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Arylsulfatase K is the Lysosomal 2-Sulfoglucuronate Sulfatase.
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
Arylsulfatase K is the Lysosomal 2‑Sulfoglucuronate Sulfatase
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-<i>O</i>-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