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| Main Authors: | , , , , , |
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| Format: | Artículo científico |
| Language: | en |
| Published: |
Proceedings of the National Academy of Sciences of the United States of America
2026
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| Subjects: | |
| Online Access: | https://pubmed.ncbi.nlm.nih.gov/41955116/ |
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| _version_ | 1868266061997015040 |
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| author | Cao, Tianjun Bai, Xuechun You, Tingting Jiang, Yanyou Lohr, Martin Li, Xiaobo |
| author_facet | Cao, Tianjun Bai, Xuechun You, Tingting Jiang, Yanyou Lohr, Martin Li, Xiaobo Cao, Tianjun Bai, Xuechun You, Tingting Jiang, Yanyou Lohr, Martin Li, Xiaobo |
| collection | PubMed - marine biology |
| contents | An acetyltransferase family required for biosynthesis of diverse marine carotenoids. Cao, Tianjun Bai, Xuechun You, Tingting Jiang, Yanyou Lohr, Martin Li, Xiaobo Carotenoids Phylogeny Diatoms Acetyltransferases Xanthophylls Dinoflagellida Chromalveolate algae such as diatoms, haptophytes, and dinoflagellates are main contributors to oceanic primary production, sustaining marine ecosystems and global carbon cycles while synthesizing a striking array of acetylated carotenoids like fucoxanthin and peridinin. These pigments optimize photosynthetic light harvesting in the algae and offer nutritional benefits for humans, yet knowledge of their biosynthetic pathways is still incomplete, particularly the shared acetylation step. By screening 39 candidate genes in the diatom , we identified an enzyme with anthophyll etylransferase (XACT) activity that is indispensable for this modification. Disrupting in and the eustigmatophyte abolished xanthophyll acetylation. Phylogenetic analyses revealed that XACT is exclusively present in chromalveolates synthesizing acetylated xanthophylls. In vitro assays with recombinant XACT enzymes from , , the brown alga , the dinoflagellate , and a haptophyte confirmed their general activity toward allenic precursor carotenoids but exhibited lineage-specific substrate preferences, explaining the diversified carotenoid structures across lineages. The broad substrate specificity of XACT from led us to reinvestigate the substrate specificities of other enzymes involved in fucoxanthin formation, indicating that fucoxanthin biosynthesis in diatoms proceeds via a multibranched rather than a linear pathway. XACT from showed a distinctly narrow substrate spectrum, providing key evidence for the order of the two previously proposed steps in brown algal fucoxanthin biosynthesis. Our work resolves a long-standing gap in marine carotenoid biosynthesis and identifies the relaxed substrate specificities of the enzymes involved as an important driver for the multitude of algal carotenoid structures. |
| format | Artículo científico |
| id | pubmed_41955116 |
| institution | PubMed |
| language | en |
| publishDate | 2026 |
| publisher | Proceedings of the National Academy of Sciences of the United States of America |
| record_format | pubmed |
| spellingShingle | An acetyltransferase family required for biosynthesis of diverse marine carotenoids. Cao, Tianjun Bai, Xuechun You, Tingting Jiang, Yanyou Lohr, Martin Li, Xiaobo Carotenoids Phylogeny Diatoms Acetyltransferases Xanthophylls Dinoflagellida An acetyltransferase family required for biosynthesis of diverse marine carotenoids. Cao, Tianjun Bai, Xuechun You, Tingting Jiang, Yanyou Lohr, Martin Li, Xiaobo Carotenoids Phylogeny Diatoms Acetyltransferases Xanthophylls Dinoflagellida Chromalveolate algae such as diatoms, haptophytes, and dinoflagellates are main contributors to oceanic primary production, sustaining marine ecosystems and global carbon cycles while synthesizing a striking array of acetylated carotenoids like fucoxanthin and peridinin. These pigments optimize photosynthetic light harvesting in the algae and offer nutritional benefits for humans, yet knowledge of their biosynthetic pathways is still incomplete, particularly the shared acetylation step. By screening 39 candidate genes in the diatom , we identified an enzyme with anthophyll etylransferase (XACT) activity that is indispensable for this modification. Disrupting in and the eustigmatophyte abolished xanthophyll acetylation. Phylogenetic analyses revealed that XACT is exclusively present in chromalveolates synthesizing acetylated xanthophylls. In vitro assays with recombinant XACT enzymes from , , the brown alga , the dinoflagellate , and a haptophyte confirmed their general activity toward allenic precursor carotenoids but exhibited lineage-specific substrate preferences, explaining the diversified carotenoid structures across lineages. The broad substrate specificity of XACT from led us to reinvestigate the substrate specificities of other enzymes involved in fucoxanthin formation, indicating that fucoxanthin biosynthesis in diatoms proceeds via a multibranched rather than a linear pathway. XACT from showed a distinctly narrow substrate spectrum, providing key evidence for the order of the two previously proposed steps in brown algal fucoxanthin biosynthesis. Our work resolves a long-standing gap in marine carotenoid biosynthesis and identifies the relaxed substrate specificities of the enzymes involved as an important driver for the multitude of algal carotenoid structures. |
| title | An acetyltransferase family required for biosynthesis of diverse marine carotenoids. |
| topic | Carotenoids Phylogeny Diatoms Acetyltransferases Xanthophylls Dinoflagellida |
| url | https://pubmed.ncbi.nlm.nih.gov/41955116/ |