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| Auteurs principaux: | , , , , , , , , , , , , , , , |
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| Format: | Artículo científico |
| Langue: | en |
| Publié: |
Nature communications
2025
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| Sujets: | |
| Accès en ligne: | https://pubmed.ncbi.nlm.nih.gov/41107225/ |
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| author | Chen, Guangning Shen, Jingjing Li, Xinyu Sun, Menghui Dong, Sheng Sun, Ying Khamleng, Achiraya Mei, Xuanwei Zhang, Yuying Liu, Guanchen Chen, Fangyi Song, Xiao Liu, Kaimeng Feng, Yingang Xue, Changhu Chang, Yaoguang |
| author_facet | Chen, Guangning Shen, Jingjing Li, Xinyu Sun, Menghui Dong, Sheng Sun, Ying Khamleng, Achiraya Mei, Xuanwei Zhang, Yuying Liu, Guanchen Chen, Fangyi Song, Xiao Liu, Kaimeng Feng, Yingang Xue, Changhu Chang, Yaoguang Chen, Guangning Shen, Jingjing Li, Xinyu Sun, Menghui Dong, Sheng Sun, Ying Khamleng, Achiraya Mei, Xuanwei Zhang, Yuying Liu, Guanchen Chen, Fangyi Song, Xiao Liu, Kaimeng Feng, Yingang Xue, Changhu Chang, Yaoguang |
| collection | PubMed - marine biology |
| contents | Structure-function relationship of the GH168 fucanase reveals an unusual enzyme recognition mechanism for sulfated polysaccharide. Chen, Guangning Shen, Jingjing Li, Xinyu Sun, Menghui Dong, Sheng Sun, Ying Khamleng, Achiraya Mei, Xuanwei Zhang, Yuying Liu, Guanchen Chen, Fangyi Song, Xiao Liu, Kaimeng Feng, Yingang Xue, Changhu Chang, Yaoguang Polysaccharides Structure-Activity Relationship Sulfates alpha-L-Fucosidase Phylogeny Substrate Specificity Glycoside Hydrolases Bacterial Proteins Models, Molecular Sulfated fucan is one of the most recalcitrant polysaccharides. The molecular mechanism underlying the endo-1,3-fucanase, which plays a critical role in the breakdown of sulfated fucan, remains unexplained. Here, we conduct a comprehensive structure-function relationship investigation on the endo-1,3-fucanases within a family space-GH168. The family can be divided into four subfamilies according to phylogenetic relationship and functional similarities. Subfamily I, Ⅱ and Ⅳ preferentially recognize Fucp2(OSO), Fucp2,4(OSO) and Fucp units at the +1 subsite, respectively, while consistently recognizing the Fucp2(OSO) unit at the -1 subsite. Remarkably, two-thirds of the interacting residues are dedicated to the recognition of sulfate groups along the glycoside chains. This mechanism is distinct from the direct recognition of the sugar backbone employed by neutral polysaccharide hydrolases. These findings unveil a critical enzyme recognition mechanism for sulfate polysaccharides and promote the application of endo-1,3-fucanases in the structural analysis and oligosaccharide production of sulfated fucan. |
| format | Artículo científico |
| id | pubmed_41107225 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | Nature communications |
| record_format | pubmed |
| spellingShingle | Structure-function relationship of the GH168 fucanase reveals an unusual enzyme recognition mechanism for sulfated polysaccharide. Chen, Guangning Shen, Jingjing Li, Xinyu Sun, Menghui Dong, Sheng Sun, Ying Khamleng, Achiraya Mei, Xuanwei Zhang, Yuying Liu, Guanchen Chen, Fangyi Song, Xiao Liu, Kaimeng Feng, Yingang Xue, Changhu Chang, Yaoguang Polysaccharides Structure-Activity Relationship Sulfates alpha-L-Fucosidase Phylogeny Substrate Specificity Glycoside Hydrolases Bacterial Proteins Models, Molecular Structure-function relationship of the GH168 fucanase reveals an unusual enzyme recognition mechanism for sulfated polysaccharide. Chen, Guangning Shen, Jingjing Li, Xinyu Sun, Menghui Dong, Sheng Sun, Ying Khamleng, Achiraya Mei, Xuanwei Zhang, Yuying Liu, Guanchen Chen, Fangyi Song, Xiao Liu, Kaimeng Feng, Yingang Xue, Changhu Chang, Yaoguang Polysaccharides Structure-Activity Relationship Sulfates alpha-L-Fucosidase Phylogeny Substrate Specificity Glycoside Hydrolases Bacterial Proteins Models, Molecular Sulfated fucan is one of the most recalcitrant polysaccharides. The molecular mechanism underlying the endo-1,3-fucanase, which plays a critical role in the breakdown of sulfated fucan, remains unexplained. Here, we conduct a comprehensive structure-function relationship investigation on the endo-1,3-fucanases within a family space-GH168. The family can be divided into four subfamilies according to phylogenetic relationship and functional similarities. Subfamily I, Ⅱ and Ⅳ preferentially recognize Fucp2(OSO), Fucp2,4(OSO) and Fucp units at the +1 subsite, respectively, while consistently recognizing the Fucp2(OSO) unit at the -1 subsite. Remarkably, two-thirds of the interacting residues are dedicated to the recognition of sulfate groups along the glycoside chains. This mechanism is distinct from the direct recognition of the sugar backbone employed by neutral polysaccharide hydrolases. These findings unveil a critical enzyme recognition mechanism for sulfate polysaccharides and promote the application of endo-1,3-fucanases in the structural analysis and oligosaccharide production of sulfated fucan. |
| title | Structure-function relationship of the GH168 fucanase reveals an unusual enzyme recognition mechanism for sulfated polysaccharide. |
| topic | Polysaccharides Structure-Activity Relationship Sulfates alpha-L-Fucosidase Phylogeny Substrate Specificity Glycoside Hydrolases Bacterial Proteins Models, Molecular |
| url | https://pubmed.ncbi.nlm.nih.gov/41107225/ |