ArticleThe Journal of biological chemistry2021
A new carbohydrate-active oligosaccharide dehydratase is involved in the degradation of ulvan.
Article in The Journal of biological chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 16 citations in OpenAlex.
- Catalyzing Carbohydrate Cleavage: Glycosidases and Their Mechanisms.Chemical reviews · 2026Review
- Ulvan and Ulva oligosaccharides: a systematic review of structure, preparation, biological activities and applications.Bioresources and bioprocessing · 2023Review
- Unique alcohol dehydrogenases involved in algal sugar utilization by marine bacteria.Applied microbiology and biotechnology · 2023Article
- Metabolic engineering enables Bacillus licheniformis to grow on the marine polysaccharide ulvan.Microbial cell factories · 2022Article
- Functional metagenomic screening identifies an unexpected β-glucuronidase.Nature chemical biology · 2022Article
- Marine Polysaccharides: Occurrence, Enzymatic Degradation and Utilization.Chembiochem : a European journal of chemical biology · 2021Review
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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