EC Number |
Natural Substrates |
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4.2.2.3 | more |
preferably degrades poly(M)-rich substrate producing unsaturated tri- and disaccharides and rapidly decreases the viscosity of sodium alginate solution in the initial phase of degradation |
4.2.2.3 | alginate |
the alginate oligomers prepared by the lyase show growth-promoting activity on the roots of banana plantlets (Streptomyces sp. A5 is isolated from banana rhizosphere) |
4.2.2.3 | more |
the alginate-degrading protein AlgL transports the growing alginate polymer chain through the periplasm |
4.2.2.3 | alginate |
the bacterial alginate is degraded towards the end of cell culture by the wild-type strain ATCC 9046 in industrial alginate production |
4.2.2.3 | alginate |
the bifunctional alginate lyase shows substrate specificity for poly(alpha-L-guluronate) and poly(beta-D-mannuronate) units in alginate molecules, cf. EC 4.2.2.11 |
4.2.2.3 | alginate |
the biological function of AlgL to degrade alginates that fail to become exported out of the cell and thereby become stranded in the periplasmic space. At high levels of alginate synthesis in the absence of AlgL, such stranded polymers may accumulate in the periplasm to such an extent that the integrity of the cell is lost, leading to toxic effects |
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 | alginate |
the enzyme is involved in alginate production |