Arylsulfatase K (ARSK)

Arylsulfatase K is a novel lysosomal enzyme of the sulfatase family, encoded by the ARSK gene (chromosome 5q15) and expressed as a 68 kDa glycoprotein with multiple N-glycosylation sites[1]. It is essential for the catabolism of complex carbohydrates, specifically catalyzing the removal of 2-O-sulfate groups from glucuronate in glycosaminoglycans such as heparan sulfate and chondroitin sulfate[3][5]. ARSK exhibits an acidic pH optimum (~4.6), localizes to lysosomes, and is sorted via mannose-6-phosphate receptors[1][3]. Deficiency of ARSK activity is predicted to result in a lysosomal storage disorder with currently undefined clinical presentation, analogous to other sulfatase deficiencies[1][3][5]. The enzyme is ubiquitously expressed in human tissues, suggesting a widespread physiological function[1]. No drugs are currently approved to target ARSK directly, and no known inhibitors have been described in the literature[1][3][5].

Other names

Arylsulfatase KARSKTSULFUNQ630/PRO1246ASKDKFZp313G1735Glucuronate-2-sulfataseTelethon sulfataseMPS10

Enzymatic hydrolysis of 2-O-sulfate esters from glucuronate in glycosaminoglycans.