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- W1987360609 abstract "The gene structure of the human lysosomal enzyme glycosylasparaginase was determined. The gene spans 13 kb and consists of 9 exons. Both 5' and 3' untranslated regions of the gene are uninterrupted by introns. A number of transcriptional elements were identified in the 5' upstream sequence that includes two putative CAAT boxes followed by TATA-like sequences together with two AP-2 binding sites and one for Spl. A 100 bp CpG island and several ETF binding sites were also found. Additional AP-2 and Sp1 binding sites are present in the first intron. Two polyadenylation sites are present and appear to be functional. The major known glycosylasparaginase gene defect G488----C, which causes the lysosomal storage disease aspartylglycosaminuria (AGU) in Finland, is located in exon 4. Exon 5 encodes the post-translational cleavage site for the formation of the mature alpha/beta subunits of the enzyme as well as a recently proposed active site threonine, Thr206." @default.
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- W1987360609 date "1991-08-19" @default.
- W1987360609 modified "2023-10-13" @default.
- W1987360609 title "Genomic structure of human lysosomal glycosylasparaginase" @default.
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- W1987360609 doi "https://doi.org/10.1016/0014-5793(91)81027-6" @default.
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