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Single base deletion in exon 7 of the glycosylasparaginase gene causes a mild form of aspartylglycosaminuria in a patient of Mauritian origin
Author(s) -
Park H.,
Rossiter M.,
Fensom A. H.,
Winchester B.,
Aronson N. N.
Publication year - 1996
Publication title -
journal of inherited metabolic disease
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.462
H-Index - 102
eISSN - 1573-2665
pISSN - 0141-8955
DOI - 10.1007/bf01799351
Subject(s) - frameshift mutation , exon , gene , mutation , genetics , biology , microbiology and biotechnology , stop codon , glycoprotein , human genetics
Summary Aspartylglycosaminuria (AGU) is a lysosomal storage disorder of glycoprotein degradation caused by deficiency of glycosylasparaginase (GA). A deletion mutation was found in a mildly affected AGU patient whose parents are first‐cousins of Mauritian origin. One bp deletion at position 787 or 788 (ΔT 788 ) in exon 7 of the GA gene resulted in a frameshift and produced an immediate stop codon. The resulting truncated polypeptide was defective in its post‐translational proteolytic processing and remained as a single chain (36 kDa) with no GA activity.