-transparent.png){kind=logo}
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.
H Park, and
K J Fisher, and
N N Aronson
April 1996,
Archives of biochemistry and biophysics,
H Park, and
K J Fisher, and
N N Aronson
April 1988,
Biochimica et biophysica acta,
H Park, and
K J Fisher, and
N N Aronson
June 1997,
Genomics,
H Park, and
K J Fisher, and
N N Aronson
March 1998,
Protein science : a publication of the Protein Society,
H Park, and
K J Fisher, and
N N Aronson
February 1997,
Structure (London, England : 1993),
H Park, and
K J Fisher, and
N N Aronson
September 1990,
FEBS letters,
H Park, and
K J Fisher, and
N N Aronson
December 1990,
FEBS letters,
H Park, and
K J Fisher, and
N N Aronson
July 1997,
FEBS letters,
H Park, and
K J Fisher, and
N N Aronson
December 1995,
Nature structural biology,
H Park, and
K J Fisher, and
N N Aronson
March 1994,
Genomics,
