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BcelPL6 is a mannuronic acid-specific alginate lyase belonging to the polysaccharide lyase family 6 (PL6), sourced from the human gut bacterium Bacteroides cellulosilyticus. This enzyme is a monomeric, single-domain protein characterized by a parallel beta-helix fold and a conserved asparagine ladder. It functions by depolymerizing alginate, a structural polysaccharide from brown algae, specifically targeting poly-mannuronic acid (polyM) blocks through a beta-elimination mechanism. BcelPL6 releases unsaturated oligosaccharides, primarily di- and trisaccharides, as end products. Its discovery in the human gut microbiome highlights the specialized metabolic pathways that allow commensal bacteria to process marine-derived dietary fibers, contributing to the overall carbohydrate fermentation capacity of the host's microbiota.
Cleavage of 1,4-glycosidic linkages in alginate via a beta-elimination reaction
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