4.5 Article

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

期刊

BIOCHEMICAL JOURNAL
卷 478, 期 2, 页码 281-298

出版社

PORTLAND PRESS LTD
DOI: 10.1042/BCJ20200657

关键词

-

资金

  1. National Natural Science Foundation of China [31570071, 31971201, 31800665]
  2. National Natural Science Foundation of Shandong Province [ZR2018BC013]
  3. Science and Technology Development Project of Shandong Province [2018GSF121002]
  4. China Postdoctoral Science Foundation [2019M662343]
  5. Major Scientific and Technological Innovation Project (MSTIP) of Shandong Province [2019JZZY010817]
  6. Project of Taishan Industry Leading Talent of Shandong Province [tscy20160311]

向作者/读者索取更多资源

This study identified a novel CS/DS 4-O-endosulfatase from a marine bacterium and investigated its catalytic mechanism, revealing substrate specificities, action patterns, and a decrease in enzyme activity with increasing substrate size. The deeper understanding of this enzyme provides a useful tool for exploring the structure-function relationship of CS/DS.
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 4-0-sulfate of disaccharide sequences GlcUA beta 1-3GalNAc(4S) or GlcUA beta 1-3GalNAc(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 GlcUA-Investigation of action pattern of a novel chondroitin sulfate/dermatan sulfate 4-O-endosulfatase1-3GaINAc(4S) connected to a disaccharide GlcUA(2S)beta 1-3GalNAc(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.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.5
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据