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Journal Articles PLoS ONE Year : 2016

Functional Exploration of the Polysaccharide Lyase Family PL6


Alginate, the main cell-wall polysaccharide of brown algae, is composed of two residues: mannuronic acid (M-residues) and, its C5-epimer, guluronic acid (G-residues). Alginate lyases define a class of enzymes that cleave the glycosidic bond of alginate by β-elimination. They are classified according to their ability to recognize the distribution of M- and G-residues and are named M-, G- or MG-lyases. In the CAZy database, alginate lyases have been grouped by sequence similarity into seven distinct polysaccharide lyase families. The polysaccharide lyase family PL6 is subdivided into three subfamilies. Subfamily PL6_1 includes three biochemically characterized enzymes (two alginate lyases and one dermatan sulfatase lyase). No characterized enzymes have been described in the two other subfamilies (PL6_2 and PL6_3). To improve the prediction of polysaccharide-lyase activity in the PL6 family, we re-examined the classification of the PL6 family and biochemically characterized a set of enzymes reflecting the diversity of the protein sequences. Our results show that subfamily PL6_1 includes two dermatan sulfates lyases and several alginate lyases that have various substrate specificities and modes of action. In contrast, subfamilies PL6_2 and PL6_3 were found to contain only endo-poly-MG-lyases.
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hal-01439117 , version 1 (07-09-2018)





Sophie Mathieu, Bernard Henrissat, Flavien Labre, Gudmund Skjak-Braek, William Helbert. Functional Exploration of the Polysaccharide Lyase Family PL6. PLoS ONE, 2016, 11 (7), pp.1-15. ⟨10.1371/journal.pone.0159415⟩. ⟨hal-01439117⟩
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