A library of 23 synthetic heparan sulfate (HS) oligosaccharides, varying in chain length, types and positions of modifications, was used to analyze the substrate specificities of heparin lyase III enzymes from both Flavobacterium heparinum and Bacteroides eggerthii. The influence of specific modifications, including N-substitution, 2-O sulfation, 6-O sulfation and 3-O sulfation on lyase III digestion was examined systematically. It was demonstrated that lyase III from both sources can completely digest oligosaccharides lacking O-sulfates. 2-O Sulfation completely blocked cleavage at the corresponding site; 6-O and 3-O sulfation on glucosamine residues inhibited enzyme activity. We also observed that there are differences in substrate specificities between the two lyase III enzymes for highly sulfated oligosaccharides. These findings will facilitate obtaining and analyzing the functional sulfated domains from large HS polymer, to better understand their structure/function relationships in biological processes.

Original languageEnglish
Pages (from-to)208-217
Number of pages10
Issue number3
Early online date1 Apr 2021
Publication statusPublished - 1 Mar 2022


  • glycomics
  • glycosaminoglycans
  • heparan sulfate
  • heparin lyase
  • mass spectrometry


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