urate to (S)-allantoin, which is present in bacteria, plants and animals (but not in humans). |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB |
| References: |
| 1. |
Ramazzina, I., Folli, C., Secchi, A., Berni, R. and Percudani, R. Completing the uric acid degradation pathway through phylogenetic comparison of whole genomes. Nat. Chem. Biol. 2 (2006) 144–148. [DOI] [PMID: 16462750] |
| 2. |
Cendron, L., Berni, R., Folli, C., Ramazzina, I., Percudani, R. and Zanotti, G. The structure of 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase provides insights into the mechanism of uric acid degradation. J. Biol. Chem. 282 (2007) 18182–18189. [DOI] [PMID: 17428786] |
| 3. |
Kim, K., Park, J. and Rhee, S. Structural and functional basis for (S)-allantoin formation in the ureide pathway. J. Biol. Chem. 282 (2007) 23457–23464. [DOI] [PMID: 17567580] |
| 4. |
French, J.B. and Ealick, S.E. Structural and mechanistic studies on Klebsiella pneumoniae 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase. J. Biol. Chem. 285 (2010) 35446–35454. [DOI] [PMID: 20826786] |
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| [EC 4.1.1.97 created 2014] |
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