N-acyl-D-glutamate deacylase

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
Search PMC articles PubMed articles NCBI proteins

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 ${\displaystyle \rightleftharpoons }$ 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. Tokyo. 118 (1): 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.