N-carbamoyl-L-amino-acid hydrolase
| N-carbamoyl-L-amino-acid hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.87 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a N-carbamoyl-L-amino-acid hydrolase (EC 3.5.1.87) is an enzyme that catalyzes the chemical reaction
- N-carbamoyl-L-2-amino acid (a 2-ureido carboxylate) + H2O L-2-amino acid + NH3 + CO2
Thus, the two substrates of this enzyme are N-carbamoyl-L-2-amino acid and H2O, whereas its 3 products are L-2-amino acid, NH3, and CO2.
This enzyme belongs to the subfamily of hydrolases which act on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-carbamoyl-L-amino acid amidohydrolase.
References
[edit]- Ogawa J, Miyake H, Shimizu S (1995). "Purification and characterization of N-carbamoyl-L-amino acid amidohydrolase with broad substrate specificity from Alcaligenes xylosoxidans". Appl. Microbiol. Biotechnol. 43 (6): 1039–43. doi:10.1007/BF00166922. PMID 8590654.
