| N-carbamoyl-D-amino acid hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.77 | ||||||||
| CAS no. | 71768-08-6 | ||||||||
| 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-D-amino acid hydrolase ( EC 3.5.1.77) is an enzyme that catalyzes the chemical reaction
- N-carbamoyl-D-amino acid + H2O D-amino acid + NH3 + CO2
Thus, the two substrates of this enzyme are N-carbamoyl-D-amino acid and H2O, whereas its 3 products are D-amino acid, NH3, and CO2.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides.
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1ERZ, 1UF4, 1UF5, 1UF7, 1UF8, 2GGK, and 2GGL.
- Ogawa J, Shimizu S, Yamada H (1993). "N-carbamoyl-D-amino acid amidohydrolase from Comamonas sp. E222c purification and characterization". Eur. J. Biochem. 212 (3): 685–91. doi: 10.1111/j.1432-1033.1993.tb17706.x. PMID 8462543.
| N-carbamoyl-D-amino acid hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.77 | ||||||||
| CAS no. | 71768-08-6 | ||||||||
| 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-D-amino acid hydrolase ( EC 3.5.1.77) is an enzyme that catalyzes the chemical reaction
- N-carbamoyl-D-amino acid + H2O D-amino acid + NH3 + CO2
Thus, the two substrates of this enzyme are N-carbamoyl-D-amino acid and H2O, whereas its 3 products are D-amino acid, NH3, and CO2.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides.
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes 1ERZ, 1UF4, 1UF5, 1UF7, 1UF8, 2GGK, and 2GGL.
- Ogawa J, Shimizu S, Yamada H (1993). "N-carbamoyl-D-amino acid amidohydrolase from Comamonas sp. E222c purification and characterization". Eur. J. Biochem. 212 (3): 685–91. doi: 10.1111/j.1432-1033.1993.tb17706.x. PMID 8462543.