hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
metal ion binding
hydrolase activity, acting on ester bonds
aspartoacylase activity
aminoacylase activity
identical protein binding
Cellular component
nucleus
cytoplasm
cytosol
Biological process
metabolism
cellular amino acid biosynthetic process
aspartate catabolic process
central nervous system myelination
positive regulation of oligodendrocyte differentiation
Sources:Amigo / QuickGO
Orthologs
Species
Human
Mouse
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 Mb
Chr 11: 73.2 – 73.22 Mb
PubMed search
[3]
[4]
Wikidata
View/Edit Human
View/Edit Mouse
Aspartoacylase
Structure of aspartoacylase dimer. Generated from 2I3C.[5]
Identifiers
EC no.
3.5.1.15
Databases
IntEnz
IntEnz view
BRENDA
BRENDA entry
ExPASy
NiceZyme view
KEGG
KEGG entry
MetaCyc
metabolic pathway
PRIAM
profile
PDB structures
RCSB PDB PDBe PDBsum
Search
PMC
articles
PubMed
articles
NCBI
proteins
Aspartoacylase is a hydrolytic enzyme (EC 3.5.1.15, also called aminoacylase II, ASPA and other names[a]) that in humans is encoded by the ASPA gene. ASPA catalyzes the deacylation of N-acetyl-l-aspartate (N-acetylaspartate) into aspartate and acetate.[7][8] 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.[9] 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.[10]
^ abcGRCh38: Ensembl release 89: ENSG00000108381 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000020774 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Bitto E, Bingman CA, Wesenberg GE, McCoy JG, Phillips GN (January 2007). "Structure of aspartoacylase, the brain enzyme impaired in Canavan disease". Proceedings of the National Academy of Sciences of the United States of America. 104 (2): 456–61. doi:10.1073/pnas.0607817104. PMC 1766406. PMID 17194761.
^"Aspartoacylase (EC 3.5.1.15)". biocyc.org. Archived from the original on 22 July 2022. Retrieved 2022-07-22.
^Birnbaum SM (1955). [12] Aminoacylase. Methods in Enzymology. Vol. 2. pp. 115–119. doi:10.1016/S0076-6879(55)02176-9. ISBN 9780121818029.
^Birnbaum SM, Levintow L, Kingsley RB, Greenstein JP (January 1952). "Specificity of amino acid acylases". The Journal of Biological Chemistry. 194 (1): 455–70. doi:10.1016/S0021-9258(18)55898-1. PMID 14927637.
^Le Coq J, An HJ, Lebrilla C, Viola RE (May 2006). "Characterization of human aspartoacylase: the brain enzyme responsible for Canavan disease". Biochemistry. 45 (18): 5878–84. doi:10.1021/bi052608w. PMC 2566822. PMID 16669630.
^Hershfield JR, Pattabiraman N, Madhavarao CN, Namboodiri MA (May 2007). "Mutational analysis of aspartoacylase: implications for Canavan disease". Brain Research. 1148: 1–14. doi:10.1016/j.brainres.2007.02.069. PMC 1933483. PMID 17391648.
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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...
which is responsible for the production of the enzyme aspartoacylase. Decreased aspartoacylase activity prevents the normal breakdown of N-acetylaspartate...
recessive pattern. It is due to a mutation in the ASPA gene that encodes aspartoacylase, an enzyme needed to metabolize N-acetyl-L-aspartate (NAA). The mutation...
Student Press Association ASPA (car), a 1920s Czech car ASPA (gene), Aspartoacylase, on human chromosome 17 Autonomous System Provider Authorizations in...
Canavan's disease: Canavan's disease is a white matter disease due to aspartoacylase deficiency. The dentate nucleus is not affected until late in disease...
system, also known as Canavan's disease, Van Bogaert-Bertrand type or Aspartoacylase (AspA) deficiency, is a rare autosomal recessive neurodegenerative disorder...
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