Insights into the role of 3-O-sulfotransferase in heparan sulfate biosynthesis.

ABSTRACT: 3-O-Sulfotransferase enzyme (sHS) from Litopenaeus vannamei was cloned and its substrate specificity was investigated against a number of GAG structures, including modified heparin polysaccharides and model oligosaccharides. For the heparin polysaccharides, derived from porcine intestinal mucosa heparin, sulfate groups were incorporated into glucosamine residues containing both N-sulfated and N-acetylated substitution within the regions of the predominant repeating disaccharide, either I-A_NS or I-A_NAc. However, the resulting polysaccharides did not stabilize antithrombin, which is correlated with anticoagulant activity. It was also shown that the enzyme was able to sulfate disaccharides, I_2S-A_NS and G-A_NAc. The results further illustra

SUBMITTER: Meneghetti MCZ 

PROVIDER: S-EPMC6518394 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature