Arylsulfatase K is the Lysosomal 2-Sulfoglucuronate Sulfatase

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• 作者：Omkar P. Dhamale ; Roger Lawrence ; Elena M. Wiegmann ; Bhahwal A. Shah ; Kanar Al-Mafraji ; William C. Lamanna ; Torben Lübke ; Thomas Dierks ; Geert-Jan BoonsJeffrey D. Esko
• 刊名：ACS Chemical Biology
• 出版年：2017
• 出版时间：February 17, 2017
• 年：2017
• 卷：12
• 期：2
• 页码：367-373
• 全文大小：494K
• ISSN：1554-8937

文摘

The degradation of glycosaminoglycans (GAGs) involves a series of exolytic glycosidases and sulfatases that act sequentially on the nonreducing end of the polysaccharide chain. Enzymes have been cloned that catalyze all of the known linkages with the exception of the removal of the 2-O-sulfate group from 2-sulfoglucuronate, which is found in heparan sulfate and dermatan sulfate. Here, we show using synthetic disaccharide substrates that arylsulfatase K is the glucuronate-2-sulfatase. Arylsulfatase K acts selectively on 2-sulfoglucuronate and lacks activity against 2-sulfoiduronate, whereas iduronate-2-sulfatase (IDS) desulfates synthetic disaccharides containing 2-sulfoiduronate but not 2-sulfoglucuronate. As arylsulfatase K has all of the properties expected of a lysosomal enzyme, we conclude that arylsulfatase K is the long sought lysosomal glucuronate-2-sulfatase, which we designate GDS.