| N-acyl-D-glutamate deacylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.82 | ||||||||
| 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-acyl-D-glutamate deacylase ( EC 3.5.1.82) is an enzyme that catalyzes the chemical reaction
- N-acyl-D-glutamate + H2O a carboxylate + D-glutamate
Thus, the two substrates of this enzyme are N-acyl-D-glutamate and H2O, whereas its two products are carboxylate and D-glutamate.
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 N-acyl-D-glutamate amidohydrolase. It employs one cofactor, zinc.
References
- Moriguchi M; Ashika, T; Miyamoto, Y; Yoshikawa, T; Sonoda, Y; Sakai, K; Moriguchi, M (July 1995). "Primary structure of N-acyl-D-glutamate amidohydrolase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6". J. Biochem. 118 (1). Tokyo: 204–9. PMID 8537313.
- Wakayama M, Miura Y, Oshima K, Sakai K, Moriguchi M (1995). "Metal-characterization of N-acyl-D-glutamate amidohydrolase from Pseudomonas sp. strain 5f-1". Biosci. Biotechnol. Biochem. 59 (8): 1489–92. doi: 10.1271/bbb.59.1489. PMID 7549100.
- Wakayama M, Tsutsumi T, Yada H, Sakai K, Moriguchi M (1996). "Chemical modification of histidine residue of N-acyl-D-Glutamate amidohydrolase from Pseudomonas sp. 5f-1". Biosci. Biotechnol. Biochem. 60 (4): 650–3. doi: 10.1271/bbb.60.650. PMID 8829533.
| N-acyl-D-glutamate deacylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.1.82 | ||||||||
| 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-acyl-D-glutamate deacylase ( EC 3.5.1.82) is an enzyme that catalyzes the chemical reaction
- N-acyl-D-glutamate + H2O a carboxylate + D-glutamate
Thus, the two substrates of this enzyme are N-acyl-D-glutamate and H2O, whereas its two products are carboxylate and D-glutamate.
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 N-acyl-D-glutamate amidohydrolase. It employs one cofactor, zinc.
References
- Moriguchi M; Ashika, T; Miyamoto, Y; Yoshikawa, T; Sonoda, Y; Sakai, K; Moriguchi, M (July 1995). "Primary structure of N-acyl-D-glutamate amidohydrolase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6". J. Biochem. 118 (1). Tokyo: 204–9. PMID 8537313.
- Wakayama M, Miura Y, Oshima K, Sakai K, Moriguchi M (1995). "Metal-characterization of N-acyl-D-glutamate amidohydrolase from Pseudomonas sp. strain 5f-1". Biosci. Biotechnol. Biochem. 59 (8): 1489–92. doi: 10.1271/bbb.59.1489. PMID 7549100.
- Wakayama M, Tsutsumi T, Yada H, Sakai K, Moriguchi M (1996). "Chemical modification of histidine residue of N-acyl-D-Glutamate amidohydrolase from Pseudomonas sp. 5f-1". Biosci. Biotechnol. Biochem. 60 (4): 650–3. doi: 10.1271/bbb.60.650. PMID 8829533.