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Aspartylglucosaminidase
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| PDB rendering based on 1apy. | ||||||||||||||
| Available structures: 1apy, 1apz | ||||||||||||||
| Identifiers | ||||||||||||||
| Symbol(s) | AGA; AGU; ASRG; GA | |||||||||||||
| External IDs | OMIM: 208400 MGI: 104873 HomoloGene: 13 | |||||||||||||
| EC number | 3.5.1.26 | |||||||||||||
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| RNA expression pattern | ||||||||||||||
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| Orthologs | ||||||||||||||
| Human | Mouse | |||||||||||||
| Entrez | 175 | 11593 | ||||||||||||
| Ensembl | ENSG00000038002 | ENSMUSG00000031521 | ||||||||||||
| Uniprot | P20933 | Q64191 | ||||||||||||
| Refseq | NM_000027 (mRNA) NP_000018 (protein) |
NM_001005847 (mRNA) NP_001005847 (protein) |
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| Location | Chr 4: 178.59 - 178.6 Mb | Chr 8: 55.01 - 55.02 Mb | ||||||||||||
| Pubmed search | [1] | [2] | ||||||||||||
Aspartylglucosaminidase, also known as AGA, is a human gene.[1]
Aspartylglucosaminidase is an amidohydrolase enyzme involved in the catabolism of N-linked oligosaccharides of glycoproteins. It cleaves asparagine from N-acetylglucosamines as one of the final steps in the lysosomal breakdown of glycoproteins. The lysosomal storage disease aspartylglycosaminuria is caused by a deficiency in the AGA enzyme.[1]
References
Further reading
- Ikonen E, Peltonen L (1993). "Mutations causing aspartylglucosaminuria (AGU): a lysosomal accumulation disease.". Hum. Mutat. 1 (5): 361–5. doi:. PMID 1301945.
- Mononen I, Fisher KJ, Kaartinen V, Aronson NN (1993). "Aspartylglycosaminuria: protein chemistry and molecular biology of the most common lysosomal storage disorder of glycoprotein degradation.". FASEB J. 7 (13): 1247–56. PMID 8405810.
- Enomaa N, Heiskanen T, Halila R, et al. (1992). "Human aspartylglucosaminidase. A biochemical and immunocytochemical characterization of the enzyme in normal and aspartylglucosaminuria fibroblasts.". Biochem. J. 286 ( Pt 2): 613–8. PMID 1530592.
- Ikonen E, Baumann M, Grön K, et al. (1991). "Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease.". EMBO J. 10 (1): 51–8. PMID 1703489.
- Morris C, Heisterkamp N, Groffen J, et al. (1992). "Chromosomal localization of the human glycoasparaginase gene to 4q32-q33.". Hum. Genet. 88 (3): 295–7. PMID 1733831.
- Ikonen E, Enomaa N, Ulmanen I, Peltonen L (1992). "In vitro mutagenesis helps to unravel the biological consequences of aspartylglucosaminuria mutation.". Genomics 11 (1): 206–11. PMID 1765378.
- Park H, Fisher KJ, Aronson NN (1991). "Genomic structure of human lysosomal glycosylasparaginase.". FEBS Lett. 288 (1-2): 168–72. PMID 1840528.
- Mononen T, Mononen I, Matilainen R, Airaksinen E (1991). "High prevalence of aspartylglycosaminuria among school-age children in eastern Finland.". Hum. Genet. 87 (3): 266–8. PMID 1864600.
- Fisher KJ, Aronson NN (1991). "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. 266 (18): 12105–13. PMID 1904874.
- Mononen I, Heisterkamp N, Kaartinen V, et al. (1991). "Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase.". Proc. Natl. Acad. Sci. U.S.A. 88 (7): 2941–5. PMID 2011603.
- Halila R, Baumann M, Ikonen E, et al. (1991). "Human leucocyte aspartylglucosaminidase. Evidence for two different subunits in a more complex native structure.". Biochem. J. 276 ( Pt 1): 251–6. PMID 2039475.
- Fisher KJ, Tollersrud OK, Aronson NN (1991). "Cloning and sequence analysis of a cDNA for human glycosylasparaginase. A single gene encodes the subunits of this lysosomal amidase.". FEBS Lett. 276 (1-2): 232. PMID 2265705.
- Fisher KJ, Tollersrud OK, Aronson NN (1990). "Cloning and sequence analysis of a cDNA for human glycosylasparaginase. A single gene encodes the subunits of this lysosomal amidase.". FEBS Lett. 269 (2): 440–4. PMID 2401370.
- Tollersrud OK, Aronson NN (1989). "Purification and characterization of rat liver glycosylasparaginase.". Biochem. J. 260 (1): 101–8. PMID 2775174.
- Hreidarsson S, Thomas GH, Valle DL, et al. (1983). "Aspartylglucosaminuria in the United States.". Clin. Genet. 23 (6): 427–35. PMID 6883788.
- Enomaa NE, Lukinmaa PL, Ikonen EM, et al. (1993). "Expression of aspartylglucosaminidase in human tissues from normal individuals and aspartylglucosaminuria patients.". J. Histochem. Cytochem. 41 (7): 981–9. PMID 7685790.
- McCormack AL, Mononen I, Kaartinen V, Yates JR (1995). "Localization of the disulfide bond involved in post-translational processing of glycosylasparaginase and disrupted by a mutation in the Finnish-type aspartylglycosaminuria.". J. Biol. Chem. 270 (7): 3212–5. PMID 7852406.
- Tollersrud OK, Heiskanen T, Peltonen L (1994). "Human leucocyte glycosylasparaginase is an alpha/beta-heterodimer of 19 kDa alpha-subunit and 17 and 18 kDa beta-subunit.". Biochem. J. 300 ( Pt 2): 541–4. PMID 8002961.
External links
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