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| Main Authors: | , , , , , , , , , , |
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| Format: | Artículo científico |
| Language: | en |
| Published: |
Journal of natural products
2025
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| Subjects: | |
| Online Access: | https://pubmed.ncbi.nlm.nih.gov/40498497/ |
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| _version_ | 1868266191359836160 |
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| author | Wang, Xuan Tian, Xiaolin Guo, Jiawei Cheng, Fangyuan Liu, Mingyu Zheng, Shanmin Feng, Yangliu Lv, Ying Li, Yuanning Li, Shengying Zhang, Xingwang |
| author_facet | Wang, Xuan Tian, Xiaolin Guo, Jiawei Cheng, Fangyuan Liu, Mingyu Zheng, Shanmin Feng, Yangliu Lv, Ying Li, Yuanning Li, Shengying Zhang, Xingwang Wang, Xuan Tian, Xiaolin Guo, Jiawei Cheng, Fangyuan Liu, Mingyu Zheng, Shanmin Feng, Yangliu Lv, Ying Li, Yuanning Li, Shengying Zhang, Xingwang |
| collection | PubMed - marine biology |
| contents | Carboxylic Acid Tailoring in Thioquinolobactin Biosynthesis. Wang, Xuan Tian, Xiaolin Guo, Jiawei Cheng, Fangyuan Liu, Mingyu Zheng, Shanmin Feng, Yangliu Lv, Ying Li, Yuanning Li, Shengying Zhang, Xingwang Carboxylic Acids Methyltransferases Molecular Structure Multigene Family Pseudomonas fluorescens Siderophores Quinolines The biosynthetic mechanism underlying the formation of thiocarboxylic acid moieties in natural products remains largely unknown. Thioquinolobactin (TQB) is a derived siderophore that contains a thiocarboxylic acid moiety within its structure. Although the biosynthetic gene cluster and proposed pathway for TQB formation have been reported, the biosynthetic mechanism related to the thiocarboxylic acid formation are yet to be fully understood. In this study, we address this question by demonstrating that a unique dual-domain protein QbsL, which possesses both CoA ligase and methyltransferase activities, along with the sulfurtransferase QbsK, facilitates the assembly of the thiocarboxylic acid. Based on this mechanism, we develop a chemoenzymatic method to convert carboxylic acid into selenocarboxylic acid, thereby generating selenium-containing analogues of TQB. These findings resolve the long-standing mystery in TQB biosynthesis and expand the synthetic toolkit for carboxylic acid modification. |
| format | Artículo científico |
| id | pubmed_40498497 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | Journal of natural products |
| record_format | pubmed |
| spellingShingle | Carboxylic Acid Tailoring in Thioquinolobactin Biosynthesis. Wang, Xuan Tian, Xiaolin Guo, Jiawei Cheng, Fangyuan Liu, Mingyu Zheng, Shanmin Feng, Yangliu Lv, Ying Li, Yuanning Li, Shengying Zhang, Xingwang Carboxylic Acids Methyltransferases Molecular Structure Multigene Family Pseudomonas fluorescens Siderophores Quinolines Carboxylic Acid Tailoring in Thioquinolobactin Biosynthesis. Wang, Xuan Tian, Xiaolin Guo, Jiawei Cheng, Fangyuan Liu, Mingyu Zheng, Shanmin Feng, Yangliu Lv, Ying Li, Yuanning Li, Shengying Zhang, Xingwang Carboxylic Acids Methyltransferases Molecular Structure Multigene Family Pseudomonas fluorescens Siderophores Quinolines The biosynthetic mechanism underlying the formation of thiocarboxylic acid moieties in natural products remains largely unknown. Thioquinolobactin (TQB) is a derived siderophore that contains a thiocarboxylic acid moiety within its structure. Although the biosynthetic gene cluster and proposed pathway for TQB formation have been reported, the biosynthetic mechanism related to the thiocarboxylic acid formation are yet to be fully understood. In this study, we address this question by demonstrating that a unique dual-domain protein QbsL, which possesses both CoA ligase and methyltransferase activities, along with the sulfurtransferase QbsK, facilitates the assembly of the thiocarboxylic acid. Based on this mechanism, we develop a chemoenzymatic method to convert carboxylic acid into selenocarboxylic acid, thereby generating selenium-containing analogues of TQB. These findings resolve the long-standing mystery in TQB biosynthesis and expand the synthetic toolkit for carboxylic acid modification. |
| title | Carboxylic Acid Tailoring in Thioquinolobactin Biosynthesis. |
| topic | Carboxylic Acids Methyltransferases Molecular Structure Multigene Family Pseudomonas fluorescens Siderophores Quinolines |
| url | https://pubmed.ncbi.nlm.nih.gov/40498497/ |