Aspartylglucosaminidase

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Aspartylglucosaminidase
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
RNA expression pattern

More reference expression data
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)
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]

[edit] References

  1. ^ a b Entrez Gene: AGA aspartylglucosaminidase.

[edit] Further reading

  • Ikonen E, Peltonen L (1993). "Mutations causing aspartylglucosaminuria (AGU): a lysosomal accumulation disease.". Hum. Mutat. 1 (5): 361–5. doi:10.1002/humu.1380010503. 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. 

[edit] External links

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Carbon-nitrogen non-peptide hydrolases (EC 3.5)
3.5.1 - Amidohydrolases
3.5.2
3.5.3
3.5.4 - Aminohydrolases
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Metabolism: carbohydrate metabolism - glycoprotein enzymes
Anabolism
Catabolism
Transport
M6P tagging
see also disorders