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:3.5.1.15
Description:Aspartoacylase.
Alternative Name: Aminoacylase II.
Cath: 3.30.70.1640; 3.30.70.360; 3.40.630.10; 2.20.25.160;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.1.15
BRENDA Enzyme Link: BRENDA 3.5.1.15
KEGG Enzyme Link: KEGG3.5.1.15
BioCyc Enzyme Link: BioCyc 3.5.1.15
ExPASy Enzyme Link: ExPASy3.5.1.15
EC2PDB Enzyme Link: EC2PDB 3.5.1.15
ExplorEnz Enzyme Link: ExplorEnz 3.5.1.15
PRIAM enzyme-specific profiles Link: PRIAM 3.5.1.15
IntEnz Enzyme Link: IntEnz 3.5.1.15
MEDLINE Enzyme Link: MEDLINE 3.5.1.15
MSA:

3.5.1.15;

Phylogenetic Tree:

3.5.1.15;

Uniprot:
M-CSA:
RHEA:10872 H2O + N-acyl-L-aspartate = a carboxylate + L-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
Clinically Distinct Phenotypes of Canavan Disease Correlate with Residual Aspartoacylase Enzyme Activity.Mendes MI, Smith DE, Pop A, Lennertz P, Fernandez Ojeda MR, Kanhai WA, van Dooren SJ, Anikster Y, Barić I, Boelen C, Campistol J, de Boer L, Kariminejad A, Kayserili H, Roubertie A, Verbruggen KT, Vianey-Saban C, Williams M, Salomons GS2017 May28101991
New T530C mutation in the aspartoacylase gene caused Canavan disease with no correlation between severity and N-acetylaspartate excretion.Di Pietro V, Cavallari U, Amorini AM, Lazzarino G, Longo S, Poggiani C, Cavalli P, Tavazzi B2013 Dec24036223
Identification of the zinc binding ligands and the catalytic residue in human aspartoacylase, an enzyme involved in Canavan disease.Herga S, Berrin JG, Perrier J, Puigserver A, Giardina T2006 Oct 3017027983
Aspartoacylase is a regulated nuclear-cytoplasmic enzyme.Hershfield JR, Madhavarao CN, Moffett JR, Benjamins JA, Garbern JY, Namboodiri A2006 Oct16935940
Specificity of amino acid acylases.BIRNBAUM SM, LEVINTOW L, KINGSLEY RB, GREENSTEIN JP1952 Jan14927637