N-acyl-D-glutamate deacylase

N-acyl-D-glutamate deacylase
N-acyl-D-glutamate deacylase
Identifiers
EC number 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 / EGO

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 \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 (Tokyo). "Primary structure of N-acyl-D-glutamate amidohydrolase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6". J. Biochem. (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. 
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