RGD Reference Report - A single protein catalyzes both N-deacetylation and N-sulfation during the biosynthesis of heparan sulfate. - Rat Genome Database

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

Authors: Wei, Z  Swiedler, S J  Ishihara, M  Orellana, A  Hirschberg, C B 
Citation: Wei Z, etal., Proc Natl Acad Sci U S A. 1993 May 1;90(9):3885-8. doi: 10.1073/pnas.90.9.3885.
RGD ID: 151356652
Pubmed: PMID:8483907   (View Abstract at PubMed)
PMCID: PMC46410   (View Article at PubMed Central)
DOI: DOI:10.1073/pnas.90.9.3885   (Journal Full-text)

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.



Gene Ontology Annotations    

Biological Process

Molecular Function

Objects Annotated

Genes (Rattus norvegicus)
Ndst1  (N-deacetylase and N-sulfotransferase 1)


Additional Information