N-malonylurea hydrolase
 | This article includes a list of references, related reading, or external links, but its sources remain unclear because it lacks inline citations. (February 2023) |
| N-malonylurea hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.95 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
In enzymology, a N-malonylurea hydrolase (EC 3.5.1.95) is an enzyme that catalyzes the chemical reaction
- 3-oxo-3-ureidopropanoate + H2O malonate + urea
Thus, the two substrates of this enzyme are 3-oxo-3-ureidopropanoate and H2O, whereas its two products are malonate and urea.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is 3-oxo-3-ureidopropanoate amidohydrolase (urea- and malonate-forming). This enzyme is also called ureidomalonase.
References
[edit]- Soong CL, Ogawa J, Shimizu S (2001). "Novel amidohydrolytic reactions in oxidative pyrimidine metabolism: analysis of the barbiturase reaction and discovery of a novel enzyme, ureidomalonase". Biochem. Biophys. Res. Commun. 286 (1): 222–6. doi:10.1006/bbrc.2001.5356. PMID 11485332.
- Soong CL, Ogawa J, Sakuradani E, Shimizu S (2002). "Barbiturase, a novel zinc-containing amidohydrolase involved in oxidative pyrimidine metabolism". J. Biol. Chem. 277 (9): 7051–8. doi:10.1074/jbc.M110784200. PMID 11748240.
