EC number:3.5.1.83

Enzyme

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EC Tree
     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.1 In linear amides
ID:3.5.1.83
Description:N-acyl-D-aspartate deacylase.
Alternative Name: N-acyl-D-aspartate amidohydrolase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.1.83
BRENDA Enzyme Link: BRENDA 3.5.1.83
KEGG Enzyme Link: KEGG3.5.1.83
BioCyc Enzyme Link: BioCyc 3.5.1.83
ExPASy Enzyme Link: ExPASy3.5.1.83
EC2PDB Enzyme Link: EC2PDB 3.5.1.83
ExplorEnz Enzyme Link: ExplorEnz 3.5.1.83
PRIAM enzyme-specific profiles Link: PRIAM 3.5.1.83
IntEnz Enzyme Link: IntEnz 3.5.1.83
MEDLINE Enzyme Link: MEDLINE 3.5.1.83

EC number:3.5.1.83

MSA:

3.5.1.83;
Phylogenetic Tree:

3.5.1.83;
Uniprot:
M-CSA:
RHEA:18285 an N-acyl-D-aspartate + H2O = a carboxylate + D-aspartate
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
Purification and characterization of novel N-acyl-D-aspartate amidohydrolase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6.Moriguchi M, Sakai K, Katsuno Y, Maki T, Wakayama M1993 Jul7763985