Aspartylglucosaminidase

PDB rendering based on 1apy.

Available structures
PDB	1APY, 1APZ

Identifiers

Symbols

AGA; AGU; ASRG; GA

External IDs

OMIM: 613228 MGI: 104873 HomoloGene: 13 GeneCards: AGA Gene

EC number

3.5.1.26

Gene Ontology
Molecular function	• N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity • N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity • hydrolase activity • protein self-association
Cellular component	• lysosome • endoplasmic reticulum • microtubule cytoskeleton • intracellular membrane-bounded organelle • intermediate filament cytoskeleton
Biological process	• protein deglycosylation • protein deglycosylation • asparagine catabolic process via L-aspartate • protein maturation
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 4:
178.35 – 178.36 Mb

Chr 8:
54.6 – 54.61 Mb

PubMed search

[1]

[2]

N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase is an enzyme that in humans is encoded by the AGA gene.^[1]

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.^[1]

References

^ ^a ^b "Entrez Gene: AGA aspartylglucosaminidase". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=175.

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) (Pt 2): 613–8. PMC 1132942. PMID 1530592. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1132942.
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. PMC 452610. PMID 1703489. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=452610.
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.
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. doi:10.1016/0014-5793(91)81027-6. 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. doi:10.1007/BF00200902. 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. doi:10.1073/pnas.88.7.2941. PMC 51356. PMID 2011603. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=51356.
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. PMC 1151172. PMID 2039475. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1151172.
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.
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. doi:10.1016/0014-5793(90)81211-6. PMID 2401370.
Tollersrud OK, Aronson NN (1989). "Purification and characterization of rat liver glycosylasparaginase". Biochem. J. 260 (1): 101–8. PMC 1138631. PMID 2775174. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1138631.
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.
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. PMC 1138195. PMID 8002961. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1138195.

PDB gallery

1apy: HUMAN ASPARTYLGLUCOSAMINIDASE

1apz: HUMAN ASPARTYLGLUCOSAMINIDASE COMPLEX WITH REACTION PRODUCT

External links

MeSH Aspartylglucosylaminase

Hydrolases: carbon-nitrogen non-peptide (EC 3.5)

3.5.1: Linear amides / Amidohydrolases	Asparaginase · Glutaminase · Urease · Biotinidase · Aspartoacylase · Ceramidase · Aspartylglucosaminidase · Fatty acid amide hydrolase · Histone deacetylase (Sirtuin)

3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase · Beta-lactamase

3.5.3: Linear amidines/ Ureohydrolases	Arginase · Agmatinase · Protein-arginine deiminase

3.5.4: Cyclic amidines/ Aminohydrolases	Guanine deaminase · Adenosine deaminase · AMP deaminase · Inosine monophosphate synthase · DCMP deaminase · GTP cyclohydrolase I · Cytidine deaminase (AICDA, Activation-Induced (Cytidine) Deaminase)

3.5.5: Nitriles/ Aminohydrolases	Nitrilase

3.5.99: Other	Riboflavinase · Thiaminase II

B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6

Metabolism: carbohydrate metabolism · glycoprotein enzymes

Anabolism

Dolichol kinase · GCS1 · Oligosaccharyltransferase

Catabolism

Neuraminidase · Beta-galactosidase · Hexosaminidase · mannosidase (alpha-Mannosidase, beta-mannosidase) · Aspartylglucosaminidase · Fucosidase · NAGA

Transport

SLC17A5

M6P tagging

N-acetylglucosamine-1-phosphate transferase

M: MET

mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m

k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon

m(A16/C10),i(k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)

Aspartylglucosaminidase

References

Further reading

External links