Sequence of ACY2_HUMAN
EC Number:3.5.1.15
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
N-acyl-L-aspartate + H2O = a carboxylate + L-aspartate
Other sequences found for EC No. 3.5.1.15
General information:
Sequence
0 MTSCHIAEEH IQKVAIFGGT HGNELTGVFL VKHWLENGAE IQRTGLEVKP FITNPRAVKK
60 CTRYIDCDLN RIFDLENLGK KMSEDLPYEV RRAQEINHLF GPKDSEDSYD IIFDLHNTTS
120 NMGCTLILED SRNNFLIQMF HYIKTSLAPL PCYVYLIEHP SLKYATTRSI AKYPVGIEVG
180 PQPQGVLRAD ILDQMRKMIK HALDFIHHFN EGKEFPPCAI EVYKIIEKVD YPRDENGEIA
240 AIIHPNLQDQ DWKPLHPGDP MFLTLDGKTI PLGGDCTVYP VFVNEAAYYE KKEAFAKTTK
300 LTLNAKSIRC CLH
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
639584
Kaul R.,Gao G.P.,Balamurugan K.,Matalon R.
Cloning of the human aspartoacylase cDNA and a common missense mutation in Canavan disease.
Nat. Genet.
5
118-123
1993
639585
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
639586
Moore R.A.,Le Coq J.,Faehnle C.R.,Viola R.E.
Purification and preliminary characterization of brain aspartoacylase.
Arch. Biochem. Biophys.
413
1-8
2003
639587
Herga S.,Berrin J.G.,Perrier J.,Puigserver A.,Giardina T.
Identification of the zinc binding ligands and the catalytic residue in human aspartoacylase, an enzyme involved in Canavan disease.
FEBS Lett.
580
5899-5904
2006
639588
Le Coq J.,Pavlovsky A.,Malik R.,Sanishvili R.,Xu C.,Viola R.E.
Examination of the mechanism of human brain aspartoacylase through the binding of an intermediate analogue.
Biochemistry
47
3484-3492
2008
639589
Bitto E.,Bingman C.A.,Wesenberg G.E.,McCoy J.G.,Phillips G.N. Jr.
Structure of aspartoacylase, the brain enzyme impaired in Canavan disease.
Proc. Natl. Acad. Sci. U.S.A.
104
456-461
2007
639590
Kaul R.,Gao G.P.,Aloya M.,Balamurugan K.,Petrosky A.,Michals K.,Matalon R.
Canavan disease: mutations among Jewish and non-Jewish patients.
Am. J. Hum. Genet.
55
34-41
1994
639591
Shaag A.,Anikster Y.,Christensen E.,Glustein J.Z.,Fois A.,Michelakakis H.,Nigro F.,Pronicka E.,Ribes A.,Zabot M.-T.,Elpeleg O.N.
The molecular basis of canavan (aspartoacylase deficiency) disease in European non-Jewish patients.
Am. J. Hum. Genet.
57
572-580
1995
639592
Kaul R.,Gao G.P.,Michals K.,Whelan D.T.,Levin S.,Matalon R.
Novel (Cys152 > Arg) missense mutation in an Arab patient with Canavan disease.
Hum. Mutat.
5
269-271
1995
639593
Kaul R.,Gao G.P.,Matalon R.,Aloya M.,Su Q.,Jin M.,Johnson A.B.,Schutgens R.B.H.,Clarke J.T.R.
Identification and expression of eight novel mutations among non-Jewish patients with Canavan disease.
Am. J. Hum. Genet.
59
95-102
1996
639594
Kobayashi K.,Tsujino S.,Ezoe T.,Hamaguchi H.,Nihei K.,Sakuragawa N.
Missense mutation (I143T) in a Japanese patient with Canavan disease.
Hum. Mutat. Suppl.
1
0-0
1998
639595
Rady P.L.,Vargas T.,Tyring S.K.,Matalon R.,Langenbeck U.
Novel missense mutation (Y231C) in a Turkish patient with Canavan disease.
Am. J. Med. Genet.
87
273-275
1999
639596
Elpeleg O.N.,Shaag A.
The spectrum of mutations of the aspartoacylase gene in Canavan disease in non-Jewish patients.
J. Inherit. Metab. Dis.
22
531-534
1999
639597
Sistermans E.A.,de Coo R.F.,van Beerendonk H.M.,Poll-The B.T.,Kleijer W.J.,van Oost B.A.
Mutation detection in the aspartoacylase gene in 17 patients with Canavan disease: four new mutations in the non-Jewish population.
Eur. J. Hum. Genet.
8
557-560
2000
639598
Zeng B.J.,Wang Z.H.,Ribeiro L.A.,Leone P.,De Gasperi R.,Kim S.J.,Raghavan S.,Ong E.,Pastores G.M.,Kolodny E.H.
Identification and characterization of novel mutations of the aspartoacylase gene in non-Jewish patients with Canavan disease.
J. Inherit. Metab. Dis.
25
557-570
2002
639599
Olsen T.R.,Tranebjaerg L.,Kvittingen E.A.,Hagenfeldt L.,Moller C.,Nilssen O.
Two novel aspartoacylase gene (ASPA) missense mutations specific to Norwegian and Swedish patients with Canavan disease.
J. Med. Genet.
39
0-0
2002
639600
Di Pietro V.,Cavallari U.,Amorini A.M.,Lazzarino G.,Longo S.,Poggiani C.,Cavalli P.,Tavazzi B.
New T530C mutation in the aspartoacylase gene caused Canavan disease with no correlation between severity and N-acetylaspartate excretion.
Clin. Biochem.
46
1902-1904
2013
639601
Mendes M.I.,Smith D.E.,Pop A.,Lennertz P.,Fernandez Ojeda M.R.,Kanhai W.A.,van Dooren S.J.,Anikster Y.,Baric I.,Boelen C.,Campistol J.,de Boer L.,Kariminejad A.,Kayserili H.,Roubertie A.,Verbruggen K.T.,Vianey-Saban C.,Williams M.,Salomons G.S.
Clinically distinct phenotypes of Canavan disease correlate with residual aspartoacylase enzyme activity.
Hum. Mutat.
38
524-531
2017
