Polysaccharide lyase that catalyzes the depolymerization of alginate via a beta-elimination mechanism, cleaving the beta-1,4 glycosidic bond between two adjacent sugar residues. Acts specifically on alginate and each of its block structures, with highest activity toward poly-beta-D-mannuronate (poly-ManA). Shows an exolytic mode of action, producing unsaturated monomers. Displays a very low activity against poly-beta-D-glucuronate (poly-GlcA), and is not active on poly-alpha-D-galacturonate, hyaluronan, heparin, heparan sulfate and chondroitin sulfate.
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Also known as Alginate lyase (Exolytic alginate lyase) (Exolytic polysaccharide lyase).
Also known as Alginate lyase 7 (Mannuronan epimerase 7) (Poly(beta-D-mannuronate) C5 epimerase 7) (Poly(beta-D-mannuronate) lyase 7) (Poly(mana) alginate lyase 7).
Converts beta-D-mannuronic acid (M) to alpha-L-guluronic acid (G). Has both epimerase and lyase activities. Contributes to abortive encystment by degrading the coat from inside the cyst. Important for cyst germination.