EC Number   |
Natural Substrates  |
|---|
   4.2.2.3 | more |
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 | more |
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 | more |
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 | more |
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 | more |
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 | more |
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 |
