Investigation of action pattern of a novel chondroitin sulfate/dermatan sulfate 4-O-endosulfatase

Recently, a novel CS/DS 4-O-endosulfatase was identified from marine bacterium and its catalytic mechanism investigated further (Wang, W., et. al (2015) J. Biol. Chem.290, 7823–7832; Wang, S., (2019) Front. Microbiol.10, 1309). In the study herein, we provide new insight about structural characteristics of substrate which determine activity this enzyme. The specificities were probed by using libraries structure-defined oligosaccharides issued synthetic enzymatic sources. We found that effectively remove 4-O-sulfate disaccharide sequences GlcUAβ1-3GalNAc(4S) or GlcUAβ1-3GalNAc(4S,6S) in all tested hexasaccharides. sulfated GalNac residue is resistant to enzyme when adjacent uronic residues are as shown lack desulfation connected GlcUA(2S)β1-3GalNAc(6S) an octasaccharide. 3-O-sulfation GlcUA also hinder action exhibited oriented reducing non-reducing whatever saturation not end. Finally, decreases with increase size. With deeper understanding 4-O-endosulfatase, such chondroitin sulfate (CS)/dermatan (DS) sulfatase useful tool for exploring structure–function relationship CS/DS.