title: Arylsulfatase K is the Lysosomal 2-Sulfoglucuronate Sulfatase.
abstract: 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.
authors.affiliation: Complex Carbohydrate Research Center, University of Georgia , Athens, Georgia, United States.
authors.forename: Omkar P
authors.initials: OP
authors.lastname: Dhamale
authors.affiliation: Department of Cellular and Molecular Medicine, Glycobiology Research and Training Center, University of California, San Diego , La Jolla, California, United States.
authors.forename: Roger
authors.initials: R
authors.lastname: Lawrence
authors.affiliation: Department of Chemistry, Biochemistry I, Bielefeld University , Bielefeld, Germany.
authors.forename: Elena M
authors.initials: EM
authors.lastname: Wiegmann
authors.affiliation: Complex Carbohydrate Research Center, University of Georgia , Athens, Georgia, United States.
authors.forename: Bhahwal A
authors.initials: BA
authors.lastname: Shah
authors.affiliation: Complex Carbohydrate Research Center, University of Georgia , Athens, Georgia, United States.
authors.forename: Kanar
authors.initials: K
authors.lastname: Al-Mafraji
authors.affiliation: Department of Cellular and Molecular Medicine, Glycobiology Research and Training Center, University of California, San Diego , La Jolla, California, United States.
authors.forename: William C
authors.initials: WC
authors.lastname: Lamanna
authors.affiliation: Department of Chemistry, Biochemistry I, Bielefeld University , Bielefeld, Germany.
authors.forename: Torben
authors.initials: T
authors.lastname: Lübke
authors.affiliation: Department of Chemistry, Biochemistry I, Bielefeld University , Bielefeld, Germany.
authors.forename: Thomas
authors.initials: T
authors.lastname: Dierks
authors.affiliation: Complex Carbohydrate Research Center, University of Georgia , Athens, Georgia, United States.|Department of Chemical Biology and Drug Discovery, Utrecht Institute for Pharmaceutical Sciences, and Bijvoet Center for Biomolecular Research, Utrecht University , Universiteitsweg 99, 3584 CG Utrecht, The Netherlands.
authors.forename: Geert-Jan
authors.identifier: 0000-0003-3111-5954
authors.initials: GJ
authors.lastname: Boons
authors.affiliation: Department of Cellular and Molecular Medicine, Glycobiology Research and Training Center, University of California, San Diego , La Jolla, California, United States.
authors.forename: Jeffrey D
authors.identifier: 0000-0001-8322-1834
authors.initials: JD
authors.lastname: Esko
mesh_terms: D001192:Arylsulfatases / Q000378:metabolism*; D002853:Chromatography, Liquid; D006025:Glycosaminoglycans / Q000378:metabolism; D006801:Humans; D008247:Lysosomes / Q000201:enzymology*; D013058:Mass Spectrometry; D013379:Substrate Specificity
chemical_list: D006025:Glycosaminoglycans; C511172:ARSK protein, human; D001192:Arylsulfatases