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Chemical Compound Review

AADG     (2S)-3-[[(2R,3R,4R,5S,6R)-3- acetamido-4,5...

Synonyms: SureCN243608, CHEBI:17261, HMDB00489, AR-1K5609, AC1L3XD4, ...
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Disease relevance of Aspartylglucosylamine


High impact information on Aspartylglucosylamine

  • The resulting enzyme deficiency allows aspartylglucosamine (GlcNAc-Asn) and other glycoasparagines to accumulate in tissues and body fluids, from early fetal life onward [2].
  • These homozygous mutant mice have no detectable AGA activity and excrete aspartylglucosamine in their urine [3].
  • Supplementation of culture medium with either isoform cleared AGU lymphoblasts of stored aspartylglucosamine when glycosylasparaginase activity in the cells reached 3-4% of that in normal lymphoblasts [4].
  • 5. The enzyme activity is competitively protected against this inactivation by its natural substrate, aspartylglucosamine, indicating that this inhibitor binds to the active site or very close to it [5].
  • L-Asparagine competitively inhibits the hydrolysis of aspartylglucosamine indicating that both the amino acid and glycoasparagine are interacting with the same active site of the enzyme [6].

Anatomical context of Aspartylglucosylamine

  • The sensitivity of the assay also allows direct quantitation of aspartylglucosamine in normal urine and leukocytes of aspartylglycosaminuria patients, and may thus be used in metabolic studies of the compound [7].
  • 2. By use of a highly specific and sensitive gaschromatographic-mass-spectrometric technique, 4-N-2-acetamido-2-deoxy-beta-D-glycopyranosyl-L-asparagine (N-acetylglucosaminylasparagine) was found to accumulate in the patient's lymphocytes, but not in those of the control subject [8].
  • Biochemical studies showed elevated levels of urinary aspartylglucosamine and very low activity of aspartylglucosaminidase(AGA) in cultured fibroblasts [9].
  • The condition is apparently due to decreased activity of aspartylglycosamine amido hydrolase, with accumulation of products of flycoprotein carabolism in cytoplasmic vacuoles in both epithelial and mesenchymal cells [10].
  • As a conclusion, the determination of aspartylglucosamine in urine allowed postnatal detection of aspartylglycosaminuria, but in amniotic fluid it was useless in prenatal detection of the disease [11].

Analytical, diagnostic and therapeutic context of Aspartylglucosylamine


  1. Human leukocyte glycosylasparaginase: cell-to-cell transfer and properties in correction of aspartylglycosaminuria. Dunder, U., Mononen, I. FEBS Lett. (2001) [Pubmed]
  2. A mouse model for the human lysosomal disease aspartylglycosaminuria. Kaartinen, V., Mononen, I., Voncken, J.W., Noronkoski, T., Gonzalez-Gomez, I., Heisterkamp, N., Groffen, J. Nat. Med. (1996) [Pubmed]
  3. Mice with an aspartylglucosaminuria mutation similar to humans replicate the pathophysiology in patients. Jalanko, A., Tenhunen, K., McKinney, C.E., LaMarca, M.E., Rapola, J., Autti, T., Joensuu, R., Manninen, T., Sipilä, I., Ikonen, S., Riekkinen, P., Ginns, E.I., Peltonen, L. Hum. Mol. Genet. (1998) [Pubmed]
  4. Recombinant glycosylasparaginase and in vitro correction of aspartylglycosaminuria. Mononen, I., Heisterkamp, N., Dunder, U., Romppanen, E.L., Noronkoski, T., Kuronen, I., Groffen, J. FASEB J. (1995) [Pubmed]
  5. Glycosaparaginase from human leukocytes. Inactivation and covalent modification with diazo-oxonorvaline. Kaartinen, V., Williams, J.C., Tomich, J., Yates, J.R., Hood, L.E., Mononen, I. J. Biol. Chem. (1991) [Pubmed]
  6. Recombinant human glycosylasparaginase catalyzes hydrolysis of L-asparagine. Noronkoski, T., Stoineva, I.B., Petkov, D.D., Mononen, I. FEBS Lett. (1997) [Pubmed]
  7. Analysis of aspartylglucosamine at the picomole level by high-performance liquid chromatography. Kaartinen, V., Mononen, I. J. Chromatogr. (1989) [Pubmed]
  8. Characterization of the storage material of peripheral lymphocytes in aspartylglycosaminuria. Maury, P., Palo, J. Clin. Sci. (1980) [Pubmed]
  9. Aspartylglucosaminuria in a Puerto Rican family: additional features of a panethnic disorder. Chitayat, D., Nakagawa, S., Marion, R.W., Sachs, G.S., Hahm, S.Y., Goldman, H.S. Am. J. Med. Genet. (1988) [Pubmed]
  10. Aspartylglycosaminuria: a generalized storage disease. Morphological and histochemical studies. Haltia, M., Palo, J., Autio, S. Acta Neuropathol. (1975) [Pubmed]
  11. Laboratory detection of aspartylglycosaminuria. Mononen, I., Kaartinen, V., Mononen, T. Scand. J. Clin. Lab. Invest. Suppl. (1988) [Pubmed]
  12. High prevalence of aspartylglycosaminuria among school-age children in eastern Finland. Mononen, T., Mononen, I., Matilainen, R., Airaksinen, E. Hum. Genet. (1991) [Pubmed]
  13. Aspartylglycosaminuria in Northern Norway in eight patients: clinical heterogeneity and variations with the diet. Borud, O., Strömme, J.H., Lie, S.O., Torp, K.H. J. Inherit. Metab. Dis. (1978) [Pubmed]
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