The Enzyme Database

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Accepted name: hydroxyisourate hydrolase
Reaction: 5-hydroxyisourate + H2O = 5-hydroxy-2-oxo-4-ureido-2,5-dihydro-1H-imidazole-5-carboxylate
For diagram of AMP catabolism, click here
Other name(s): HIUHase; 5-hydroxyisourate hydrolase
Systematic name: 5-hydroxyisourate amidohydrolase
Comments: The reaction is the first stage in the conversion of 5-hydroxyisourate into S-allantoin. This reaction will also occur spontaneously but more slowly.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 255885-20-2
1.  Raychaudhuri, A. and Tipton, P.A. A familiar motif in a new context: the catalytic mechanism of hydroxyisourate hydrolase. Biochemistry 42 (2003) 6848–6852. [DOI] [PMID: 12779339]
2.  Raychaudhuri, A. and Tipton, P.A. Cloning and expression of the gene for soybean hydroxyisourate hydrolase. Localization and implications for function and mechanism. Plant Physiol. 130 (2002) 2061–2068. [DOI] [PMID: 12481089]
3.  Sarma, A.D., Serfozo, P., Kahn, K. and Tipton, P.A. Identification and purification of hydroxyisourate hydrolase, a novel ureide-metabolizing enzyme. J. Biol. Chem. 274 (1999) 33863–33865. [DOI] [PMID: 10567345]
[EC created 2004]
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
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, KEGG, MetaCyc
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]
[EC created 2014]

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