User:Elalol1994/sandbox
| aspartoacylase (Canavan disease) | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | ASPA | ||||||
| NCBI gene | 443 | ||||||
| HGNC | 756 | ||||||
| OMIM | 608034 | ||||||
| RefSeq | NM_000049 | ||||||
| UniProt | P45381 | ||||||
| Other data | |||||||
| EC number | 3.5.1.15 | ||||||
| Locus | Chr. 17 p13-ter | ||||||
| |||||||
| aspartoacylase (aminocyclase) 3 | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | ACY3 | ||||||
| NCBI gene | 91703 | ||||||
| HGNC | 24104 | ||||||
| RefSeq | NM_080658 | ||||||
| UniProt | Q96HD9 | ||||||
| Other data | |||||||
| Locus | Chr. 11 q13 | ||||||
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Aspartoacylase (EC 3.5.1.15, aminoacylase II, N-acetylaspartate amidohydrolase, acetyl-aspartic deaminase, acylase II) is a hydrolase enzyme with system name N-acyl-L-aspartate amidohydrolase.,[1][2] which breaks down N-acetylaspartate. A deficiency is associated with Canavan disease.This enzyme catalyses the following chemical reaction
Structure
Mechanism
Biological Function
Aspartoacylase catalyzes the deacylation of N-acetyl-L-aspartate, primarily in the brain. N-acetyl-L-aspartate is one of the most abundant amino acids found in the brain with concentrations of up to 10mM and makes up about 1% of the brain's dry weight. [3] This enzyme is essential to prevent the build up of N-acetyl-L-aspartate. It is not known why so much N-acetyl-L-aspartate is produced in the brain nor what its primary function is. However, it is hypothesized that it is potentially used as a reservoir that can be tapped into for acetate for acetyl coA synthesis or aspartate for glutamate synthesis. [3] [4]
Heading text
Disease Relevance
References
- ^ Birnbaum, S.M. (1955). "Aminoacylase. Amino acid aminoacylases I and II from hog kidney". Methods Enzymol. 2: 115–119. doi:10.1016/S0076-6879(55)02176-9.
- ^ Birnbaum, S.M., Levintow, L., Kingsley, R.B. and Greenstein, J.P. (1952). "Specificity of amino acid acylases". J. Biol. Chem. 194: 455–470. PMID 14927637.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ a b Clark, JF; Doepke, A; Filosa, JA; Wardle, RL; Lu, A; Meeker, TJ; Pyne-Geithman, GJ (2006). "N-acetylaspartate as a reservoir for glutamate". Medical hypotheses. 67 (3): 506–12. PMID 16730130.
- ^ Hershfield, JR; Madhavarao, CN; Moffett, JR; Benjamins, JA; Garbern, JY; Namboodiri, A (October 2006). "Aspartoacylase is a regulated nuclear-cytoplasmic enzyme". FASEB journal : official publication of the Federation of American Societies for Experimental Biology. 20 (12): 2139–41. PMID 16935940.
External links
- aspartoacylase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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