Aspartoacylase

ASPA
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesASPA, ACY2, ASP, aspartoacylase
External IDsOMIM: 608034; MGI: 87914; HomoloGene: 33; GeneCards: ASPA; OMA:ASPA - orthologs
Orthologs
SpeciesHumanMouse
Entrez

443

11484

Ensembl

ENSG00000108381

ENSMUSG00000020774

UniProt

P45381

Q8R3P0

RefSeq (mRNA)

NM_000049
NM_001128085

NM_023113

RefSeq (protein)

NP_000040
NP_001121557

NP_075602

Location (UCSC)Chr 17: 3.47 – 3.5 MbChr 11: 73.2 – 73.22 Mb
PubMed search
Wikidata
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Aspartoacylase
Structure of aspartoacylase dimer. Generated from 2I3C.
Identifiers
EC no.3.5.1.15
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

Aspartoacylase is a hydrolytic enzyme (EC 3.5.1.15, also called aminoacylase II, ASPA and other names) that in humans is encoded by the ASPA gene. ASPA catalyzes the deacylation of N-acetyl-l-aspartate (N-acetylaspartate) into aspartate and acetate. It is a zinc-dependent hydrolase that promotes the deprotonation of water to use as a nucleophile in a mechanism analogous to many other zinc-dependent hydrolases. It is most commonly found in the brain, where it controls the levels of N-acetyl-l-aspartate. Mutations that result in loss of aspartoacylase activity are associated with Canavan disease, a rare autosomal recessive neurodegenerative disease.