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Cloning and Characterization of a Novel Chondroitin Sulfate/Dermatan Sulfate 4-O-Endosulfatase from a Marine Bacterium
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| 作成者 |
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| アクセス権 |
open access |
| 権利情報 |
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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
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| 主題 |
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Other
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Chondroitin Sulfate
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Other
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Dermatan Sulfate
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Other
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Glycosaminoglycan
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Other
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Oligosaccharide
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Other
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Polysaccharide
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Other
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Endosulfatase
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Other
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Marine Bacterium
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Other
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Sulfated Polysaccharide
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NDC
460
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| 内容注記 |
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Abstract
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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.
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| 出版者 |
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American Society for Biochemistry and Molecular Biology (ASBMB)
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| 日付 |
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| 言語 |
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| 資源タイプ |
journal article |
| 出版タイプ |
VoR |
| 資源識別子 |
HDL
http://hdl.handle.net/2115/62913
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| 関連 |
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DOI
https://doi.org/10.1074/jbc.M114.629154
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PMID
25648894
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| 収録誌情報 |
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PISSN
0021-9258
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EISSN
1083-351X
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Journal of Biological Chemistry
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巻290
号12
開始ページ7823
終了ページ7832
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| ファイル |
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| コンテンツ更新日時 |
2023-08-19 |
