A single protein catalyzes both N-deacetylation and N-sulfation during the biosynthesis of heparan sulfate

Z. Wei, S. J. Swiedler, M. Ishihara, A. Orellana, C. B. Hirschberg

Research output: Contribution to journalArticlepeer-review

65 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)3885-3888
Number of pages4
JournalProceedings of the National Academy of Sciences of the United States of America
Volume90
Issue number9
DOIs
Publication statusPublished - 1993

Keywords

  • N-deacetylase
  • N-sulfotransferase
  • recombinant enzyme

ASJC Scopus subject areas

  • General

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