Identification and characterization of a critical loop for the high activity of alginate lyase VaAly2 from the PL7_5 subfamily
As the major component in the cell wall of brown algae, alginates are degradable by alginate lyases via β-elimination. Alginate lyases can be categorized into various polysaccharide lyase (PL) families, and PL7 family alginate lyases are the largest group and can be divided into six subfamilies. How...
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Frontiers Media S.A.
2024-01-01
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| Series: | Frontiers in Microbiology |
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fmicb.2023.1333597/full |
| _version_ | 1797356958542462976 |
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| author | Muxuan Du Muxuan Du Xue Li Weipeng Qi Yingjie Li Lushan Wang |
| author_facet | Muxuan Du Muxuan Du Xue Li Weipeng Qi Yingjie Li Lushan Wang |
| author_sort | Muxuan Du |
| collection | DOAJ |
| description | As the major component in the cell wall of brown algae, alginates are degradable by alginate lyases via β-elimination. Alginate lyases can be categorized into various polysaccharide lyase (PL) families, and PL7 family alginate lyases are the largest group and can be divided into six subfamilies. However, the major difference among different PL7 subfamilies is not fully understood. In this work, a marine alginate lyase, VaAly2, from Vibrio alginolyticus ATCC 17749 belonging to the PL7_5 subfamily was identified and characterized. It displayed comparatively high alginolytic activities toward different alginate substrates and functions as a bifunctional lyase. Molecular docking and biochemical analysis suggested that VaAly2 not only contains a key catalyzing motif (HQY) conserved in the PL7 family but also exhibits some specific characters limited in the PL7_5 subfamily members, such as the key residues and a long loop1 structure around the active center. Our work provides insight into a loop structure around the center site which plays an important role in the activity and substrate binding of alginate lyases belonging to the PL7_5 subfamily. |
| first_indexed | 2024-03-08T14:37:22Z |
| format | Article |
| id | doaj.art-810191d58d1648dba0d1f38f0fa2f2eb |
| institution | Directory Open Access Journal |
| issn | 1664-302X |
| language | English |
| last_indexed | 2024-03-08T14:37:22Z |
| publishDate | 2024-01-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Microbiology |
| spelling | doaj.art-810191d58d1648dba0d1f38f0fa2f2eb2024-01-12T04:31:53ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2024-01-011410.3389/fmicb.2023.13335971333597Identification and characterization of a critical loop for the high activity of alginate lyase VaAly2 from the PL7_5 subfamilyMuxuan Du0Muxuan Du1Xue Li2Weipeng Qi3Yingjie Li4Lushan Wang5State Key Laboratory of Microbial Technology, Shandong University, Qingdao, ChinaSchool of Life Sciences, Shandong University, Qingdao, ChinaState Key Laboratory of Microbial Technology, Shandong University, Qingdao, ChinaFoshan Haitian (Gaoming) Flavoring & Food Co., Ltd., Foshan, ChinaState Key Laboratory of Microbial Technology, Shandong University, Qingdao, ChinaState Key Laboratory of Microbial Technology, Shandong University, Qingdao, ChinaAs the major component in the cell wall of brown algae, alginates are degradable by alginate lyases via β-elimination. Alginate lyases can be categorized into various polysaccharide lyase (PL) families, and PL7 family alginate lyases are the largest group and can be divided into six subfamilies. However, the major difference among different PL7 subfamilies is not fully understood. In this work, a marine alginate lyase, VaAly2, from Vibrio alginolyticus ATCC 17749 belonging to the PL7_5 subfamily was identified and characterized. It displayed comparatively high alginolytic activities toward different alginate substrates and functions as a bifunctional lyase. Molecular docking and biochemical analysis suggested that VaAly2 not only contains a key catalyzing motif (HQY) conserved in the PL7 family but also exhibits some specific characters limited in the PL7_5 subfamily members, such as the key residues and a long loop1 structure around the active center. Our work provides insight into a loop structure around the center site which plays an important role in the activity and substrate binding of alginate lyases belonging to the PL7_5 subfamily.https://www.frontiersin.org/articles/10.3389/fmicb.2023.1333597/fullalginatealginate lyasePL7_5 subfamilymutagenesismolecular docking |
| spellingShingle | Muxuan Du Muxuan Du Xue Li Weipeng Qi Yingjie Li Lushan Wang Identification and characterization of a critical loop for the high activity of alginate lyase VaAly2 from the PL7_5 subfamily Frontiers in Microbiology alginate alginate lyase PL7_5 subfamily mutagenesis molecular docking |
| title | Identification and characterization of a critical loop for the high activity of alginate lyase VaAly2 from the PL7_5 subfamily |
| title_full | Identification and characterization of a critical loop for the high activity of alginate lyase VaAly2 from the PL7_5 subfamily |
| title_fullStr | Identification and characterization of a critical loop for the high activity of alginate lyase VaAly2 from the PL7_5 subfamily |
| title_full_unstemmed | Identification and characterization of a critical loop for the high activity of alginate lyase VaAly2 from the PL7_5 subfamily |
| title_short | Identification and characterization of a critical loop for the high activity of alginate lyase VaAly2 from the PL7_5 subfamily |
| title_sort | identification and characterization of a critical loop for the high activity of alginate lyase vaaly2 from the pl7 5 subfamily |
| topic | alginate alginate lyase PL7_5 subfamily mutagenesis molecular docking |
| url | https://www.frontiersin.org/articles/10.3389/fmicb.2023.1333597/full |
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