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Title
  • Cloning and Characterization of a Novel Chondroitin Sulfate/Dermatan Sulfate 4-O-Endosulfatase from a Marine Bacterium
Creator

Wang, Wenshuang

Han, Wenjun

Cai, Xingya

Zheng, Xiaoyu

Sugahara, Kazuyuki

Li, Fuchuan

Rights
    • 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 Chondroitin Sulfate
  • Other Dermatan Sulfate
  • Other Glycosaminoglycan
  • Other Oligosaccharide
  • Other Polysaccharide
  • Other Endosulfatase
  • Other Marine Bacterium
  • Other Sulfated Polysaccharide
  • NDC 460
Description
Other
  • 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.
PublisherAmerican Society for Biochemistry and Molecular Biology (ASBMB)
Date Issued 2015-03-20
Languageeng
NIItypejournal article
VersiontypeVoR
Identifier URI http://hdl.handle.net/2115/62913
Relation
  • isIdenticalTo PMID 25648894
  • isIdenticalTo DOI https://doi.org/10.1074/jbc.M114.629154
Journal
    • ISSN 0021-9258
    • ISSN 1083-351X
    • Journal of Biological Chemistry
    290(12), 7823-7832
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Oaidate2019-10-09T00:14:32Z