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| Name = aspartoacylase (Canavan disease) |
| Name = aspartoacylase (Canavan disease) |
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| image = [[File:ASPA dimer.png|thumb|Structure of aspartoacylase dimer generated from 2I3C.<ref name="Bitto 2007">{{cite journal|last1=Bitto|first1=E|last2=Bingman|first2=CA|last3=Wesenberg|first3=GE|last4=McCoy|first4=JG|last5=Phillips GN|first5=Jr|title=Structure of aspartoacylase, the brain enzyme impaired in Canavan disease.|journal=Proceedings of the National Academy of Sciences of the United States of America|date=9 January 2007|volume=104|issue=2|pages=456-61|pmid=17194761}}</ref> ]] |
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| image = [[File:ASPA dimer.png|thumb|Structure of Aspartoacylase generated from 2I3C.]] |
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| HGNCid = 756 |
| HGNCid = 756 |
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Revision as of 17:24, 28 February 2016
| 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.,[2][3] which breaks down N-acetylaspartate. A deficiency is associated with Canavan disease.This enzyme catalyses the following chemical reaction
Structure
Mechanism
Biological Function
Aspartoacylase is used to metabolize N-acetyl-L-aspartate by catalyzing its deacylation. Aspartoacylase prevents the build up of N-acetyl-L-aspartate 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. [4] It is believed that controlling N-acetyl-L-aspartate levels is essential for developing and maintaining white matter.[1] It is not known why so much N-acetyl-L-aspartate is produced in the brain nor what its primary function is.[5] However, one hypothesis is that it is potentially used as a reservoir that can be tapped into for acetate for acetyl coA synthesis or aspartate for glutamate synthesis. [4] [5] [6] This way, N-acetyl-L-aspartate can be used to transport these precursor molecules and aspartoacylase is used to release them. For example, N-acetyl-L-aspartate produced in neurons can be transported into oligodendrocytes and the acetate released can be used for myelin synthesis.[7]
Disease Relevance
References
- ^ a b Bitto, E; Bingman, CA; Wesenberg, GE; McCoy, JG; Phillips GN, Jr (9 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. PMID 17194761.
- ^ 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.
- ^ a b Moffett, JR; Arun, P; Ariyannur, PS; Namboodiri, AM (26 December 2013). "N-Acetylaspartate reductions in brain injury: impact on post-injury neuroenergetics, lipid synthesis, and protein acetylation". Frontiers in neuroenergetics. 5: 11. PMID 24421768.
- ^ 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.
- ^ Wijayasinghe, YS; Pavlovsky, AG; Viola, RE (5 August 2014). "Aspartoacylase catalytic deficiency as the cause of Canavan disease: a structural perspective". Biochemistry. 53 (30): 4970–8. PMID 25003821.
External links
- aspartoacylase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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