Aspartylglucosaminidase

AGA
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1APY, 1APZ
Identifiers
Aliases	AGA , Aga, AW060726, AGU, ASRG, GA, aspartylglucosaminidase
External IDs	OMIM: 613228; MGI: 104873; HomoloGene: 13; GeneCards: AGA; OMA:AGA - orthologs
Gene location (Human) Chr. Chromosome 4 (human) [1] Band 4q34.3 Start 177,430,774 bp [1] End 177,442,437 bp [1]
Gene location (Mouse) Chr. Chromosome 8 (mouse) [2] Band 8|8 B1.3 Start 53,964,762 bp [2] End 53,976,456 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in corpus epididymis gingival epithelium gonad skin of hip stromal cell of endometrium skin of thigh oral cavity islet of Langerhans parotid gland kidney tubule Top expressed in calvaria ascending aorta otolith organ utricle pituitary gland aortic valve epithelium of lens stroma of bone marrow right kidney lobe of prostate More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein self-association peptidase activity hydrolase activity N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity Cellular component lysosome endoplasmic reticulum extracellular region extracellular space azurophil granule lumen cytoplasm Biological process protein maturation protein deglycosylation proteolysis neutrophil degranulation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 175 11593 Ensembl ENSG00000038002 ENSMUSG00000031521 UniProt P20933 Q64191 RefSeq (mRNA) NM_000027 NM_001171988 NM_001005847 NM_001205054 RefSeq (protein) NP_000018 NP_001165459 NP_001005847 NP_001191983 Location (UCSC) Chr 4: 177.43 – 177.44 Mb Chr 8: 53.96 – 53.98 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase is an enzyme that in humans is encoded by the AGA gene. ^[5]

Aspartylglucosaminidase is an amidohydrolase enzyme 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. ^[5]

References

1. GRCh38: Ensembl release 89: ENSG00000038002 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000031521 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: AGA aspartylglucosaminidase".

External links

• Human AGA genome location and AGA gene details page in the UCSC Genome Browser .

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. S2CID   24301019.
• 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. doi: 10.1096/fasebj.7.13.8405810 . PMID   8405810. S2CID   21771613.
• 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) (Pt 2): 613–8. doi:10.1042/bj2860613. PMC   1132942 . 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. doi:10.1002/j.1460-2075.1991.tb07920.x. PMC   452610 . 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. doi:10.1007/BF00197262. PMID   1733831. S2CID   8805853.
• 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. doi:10.1016/0888-7543(91)90120-4. PMID   1765378.
• Park H, Fisher KJ, Aronson NN (1991). "Genomic structure of human lysosomal glycosylasparaginase". FEBS Lett. 288 (1–2): 168–72. Bibcode:1991FEBSL.288..168P. doi: 10.1016/0014-5793(91)81027-6 . PMID   1840528. S2CID   26680929.
• 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. doi:10.1007/BF00200902. PMID   1864600. S2CID   8240322.
• 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. doi: 10.1016/S0021-9258(18)99071-X . 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. Bibcode:1991PNAS...88.2941M. doi: 10.1073/pnas.88.7.2941 . PMC   51356 . 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) (Pt 1): 251–6. doi:10.1042/bj2760251. PMC   1151172 . 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. doi: 10.1016/0014-5793(90)80551-S . PMID   2265705. S2CID   221417722.
• 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. Bibcode:1990FEBSL.269..440F. doi: 10.1016/0014-5793(90)81211-6 . PMID   2401370. S2CID   8210082.
• Tollersrud OK, Aronson NN (1989). "Purification and characterization of rat liver glycosylasparaginase". Biochem. J. 260 (1): 101–8. doi:10.1042/bj2600101. PMC   1138631 . PMID   2775174.
• Hreidarsson S, Thomas GH, Valle DL, et al. (1983). "Aspartylglucosaminuria in the United States". Clin. Genet. 23 (6): 427–35. doi:10.1111/j.1399-0004.1983.tb01977.x. PMID   6883788. S2CID   46703938.
• 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. doi: 10.1177/41.7.7685790 . 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. doi: 10.1074/jbc.270.7.3212 . 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) (Pt 2): 541–4. doi:10.1042/bj3000541. PMC   1138195 . PMID   8002961.

External links

• Aspartylglucosylaminase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)