4.2.2.3 additional information alginate lyase A1-III is a beta-D-mannuronosyl linkage-specific enzyme that acts on alginate tetrasaccharide as the minimum substrate and produces disaccharides and trisaccharides from alginate 4.2.2.3 additional information alginate lyase AlgL catalyzes the cleavage of the polysaccharide alginate through a beta-elimination reaction. AlgL operates preferentially on non-acetylated alginate or its precursor mannuronan. AlgL operates as an exopolysaccharide lyase 4.2.2.3 additional information AlgL is a poly-(beta-D-mannuronate) lyase that preferentially degrades deacetylated polymannuronate via a beta-elimination reaction, resulting in an unsaturated uronic acid at the nonreducing end of the molecule 4.2.2.3 additional information KJ-2 poly-mannuronate-guluronate-specific alginate lyase preferably degrades the glycosidic bond in beta-D-mannuronoyl-alpha-L-guluronate linkage than that in alpha-L-guluronoyl-beta-D-mannuronate linkage 4.2.2.3 additional information the enzyme Alg17c is an exolytic alginate lyase, structure-function characterization of active site residues that are suggested to be involved in the exolytic mechanism of alginate depolymerization, overview 4.2.2.3 additional information the enzyme is an endolytic polymannuronate lyase 4.2.2.3 sodium alginate - 4.2.2.3 sodium alginate AlyA5 cleaves unsaturated units, alpha-L-guluronate or beta-D-manuronate residues, at the nonreducing end of oligo-alginates in an exolytic fashion, cf. EC 4.2.2.11 4.2.2.3 trisaccharides of alginate oligoalginate lyase, complete depolymerization of alginate