Robertson D A, Freeman C, Nelson P V, Morris C P, Hopwood J J
Department of Chemical Pathology, Adelaide Children's Hospital, South Australia.
Biochem Biophys Res Commun. 1988 Nov 30;157(1):218-24. doi: 10.1016/s0006-291x(88)80035-4.
Glucosamine-6-sulfatase is a lysosomal enzyme which degrades glycosaminoglycans and is deficient in mucopolysaccharidosis type IIID. Human liver contains two major active forms of glucosamine-6-sulfatase, form A which has a single 78 kDa polypeptide and form B which has two polypeptides of 48 kDa and 32 kDa. A 1761 base pair cDNA clone encoding the complete 48 kDa polypeptide of form B was isolated. Form A is shown to be processed to form B with the 48 kDa polypeptide C-terminal to the 32 kDa polypeptide, and it is shown that C-terminal processing is limited to a region of thirty amino acids. The glucosamine-6-sulfatase sequence reveals homology with steroid sulfatase, a microsomal enzyme.
氨基葡萄糖-6-硫酸酯酶是一种降解糖胺聚糖的溶酶体酶,在IIID型粘多糖贮积症中缺乏。人肝脏含有两种主要的活性形式的氨基葡萄糖-6-硫酸酯酶,A形式具有单一的78 kDa多肽,B形式具有48 kDa和32 kDa的两种多肽。分离出一个编码B形式完整48 kDa多肽的1761个碱基对的cDNA克隆。结果表明,A形式被加工成B形式,48 kDa多肽位于32 kDa多肽的C末端,并且表明C末端加工仅限于30个氨基酸的区域。氨基葡萄糖-6-硫酸酯酶序列与微粒体酶类固醇硫酸酯酶具有同源性。