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A Single Protein Catalyzes Both N-Deacetylation and N-Sulfation During the Biosynthesis of Heparan Sulfate
Zheng Wei, Stuart J. Swiedler, Masayuki Ishihara, Ariel Orellana and Carlos B. Hirschberg
Proceedings of the National Academy of Sciences of the United States of America
Vol. 90, No. 9 (May 1, 1993), pp. 3885-3888
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/2361856
Page Count: 4
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Heparan sulfate is a highly sulfated carbohydrate polymer that binds to and modulates the activities of numerous proteins. The formation of these protein-binding domains in heparan sulfate is dependent on a series of biosynthetic reactions that modify the polysaccharide backbone; the initiating and rate-limiting steps of this process are the N-deacetylation and N-sulfation of N-acetylglucosamine residues in the polymer. We now report that in the rat liver, biosynthesis of heparan sulfate utilizes a single protein that possesses both N-deacetylase and N-sulfotransferase activities. This was accomplished by demonstrating that both activities resided in a purified soluble fusion protein containing the Golgi-lumenal portion of the enzyme. We propose that this protein be renamed the rat liver Golgi heparan sulfate N-deacetylase/N-sulfotransferase.
Proceedings of the National Academy of Sciences of the United States of America © 1993 National Academy of Sciences