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 |
alginate lyases degrade the polysaccharide by cleaving the glycosidic linkages through a beta-elimination reaction. Lyase AlyA is bifunctional and shows activities toward both polyG (alpha-L-guluronic acid), activity of EC 4.2.2.11, and polyM (beta-D-mannuronic acid). AlyA is endolytic, acting on G-blocks and MG-blocks where G-M linkages are cleaved in the latter substrate. Substrate specificities of diverse enzyme mutants, overview |
| 4.2.2.3 | more |
alginate-lyase is not essential for the production of alginate. When this enzyme is present, as in wild-type cells of Azotobacter vinelandii, its role is restricted to a post-polymerization step, with its activity reaching a maximum in the pres-stationary phase of growth |
| 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 |
AlgL is a vital part of the alginate transport scaffold, as well as having a role in degrading alginate as a lyase |
| 4.2.2.3 | more |
AlgL is an alginate lyase that can degrade newly formed alginate polymers. Mutants of strain FRD1 defective in one of several periplasmic proteins, AlgKGX, for alginate secretion release alginate fragments due to the activity of an alginate lyase in the periplasm, which cleaves the newly formed polymers, overview. AlgK, AlgG, AlgX and AlgL may form a periplasmic scaffold to bring newly synthesized polymers to the outer-membrane porin, AlgE, and protect the polymer from degradation by AlgL |
| 4.2.2.3 | alginate |
AlgL plays a main role in alginate depolymerization |
| 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 | alginate |
Atu3025 is an exotype alginate lyase potentially involved in the assimilation of low-molecular-weight alginate in strain C58 |
