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Aspartylglycosaminuria: protein chemistry and molecular biology of the most common lysosomal storage disorder of glycoprotein degradation
Author(s) -
Mon Ilkka,
Fisher Krishna J.,
Kaartinen Vesa,
Aronson Nathan N.
Publication year - 1993
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.7.13.8405810
Subject(s) - chemistry , degradation (telecommunications) , glycoprotein , microbiology and biotechnology , biochemistry , computational biology , biology , computer science , telecommunications
Aspartylglycosaminuria (AGU) (McKusick 20840) is the most common disorder of glycoprotein degradation caused by the failure of lysosomes to digest the protein‐to‐carbohydrate linkage of Asn‐linked glycoproteins. During the past few years there has been significant progress in our understanding of both the protein chemistry and molecular biology of glycosylasparaginase (EC 3.5.1.26) as well as the molecular changes underlying the storage disease AGU that results from deficiency of this lysosomal hydrolase. Modern clinical assays have been developed for the diagnosis and carrier detection of this disease. Detailed structure, substrate specificity, mechanism of action, and a part of the active site of glycosylasparaginase have been defined. Molecular biology of glycosylasparaginase has progressed rapidly and already some mutations in the glycosylasparaginase gene resulting in AGU have been identified. Evolutionary aspects based on sequence data indicate a mechanistic relationship between mammalian glycosylasparaginases and bacterial/plant asparaginases.—Mononen, I., Fisher, K. J., Kaartinen, V., Aronson, N. N., Jr. Aspartylglycosaminuria: protein chemistry and molecular biology of the most common lysosomal storage disorder of glycoprotein degradation. FASEB J. 7: 1247‐1256; 1993.