Characterization of Redox Sensitive Brown Algal Mannitol-1-Phosphatases
Macroalgae (seaweeds) are key primary producers in marine coastal habitats and largely contribute to global ocean carbon fluxes. They also represent attractive renewable feedstock for the production of biofuels, food, feed, and bioactive. Brown algae are seaweeds that produce alginates and fucose co...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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MDPI AG
2022-12-01
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| Series: | Phycology |
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| Online Access: | https://www.mdpi.com/2673-9410/3/1/1 |
| _version_ | 1797858334196367360 |
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| author | Yoran Le Strat Thierry Tonon Catherine Leblanc Agnès Groisillier |
| author_facet | Yoran Le Strat Thierry Tonon Catherine Leblanc Agnès Groisillier |
| author_sort | Yoran Le Strat |
| collection | DOAJ |
| description | Macroalgae (seaweeds) are key primary producers in marine coastal habitats and largely contribute to global ocean carbon fluxes. They also represent attractive renewable feedstock for the production of biofuels, food, feed, and bioactive. Brown algae are seaweeds that produce alginates and fucose containing sulfated polysaccharides in their cell wall and laminarin and mannitol for carbon storage. The availability of genomes of the kelp <i>Saccharina japonica</i> and of the filamentous <i>Ectocarpus</i> sp. paved the way for the biochemical characterization of recombinant enzymes involved in their polysaccharide and carbohydrates synthesis, including, notably, mannitol. Brown algal mannitol biosynthesis starts with the conversion of fructose-6-phospate into mannitol-1-phosphate (mannitol-1P), and this intermediate is hydrolysed by a haloacid dehalogenase phosphatase (M1Pase) to produce mannitol. We report here the biochemical characterization of a second M1Pase in <i>Ectocarpus</i> sp. (EsM1Pase1). Both <i>Ectocarpus</i> M1Pases were redox-sensitive enzymes, with EsM1Pase1 active only in presence of the reducing agent. Such catalytic properties have not been observed for any M1Pases yet. EsM1Pases were specific to mannitol-1-P, in contrast to <i>S. japonica</i> M1Pases that could act on other phosphorylated sugars. Finally, brown algal M1Pases formed two well-supported clades, with possible distinct subcellular localization and physiological role(s) under diverse environmental conditions and/or life cycle stages. |
| first_indexed | 2024-04-09T21:11:45Z |
| format | Article |
| id | doaj.art-3052a1f230ab4881a5cecd18327e77d9 |
| institution | Directory Open Access Journal |
| issn | 2673-9410 |
| language | English |
| last_indexed | 2024-04-09T21:11:45Z |
| publishDate | 2022-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Phycology |
| spelling | doaj.art-3052a1f230ab4881a5cecd18327e77d92023-03-28T14:33:00ZengMDPI AGPhycology2673-94102022-12-013111210.3390/phycology3010001Characterization of Redox Sensitive Brown Algal Mannitol-1-PhosphatasesYoran Le Strat0Thierry Tonon1Catherine Leblanc2Agnès Groisillier3UMR 8227, Integrative Biology of Marine Models (LBI2M), Station Biologique de Roscoff (SBR), Sorbonne Université, CNRS, F-29680 Roscoff, FranceCentre for Novel Agricultural Products, Department of Biology, University of York, York YO10 5DD, UKUMR 8227, Integrative Biology of Marine Models (LBI2M), Station Biologique de Roscoff (SBR), Sorbonne Université, CNRS, F-29680 Roscoff, FranceUMR 8227, Integrative Biology of Marine Models (LBI2M), Station Biologique de Roscoff (SBR), Sorbonne Université, CNRS, F-29680 Roscoff, FranceMacroalgae (seaweeds) are key primary producers in marine coastal habitats and largely contribute to global ocean carbon fluxes. They also represent attractive renewable feedstock for the production of biofuels, food, feed, and bioactive. Brown algae are seaweeds that produce alginates and fucose containing sulfated polysaccharides in their cell wall and laminarin and mannitol for carbon storage. The availability of genomes of the kelp <i>Saccharina japonica</i> and of the filamentous <i>Ectocarpus</i> sp. paved the way for the biochemical characterization of recombinant enzymes involved in their polysaccharide and carbohydrates synthesis, including, notably, mannitol. Brown algal mannitol biosynthesis starts with the conversion of fructose-6-phospate into mannitol-1-phosphate (mannitol-1P), and this intermediate is hydrolysed by a haloacid dehalogenase phosphatase (M1Pase) to produce mannitol. We report here the biochemical characterization of a second M1Pase in <i>Ectocarpus</i> sp. (EsM1Pase1). Both <i>Ectocarpus</i> M1Pases were redox-sensitive enzymes, with EsM1Pase1 active only in presence of the reducing agent. Such catalytic properties have not been observed for any M1Pases yet. EsM1Pases were specific to mannitol-1-P, in contrast to <i>S. japonica</i> M1Pases that could act on other phosphorylated sugars. Finally, brown algal M1Pases formed two well-supported clades, with possible distinct subcellular localization and physiological role(s) under diverse environmental conditions and/or life cycle stages.https://www.mdpi.com/2673-9410/3/1/1brown algae<i>Ectocarpus</i> sp.mannitol cyclemannitol-1-phosphataserecombinant proteinredox sensitivity |
| spellingShingle | Yoran Le Strat Thierry Tonon Catherine Leblanc Agnès Groisillier Characterization of Redox Sensitive Brown Algal Mannitol-1-Phosphatases Phycology brown algae <i>Ectocarpus</i> sp. mannitol cycle mannitol-1-phosphatase recombinant protein redox sensitivity |
| title | Characterization of Redox Sensitive Brown Algal Mannitol-1-Phosphatases |
| title_full | Characterization of Redox Sensitive Brown Algal Mannitol-1-Phosphatases |
| title_fullStr | Characterization of Redox Sensitive Brown Algal Mannitol-1-Phosphatases |
| title_full_unstemmed | Characterization of Redox Sensitive Brown Algal Mannitol-1-Phosphatases |
| title_short | Characterization of Redox Sensitive Brown Algal Mannitol-1-Phosphatases |
| title_sort | characterization of redox sensitive brown algal mannitol 1 phosphatases |
| topic | brown algae <i>Ectocarpus</i> sp. mannitol cycle mannitol-1-phosphatase recombinant protein redox sensitivity |
| url | https://www.mdpi.com/2673-9410/3/1/1 |
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