4.2.2.3 acetyl-beta1,4-D-mannuronic acid - 4.2.2.3 alginate incorporated into cells, substrate of alginate lyase isozymes A1-I, A1-II, and A1-III 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 Atu3025 is an exotype alginate lyase potentially involved in the assimilation of low-molecular-weight alginate in strain C58 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 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 a heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid 4.2.2.3 alginate a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid 4.2.2.3 alginate AlgL plays a main role in alginate depolymerization 4.2.2.3 alginate increased expression of alginate lyase in mucoid strain 8830 leads to alginate degradation and increased cell detachment. When expressed from a regulated promoter, the alginate lyase can induce enhanced sloughing of cells because of degradation of the alginate. Possible role for lyase in the development of bacterial growth films 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 alginate the enzyme is involved in alginate production 4.2.2.3 disaccharides of alginate oligoalginate lyase, complete depolymerization of alginate 4.2.2.3 additional information - 4.2.2.3 additional information induced by native alginate 4.2.2.3 additional information biological function of the enzyme 4.2.2.3 additional information biological function of the enzyme, Pseudomonas aeruginosa produces a bacterial alginate which seems to be necessary for cell attachment to the capsule-like biofilm build in lung of infected humans suffering cystic fibrosis 4.2.2.3 additional information A1-1V' has no significant role in alginate metabolism 4.2.2.3 additional information activity of AlgL is required for alginate production 4.2.2.3 additional information 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 additional information the alginate-degrading protein AlgL transports the growing alginate polymer chain through the periplasm 4.2.2.3 additional information 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 additional information 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 additional information AkAly28 hardly degrades oligosaccharides smaller than tetrasaccharide, while AkAly33 degrades oligosaccharides larger than disaccharide producing disaccharide and 2-keto-3-deoxy-gluconaldehyde, substrate specificities, production of oligosaccharides, analysis by anion-exchange chromatography, overview 4.2.2.3 additional information alginate is a linear hetero-polyuronic acid composed of 1,4 linked alpha-L-guluronic acid (G) and beta-D-mannuronic acid. Alginate lyase aly-SJ02 is bifunctional. Aly-SJ02 shows activities toward both polyG (alpha-L-guluronic acid), activity of EC 4.2.2.11, and polyM (beta-D-mannuronic acid). Aly-SJ02 mainly releases dimers and trimers from polyM and alginate, and trimers and tetramers from polyG 4.2.2.3 additional information alginate lyase A degrades M and G blocks, and the enzyme activity acting on M block is much more than that of G block, while for alginate lyase B, the enzyme activities on M block are slightly higher than that of G block 4.2.2.3 additional information 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 additional information enzymatic depolymerization of sodium alginate, the enzyme shows specificity for cleaving at the beta-1,4 glycosidic bond between polyM and polyG blocks of sodium alginate 4.2.2.3 additional information preferably degrades poly(M)-rich substrate and rapidly decreases the viscosity of sodium alginate solution in the initial phase of degradation. Aly33 degrades poly(M)-rich substrate into various sizes of oligosaccharides in the reaction time up to 1 h and further degrades the thus formed oligosaccharides to disaccharide and monosaccharide such as alpha-keto acid in the reaction time 2-6 h 4.2.2.3 additional information 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 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