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.
J. Wu et al., "Influence of Saccharide Modifications on Heparin Lyase III Substrate Specificities," Glycobiology, vol. 32, no. 3, pp. 208 - 217, Oxford University Press, Mar 2022.
The definitive version is available at https://doi.org/10.1093/glycob/cwab023
Chemical and Biochemical Engineering
Keywords and Phrases
glycomics; glycosaminoglycans; heparan sulfate; heparin lyase; mass spectrometry
International Standard Serial Number (ISSN)
Article - Journal
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01 Mar 2022
National Institutes of Health (grants P41GM104603, R21HL131554 and U01CA221234 to J.Z. and grants P41GM103390 and HLBI R01HL151617 to G.-J.B.)