A new carbohydrate-active oligosaccharide dehydratase is involved in the degradation of ulvan
| Autor: | Theresa Dutschei, Uwe T. Bornscheuer, Christoph Suster, Nadine Gerlach, Thomas Schweder, Daniel Bartosik, Jan-Hendrik Hehemann, Marcus Bäumgen, Marko D. Mihovilovic, Christian Stanetty, Lukas Reisky |
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| Rok vydání: | 2021 |
| Předmět: |
Aquatic Organisms
Iduronic acid Uronic acid Polysaccharide sulfatase Biochemistry pathway elucidation CAZyme carbohydrate active enzyme chemistry.chemical_compound Residue (chemistry) dehydratase ulvan Bacterial Proteins Polysaccharides marine polysaccharide GH glycoside hydrolase PL polysaccharide lyase Glycoside hydrolase enzyme mechanism glycoside hydrolase Molecular Biology PUL polysaccharide utilization loci chemistry.chemical_classification Cell Biology Oligosaccharide C-PAGE carbohydrate electrophoresis FACE fluorophore-assisted carbohydrate electrophoresis Uronic Acids DHy Dehydratase chemistry Dehydratase carbohydrate-active enzymes Carbohydrate Dehydrogenases Fluorophore-assisted carbohydrate electrophoresis Flavobacteriaceae Research Article novel enzyme |
| Zdroj: | The Journal of Biological Chemistry JOURNAL OF BIOLOGICAL CHEMISTRY |
| ISSN: | 1083-351X |
| Popis: | Marine algae catalyze half of all global photosynthetic production of carbohydrates. Owing to their fast growth rates, Ulva spp. rapidly produce substantial amounts of carbohydrate-rich biomass and represent an emerging renewable energy and carbon resource. Their major cell wall polysaccharide is the anionic carbohydrate ulvan. Here, we describe a new enzymatic degradation pathway of the marine bacterium Formosa agariphila for ulvan oligosaccharides involving unsaturated uronic acid at the nonreducing end linked to rhamnose-3-sulfate and glucuronic or iduronic acid (Δ-Rha3S-GlcA/IdoA-Rha3S). Notably, we discovered a new dehydratase (P29_PDnc) acting on the nonreducing end of ulvan oligosaccharides, i.e., GlcA/IdoA-Rha3S, forming the aforementioned unsaturated uronic acid residue. This residue represents the substrate for GH105 glycoside hydrolases, which complements the enzymatic degradation pathway including one ulvan lyase, one multimodular sulfatase, three glycoside hydrolases, and the dehydratase P29_PDnc, the latter being described for the first time. Our research thus shows that the oligosaccharide dehydratase is involved in the degradation of carboxylated polysaccharides into monosaccharides. |
| Databáze: | OpenAIRE |
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