1apz

Structural highlights

Disease

[ASPG_HUMAN] Defects in AGA are the cause of aspartylglucosaminuria (AGU) [MIM:208400]. AGU is an inborn lysosomal storage disease. Clinical features of AGU include mild to severe mental retardation manifesting from the age of 2, coarse facial features and mild connective tissue abnormalities. This recessively inherited disease is overrepresented in the Finnish population.^{[1] [2] [3] [4] [5] [6]}

Function

[ASPG_HUMAN] Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

• Glycosylasparaginase

References

1. ↑ Ikonen E, Baumann M, Gron K, Syvanen AC, Enomaa N, Halila R, Aula P, Peltonen L. Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease. EMBO J. 1991 Jan;10(1):51-8. PMID:1703489
2. ↑ Fisher KJ, Aronson NN Jr. Characterization of the mutation responsible for aspartylglucosaminuria in three Finnish patients. Amino acid substitution Cys163----Ser abolishes the activity of lysosomal glycosylasparaginase and its conversion into subunits. J Biol Chem. 1991 Jun 25;266(18):12105-13. PMID:1904874
3. ↑ Mononen I, Heisterkamp N, Kaartinen V, Williams JC, Yates JR 3rd, Griffin PR, Hood LE, Groffen J. Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase. Proc Natl Acad Sci U S A. 1991 Apr 1;88(7):2941-5. PMID:2011603
4. ↑ Peltola M, Tikkanen R, Peltonen L, Jalanko A. Ser72Pro active-site disease mutation in human lysosomal aspartylglucosaminidase: abnormal intracellular processing and evidence for extracellular activation. Hum Mol Genet. 1996 Jun;5(6):737-43. PMID:8776587
5. ↑ Laitinen A, Hietala M, Haworth JC, Schroeder ML, Seargeant LE, Greenberg CR, Aula P. Two novel mutations in a Canadian family with aspartylglucosaminuria and early outcome post bone marrow transplantation. Clin Genet. 1997 Mar;51(3):174-8. PMID:9137882
6. ↑ Saarela J, Laine M, Oinonen C, von Schantz C, Jalanko A, Rouvinen J, Peltonen L. Molecular pathogenesis of a disease: structural consequences of aspartylglucosaminuria mutations. Hum Mol Genet. 2001 Apr 15;10(9):983-95. PMID:11309371
7. ↑ Oinonen C, Tikkanen R, Rouvinen J, Peltonen L. Three-dimensional structure of human lysosomal aspartylglucosaminidase. Nat Struct Biol. 1995 Dec;2(12):1102-8. PMID:8846222