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Issue 32, 2017
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Insights into the role of 3-O-sulfotransferase in heparan sulfate biosynthesis

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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–ANS or I–ANAc. 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, I2S–ANS and G–ANAc. The results further illustrate that 3-O-sulfation can be induced outside of the classical heparin-binding pentasaccharide sequence, show that 3-O-sulfation of glucosamine is not a sufficient condition for antithrombin stabilization and suggest that the use of this enzyme during HS biosynthesis may not occur as the final enzymatic step.

Graphical abstract: Insights into the role of 3-O-sulfotransferase in heparan sulfate biosynthesis

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Supplementary files

Article information


Submitted
23 Jun 2017
Accepted
27 Jul 2017
First published
27 Jul 2017

Org. Biomol. Chem., 2017,15, 6792-6799
Article type
Paper

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

M. C. Z. Meneghetti, T. Gesteira Ferreira, A. K. Tashima, S. F. Chavante, E. A. Yates, J. Liu, H. B. Nader and M. A. Lima, Org. Biomol. Chem., 2017, 15, 6792
DOI: 10.1039/C7OB01533J

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