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UniProt functional annotation for P45381 | ||
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| UniProt code: P45381. |
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| Organism: | |
Homo sapiens (Human). |
| Taxonomy: | |
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo. |
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| Function: | |
Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to produce acetate and L-aspartate. NAA occurs in high concentration in brain and its hydrolysis NAA plays a significant part in the maintenance of intact white matter. In other tissues it act as a scavenger of NAA from body fluids. |
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| Catalytic activity: | |
Reaction=H2O + N-acyl-L-aspartate = a carboxylate + L-aspartate; Xref=Rhea:RHEA:10872, ChEBI:CHEBI:15377, ChEBI:CHEBI:29067, ChEBI:CHEBI:29991, ChEBI:CHEBI:58497; EC=3.5.1.15; Evidence={ECO:0000269|PubMed:17027983, ECO:0000269|PubMed:24036223, ECO:0000269|PubMed:28101991}; |
| Cofactor: | |
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:17194761, ECO:0000269|PubMed:18293939}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:17194761, ECO:0000269|PubMed:18293939}; |
| Biophysicochemical properties: | |
Kinetic parameters: Vmax=1.2 nmol/h/mg enzyme {ECO:0000269|PubMed:28101991}; |
| Subunit: | |
Homodimer. {ECO:0000305|PubMed:17194761, ECO:0000305|PubMed:18293939}. |
| Subcellular location: | |
Cytoplasm. Nucleus {ECO:0000250}. |
| Tissue specificity: | |
Brain white matter, skeletal muscle, kidney, adrenal glands, lung and liver. |
| Disease: | |
Canavan disease (CAND) [MIM:271900]: A rare neurodegenerative condition of infancy or childhood characterized by white matter vacuolization and demyelination that gives rise to a spongy appearance. The clinical features are onset in early infancy, atonia of neck muscles, hypotonia, hyperextension of legs and flexion of arms, blindness, severe mental defect, megalocephaly, and death by 18 months on the average. {ECO:0000269|PubMed:10407784, ECO:0000269|PubMed:10564886, ECO:0000269|PubMed:10909858, ECO:0000269|PubMed:12205125, ECO:0000269|PubMed:12638939, ECO:0000269|PubMed:12706335, ECO:0000269|PubMed:24036223, ECO:0000269|PubMed:28101991, ECO:0000269|PubMed:7599639, ECO:0000269|PubMed:7668285, ECO:0000269|PubMed:8023850, ECO:0000269|PubMed:8252036, ECO:0000269|PubMed:8659549, ECO:0000269|PubMed:9452117}. Note=The disease is caused by variants affecting the gene represented in this entry. |
| Similarity: | |
Belongs to the AspA/AstE family. Aspartoacylase subfamily. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.