EC number:3.5.1.82

Enzyme

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     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.1 In linear amides
ID:3.5.1.82
Description:N-acyl-D-glutamate deacylase.
Alternative Name: N-acyl-D-glutamate amidohydrolase.
Cath: 3.20.20.140; 3.30.1490.130; 2.30.40.10;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.1.82
BRENDA Enzyme Link: BRENDA 3.5.1.82
KEGG Enzyme Link: KEGG3.5.1.82
BioCyc Enzyme Link: BioCyc 3.5.1.82
ExPASy Enzyme Link: ExPASy3.5.1.82
EC2PDB Enzyme Link: EC2PDB 3.5.1.82
ExplorEnz Enzyme Link: ExplorEnz 3.5.1.82
PRIAM enzyme-specific profiles Link: PRIAM 3.5.1.82
IntEnz Enzyme Link: IntEnz 3.5.1.82
MEDLINE Enzyme Link: MEDLINE 3.5.1.82

EC number:3.5.1.82

MSA:

3.5.1.82;
Phylogenetic Tree:

3.5.1.82;
Uniprot:
M-CSA:
RHEA:12833 an N-acyl-D-glutamate + H2O = a carboxylate + D-glutamate
RULE(radius=1) [*:1]-[C;H0;+0:2](=[*:3])-[NH;+0:4]-[*:5].[OH2;+0:6]>>[*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:6].[*:5]-[NH2;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Chemical modification of histidine residue of N-acyl-D-Glutamate amidohydrolase from Pseudomonas sp. 5f-1.Wakayama M, Tsutsumi T, Yada H, Sakai K, Moriguchi M1996 Apr8829533
Primary structure of N-acyl-D-glutamate amidohydrolase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6.Wakayama M, Ashika T, Miyamoto Y, Yoshikawa T, Sonoda Y, Sakai K, Moriguchi M1995 Jul8537313
Metal-characterization of N-acyl-D-glutamate amidohydrolase from Pseudomonas sp. strain 5f-1.Wakayama M, Miura Y, Oshima K, Sakai K, Moriguchi M1995 Aug7549100