Aspartylglucosaminidase Explained

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.

Further reading

• Ikonen E, Peltonen L . Mutations causing aspartylglucosaminuria (AGU): a lysosomal accumulation disease . Hum. Mutat. . 1 . 5 . 361–5 . 1993 . 1301945 . 10.1002/humu.1380010503 . 24301019 . free .
• Mononen I, Fisher KJ, Kaartinen V, Aronson NN . Aspartylglycosaminuria: protein chemistry and molecular biology of the most common lysosomal storage disorder of glycoprotein degradation . FASEB J. . 7 . 13 . 1247–56 . 1993 . 8405810 . 10.1096/fasebj.7.13.8405810. free . 21771613 .
• Enomaa N, Heiskanen T, Halila R . Human aspartylglucosaminidase. A biochemical and immunocytochemical characterization of the enzyme in normal and aspartylglucosaminuria fibroblasts . Biochem. J. . 286 (Pt 2) . Pt 2. 613–8 . 1992 . 1530592 . 10.1042/bj2860613. 1132942 . etal.
• Ikonen E, Baumann M, Grön K . Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease . EMBO J. . 10 . 1 . 51–8 . 1991 . 1703489 . 10.1002/j.1460-2075.1991.tb07920.x. 452610 . etal.
• Morris C, Heisterkamp N, Groffen J . Chromosomal localization of the human glycoasparaginase gene to 4q32-q33 . Hum. Genet. . 88 . 3 . 295–7 . 1992 . 1733831 . 10.1007/BF00197262 . 8805853 . etal.
• Ikonen E, Enomaa N, Ulmanen I, Peltonen L . In vitro mutagenesis helps to unravel the biological consequences of aspartylglucosaminuria mutation . Genomics . 11 . 1 . 206–11 . 1992 . 1765378 . 10.1016/0888-7543(91)90120-4 .
• Park H, Fisher KJ, Aronson NN . Genomic structure of human lysosomal glycosylasparaginase . FEBS Lett. . 288 . 1–2 . 168–72 . 1991 . 1840528 . 10.1016/0014-5793(91)81027-6 . 26680929 . free .
• Mononen T, Mononen I, Matilainen R, Airaksinen E . High prevalence of aspartylglycosaminuria among school-age children in eastern Finland . Hum. Genet. . 87 . 3 . 266–8 . 1991 . 1864600 . 10.1007/BF00200902 . 8240322 .
• Fisher KJ, Aronson NN . 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 . 1991 . 10.1016/S0021-9258(18)99071-X . 1904874 . free .
• Mononen I, Heisterkamp N, Kaartinen V . 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 . 1991 . 2011603 . 10.1073/pnas.88.7.2941 . 51356 . 1991PNAS...88.2941M . etal. free .
• Halila R, Baumann M, Ikonen E . Human leucocyte aspartylglucosaminidase. Evidence for two different subunits in a more complex native structure . Biochem. J. . 276 (Pt 1) . Pt 1. 251–6 . 1991 . 2039475 . 10.1042/bj2760251. 1151172 . etal.
• Fisher KJ, Tollersrud OK, Aronson NN . 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 . 1991 . 2265705 . 10.1016/0014-5793(90)80551-S . 221417722 . free .
• Fisher KJ, Tollersrud OK, Aronson NN . 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 . 1990 . 2401370 . 10.1016/0014-5793(90)81211-6 . 8210082 . free .
• Tollersrud OK, Aronson NN . Purification and characterization of rat liver glycosylasparaginase . Biochem. J. . 260 . 1 . 101–8 . 1989 . 2775174 . 10.1042/bj2600101. 1138631 .
• Hreidarsson S, Thomas GH, Valle DL . Aspartylglucosaminuria in the United States . Clin. Genet. . 23 . 6 . 427–35 . 1983 . 6883788 . 10.1111/j.1399-0004.1983.tb01977.x . 46703938 . etal.
• Enomaa NE, Lukinmaa PL, Ikonen EM . Expression of aspartylglucosaminidase in human tissues from normal individuals and aspartylglucosaminuria patients . J. Histochem. Cytochem. . 41 . 7 . 981–9 . 1993 . 7685790 . 10.1177/41.7.7685790 . etal. free .
• McCormack AL, Mononen I, Kaartinen V, Yates JR . 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 . 1995 . 7852406 . 10.1074/jbc.270.7.3212 . free .
• Tollersrud OK, Heiskanen T, Peltonen L . 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 . 1994 . 8002961 . 10.1042/bj3000541. 1138195 .

Notes and References

1. Web site: Entrez Gene: AGA aspartylglucosaminidase.