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EC Number
Natural Substrates
Commentary (Nat. Sub.)
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the alginate-degrading protein AlgL transports the growing alginate polymer chain through the periplasm
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AlgL is a vital part of the alginate transport scaffold, as well as having a role in degrading alginate as a lyase
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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
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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
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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
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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
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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
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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
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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
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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
<< < Results 21 - 30 of 39 > >>