%0 Journal Article %T Investigation of Action Pattern of a Novel Chondroitin Sulfate/Dermatan Sulfate 4- O -Endosulfatase %+ Shandong University %+ Laboratoire Analyse, Modélisation et Matériaux pour la Biologie et l'Environnement (LAMBE - UMR 8587) %+ Institut Parisien de Chimie Moléculaire (IPCM) %+ Institut de Chimie Organique et Analytique (ICOA) %+ Meijo University %+ Universidad Miguel Hernández [Elche] (UMH) %A Wang, Wenshuang %A Przybylski, Cédric %A Cai, Xiaojuan %A Lopin-Bon, Chrystel %A Jiao, Runmiao %A Shi, Liran %A Sugahara, Kazuyuki %A Neira, José %A Daniel, Régis %A Li, Fuchuan %< avec comité de lecture %@ 0264-6021 %J Biochemical Journal %I Portland Press %V 478 %N 2 %P 281-298 %8 2020-01-04 %D 2020 %R 10.1042/BCJ20200657 %K action pattern %K chondroitin sulfate %K glycosaminoglycans %K Oligosaccharide %K sulfatase %Z Life Sciences [q-bio] %Z Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM]Journal articles %X Recently, a novel CS/DS 4-O-endosulfatase was identified from a marine bacterium and its catalytic mechanism was investigated further (Wang, W., et. al (2015) J. Biol. Chem.290, 7823–7832; Wang, S., et. al (2019) Front. Microbiol.10, 1309). In the study herein, we provide new insight about the structural characteristics of the substrate which determine the activity of this enzyme. The substrate specificities of the 4-O-endosulfatase were probed by using libraries of structure-defined CS/DS oligosaccharides issued from synthetic and enzymatic sources. We found that this 4-O-endosulfatase effectively remove the 4-O-sulfate of disaccharide sequences GlcUAβ1-3GalNAc(4S) or GlcUAβ1-3GalNAc(4S,6S) in all tested hexasaccharides. The sulfated GalNac residue is resistant to the enzyme when adjacent uronic residues are sulfated as shown by the lack of enzymatic desulfation of GlcUAβ1-3GalNAc(4S) connected to a disaccharide GlcUA(2S)β1-3GalNAc(6S) in an octasaccharide. The 3-O-sulfation of GlcUA was also shown to hinder the action of this enzyme. The 4-O-endosulfatase exhibited an oriented action from the reducing to the non-reducing whatever the saturation or not of the non-reducing end. Finally, the activity of the 4-O-endosulfatase decreases with the increase in substrate size. With the deeper understanding of this novel 4-O-endosulfatase, such chondroitin sulfate (CS)/dermatan sulfate (DS) sulfatase is a useful tool for exploring the structure–function relationship of CS/DS. %G English %2 https://univ-evry.hal.science/hal-03098070/document %2 https://univ-evry.hal.science/hal-03098070/file/manuscrit%20soumis.pdf %L hal-03098070 %U https://univ-evry.hal.science/hal-03098070 %~ CEA %~ ENS-PARIS %~ ESPCI %~ ENSCP %~ CNRS %~ UNIV-ORLEANS %~ UNIV-CERGY %~ UNIV-EVRY %~ ENSC-PARIS %~ ICOA %~ PARISTECH %~ IPCM %~ DSV %~ INC-CNRS %~ CEA-UPSAY %~ PSL %~ LAMBE %~ UNIV-PARIS-SACLAY %~ UNIV-EVRY-SACLAY %~ IPCM-CSOB %~ CEA-DRF %~ SORBONNE-UNIVERSITE %~ SORBONNE-UNIV %~ SU-SCIENCES %~ TEST-HALCNRS %~ ENSCP-PSL %~ ENS-PSL %~ ESPCI-PSL %~ UNIVERSITE-PARIS-SACLAY %~ CY-TECH-SE %~ SU-TI %~ GS-CHIMIE %~ GS-LIFE-SCIENCES-HEALTH %~ INSTITUT-SCIENCES-LUMIERE %~ ALLIANCE-SU %~ CHIMIE-SU %~ LABOS-SYNORG