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Title
  • en Cloning and Characterization of a Novel Chondroitin Sulfate/Dermatan Sulfate 4-O-Endosulfatase from a Marine Bacterium
Creator
    • en Wang, Wenshuang
    • en Han, Wenjun
    • en Cai, Xingya
    • en Zheng, Xiaoyu
    • en Li, Fuchuan
Accessrights open access
Rights
  • en This research was originally published in Journal of Biological Chemistry. Wenshuang Wang, Wenjun Han, Xingya Cai, Xiaoyu Zheng, Kazuyuki Sugahara and Fuchuan Li. Cloning and Characterization of a Novel Chondroitin Sulfate/Dermatan Sulfate 4-O-Endosulfatase from a Marine Bacterium. Journal of Biological Chemistry. 2015; Vol:290(12) p.7823-7832 © the American Society for Biochemistry and Molecular Biology
Subject
  • Other en Chondroitin Sulfate
  • Other en Dermatan Sulfate
  • Other en Glycosaminoglycan
  • Other en Oligosaccharide
  • Other en Polysaccharide
  • Other en Endosulfatase
  • Other en Marine Bacterium
  • Other en Sulfated Polysaccharide
  • NDC 460
Description
  • Abstract en Sulfatases are potentially useful tools for structure-function studies of glycosaminoglycans (GAGs). To date, various GAG exosulfatases have been identified in eukaryotes and prokaryotes. However, endosulfatases that act on GAGs have rarely been reported. Recently, a novel HA and CS lyase (HCLase) was identified for the first time from a marine bacterium (Han, W., Wang, W., Zhao, M., Sugahara, K., and Li, F. (2014) J. Biol. Chem. 289, 27886–27898). In this study, a putative sulfatase gene, closely linked to the hclase gene in the genome, was recombinantly expressed and characterized in detail. The recombinant protein showed a specific N-acetylgalactosamine-4-O-sulfatase activity that removes 4-O-sulfate from both disaccharides and polysaccharides of chondroitin sulfate (CS)/dermatan sulfate (DS), suggesting that this sulfatase represents a novel endosulfatase. The novel endosulfatase exhibited maximal reaction rate in a phosphate buffer (pH 8.0) at 30 °C and effectively removed 17–65% of 4-O-sulfates from various CS and DS and thus significantly inhibited the interactions of CS and DS with a positively supercharged fluorescent protein. Moreover, this endosulfatase significantly promoted the digestion of CS by HCLase, suggesting that it enhances the digestion of CS/DS by the bacterium. Therefore, this endosulfatase is a potential tool for use in CS/DS-related studies and applications.
Publisher en American Society for Biochemistry and Molecular Biology (ASBMB)
Date
    Issued2015-03-20
Language
  • eng
Resource Type journal article
Version Type VoR
Identifier HDL http://hdl.handle.net/2115/62913
Relation
  • isIdenticalTo DOI https://doi.org/10.1074/jbc.M114.629154
  • PMID 25648894
Journal
    • PISSN 0021-9258
    • EISSN 1083-351X
      • en Journal of Biological Chemistry
      • Volume Number290 Issue Number12 Page Start7823 Page End7832
File
Oaidate 2023-08-19