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4-deoxy-L-erythro-hex-4-ene-pyranosyluronate-(mannuronate)2-mannuronic acid
?
bound in the active cleft at subsites -3 to +1, the glycosidic linkage is cleaved existed between subsites -1 and +1
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acetyl-beta1,4-D-mannuronic acid
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Azotobacter phage A22
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acetylated alginate
acetylated algino-oligosaccharides
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acetylated poly-beta1,4-D-mannuronic acid
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endolytic activity
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alginate
algino-monosaccharides + algino-disaccharides
alginate
oligosaccharides of 4-7 monomers
substrate from brown algae Macrocystis pyrifera rich in polymannuronate and polyguluronate, cleavage sequences are G-/-MM and/or G-/-GM
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alginate
unsaturated alginate disaccharides + unsaturated alginate trisaccharides
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main products
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alginate
unsaturated algino-monosaccharides
ATU3025 acts on alginate polysaccharides and oligosaccharides exolytically and releases unsaturated monosaccharides from the substrate terminal
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alginate
unsaturated algino-oligosaccharides
alpha-L-mannuronyl linkage in alginate
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beta-D-mannuronyl linkage in alginate
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deacetylated polymannuronic acid
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disaccharides of alginate
monosaccharides of alginate
G-alginate
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purified alpha-L-guluronic acid blocks containing more than 90% alpha-L-guluronic acid
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hepta-alpha1,4-L-guluronate
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
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-
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hepta-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
hepta-beta1,4-D-mannuronic acid
D-mannuronic acid
hexa-alpha1,4-L-guluronate
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
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hexa-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
hexa-beta1,4-D-mannuronic acid
D-mannuronic acid
M-alginate
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pure 1-4-linked beta-D-mannuronic acid
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MG-alginate
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alginate epimerized by AlgE4 and containing 47% alpha-L-guluronic acid with no alpha-L-guluronic acid blocks, 100% activity
isoforms AlyA1, AlyA2, and AlyA3 produce mainly DELTAG and DELTAGMG as their end products, isoform AlyA3 produces as many trimers as it does dimers and tetramers
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nona-alpha1,4-L-guluronate
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
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nona-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
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?
nona-beta1,4-D-mannuronic acid
D-mannuronic acid
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?
octa-alpha1,4-L-guluronate
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
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octa-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
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octa-beta1,4-D-mannuronate
D-mannuronic acid
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?
octa-beta1,4-D-mannuronic acid
D-mannuronic acid
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octa-beta1,4-D-mannuronic acid
D-mannuronic acid + ?
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penta-alpha1,4-L-guluronate
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
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?
penta-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
penta-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
poly alpha-L-guluronate
oligo-alpha-1,4-L-guluronate
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poly beta-D-mannuronate
oligo-beta-1,4-D-mannuronate
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?
poly(alpha-(1,4)-L-guluronate)
4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
poly(alpha-(1,4)-L-guluronate)
4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1->4)-alpha-oligo(alpha-(1->4)-L-guluronate)
reaction of EC 4.2.2.11, about 15% of the activity with poly(beta-(1,4)-D-mannuronate)
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poly(alpha-(1,4)-L-guluronic acid)
4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
poly(alpha-1,4-L-guluronate)
4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
poly(alpha-1,4-L-guluronate)
4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1->4)-alpha-oligo(alpha-(1->4)-L-guluronate)
about 5% of the activity with poly(beta-1,4-D-mannuronate), reaction of EC 4.2.2.11
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poly(alpha-L-(1,4)-guluronate)
4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
reaction of EC 4.2.2.11
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poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1->4)-beta-oligo(beta-(1->4)-D-mannuronate)
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poly(beta-(1,4)-D-mannuronate/alpha-(1,4)-L-guluronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate) + 4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
poly(beta-(1,4)-D-mannuronic acid)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
poly(beta-(1->4)-D-mannuronate)
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poly(beta-(1->4)-D-mannuronate)
an unsaturated mannuronate disaccharide
530% of the activity with alginate
enzyme acts as an exolytic lyase, releasing unsaturated disaccharide directly from the poly(M)-rich substrate. It splits the second glycosyl linkage from the reducing terminus of the trisaccharide, the resulting disaccharide is not further degraded
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poly(beta-(1->4)-D-mannuronic acid)
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poly(beta-(1->4)-D-mannuronic acid/alpha-(1->4)-L-guluronic acid)
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poly(beta-(1->4)-D-mannuronic acid/alpha-L-guluronic acid)
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poly(beta-1,4-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
poly(beta-1,4-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1->4)-beta-oligo(beta-(1->4)-D-mannuronate)
prefered substrate
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?
poly(beta-1,4-D-mannuronate/alpha-1,4-L-guluronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate) + 4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
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about 30% of the activity with poly(alpha-1,4-L-guluronate)
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poly(beta-1,4-D-mannuronate/alpha-1,4-L-guluronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1->4)-beta-oligo(beta-(1->4)-D-mannuronate) + 4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1->4)-alpha-oligo(alpha-(1->4)-L-guluronate)
about 30% of the activity with poly(beta-1,4-D-mannuronate)
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?
poly(beta-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
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?
poly(beta-D-mannuronate)
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poly(beta-D-manuronate)
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poly-acetyl-beta1,4-D-mannuronic acid
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poly-alpha-L-guluronate
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14.9% of the activity with poly-beta-D-mannuronate
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poly-alpha-L-guluronic acid
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poly-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
poly-alpha1,4-L-guluronic acid
?
poly-alpha1,4-L-guluronic acid
alpha-D-glucuronate + ?
poly-beta-1,4-D-mannuronate
4-deoxy-L-erythro-hex-4-enepyranosyluronate-mannuronate-mannuronic acid
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?
poly-beta-D-mannuronate
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poly-beta-D-mannuronate
oligomannuronate
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i.e. alginate, cleavage site structure
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poly-beta1,4-D-mannuronate
beta-D-mannuronate
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
poly-beta1,4-D-mannuronic acid
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polyguluronan
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70% of the activity with polymannuronan
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polymannuronan
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polymannuronate
4,5-unsaturated oligomannuronic acids
polymannuronide
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tetra-alpha1,4-L-guluronate
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
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?
tetra-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
tetra-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-D-mannuronoyl-beta-1,4-D-mannuranote + D-mannuronate
trisaccharides of alginate
monosaccharides of alginate
additional information
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alginate
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preferably degrades M blocks
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alginate
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preferably degrades M blocks
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alginate
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Atu3025 is an exotype alginate lyase potentially involved in the assimilation of low-molecular-weight alginate in strain C58
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alginate
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Atu3025 is an exotype family PL-15 alginate lyase
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alginate
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Atu3025 is an exotype alginate lyase potentially involved in the assimilation of low-molecular-weight alginate in strain C58
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alginate
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Atu3025 is an exotype family PL-15 alginate lyase
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alginate
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highest activity toward poly(M)-rich substrate, moderate activity toward sodium alginate and weak activity toward poly(MG)-rich substrate, no activity toward poly (G)-rich substrate
major reaction products are tri- and disaccharide along with various sizes of intermediary oligosaccharides
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alginate
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specific for cleaving at the beta-1,4 glycosidic bond between polyM and polyG blocks of sodium alginate, producing homopolymeric blocks of polyM and polyG. Enzyme is inefficient in the degradation of polyM and polyG
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alginate
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a heteropolysaccharides of alpha-L-guluronate and beta-D-mannuronate
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alginate
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the bacterial alginate is degraded towards the end of cell culture by the wild-type strain ATCC 9046 in industrial alginate production
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alginate
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HdAlex can degrade not only unsaturated trisaccharide but also alginate and mannuronate-rich polymers. HdAlex degrades the alginate polymer in an exolytic manner
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alginate
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AB489222
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
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alginate
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AB489222
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
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alginate
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AlgL lacks of stereospecificity, in that it is able to catalyze cleavage adjacent to either mannuronate or guluronate residues in alginate. The enzyme is able to remove the C5 proton from both mannuronate and guluronate, which are C5 epimers. Exhaustive digestion of alginate by AlgL generates dimeric and trimeric products, analysis by 1H NMR spectroscopy and mass spectrometry. AlgL operates as an exopolysaccharide lyase
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alginate
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can degrade alginate and mannuronate blocks, but hardly degrades guluronate blocks. In particular, AlgL can degrade acetylated alginate of Pseudomonas aeruginosa FRD1
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alginate
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can degrade alginate and mannuronate blocks, but hardly degrades guluronate blocks. In particular, AlgL can degrade acetylated alginate of Pseudomonas aeruginosa FRD1
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alginate
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the enzyme endolytically depolymerizes alginate by beta-elimination into oligo-alginates with degrees of polymerization of 2-5
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alginate
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recombinant and native wild-type enzymes show similar activity levels
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alginate
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substrate of alginate lyase isozymes A1-I, A1-II, and A1-III
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alginate
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incorporated into cells, substrate of alginate lyase isozymes A1-I, A1-II, and A1-III
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alginate
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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)
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alginate
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substrate specificity for polyguluronate units in the alginate molecules
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alginate
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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)
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alginate
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substrate specificity for polyguluronate units in the alginate molecules
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alginate
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the alginate lyase has the specificity for poly G block
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alginate
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the enzyme is specific for hydrolyzing poly-beta-D-1,4-mannuronate in alginate
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alginate
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the enzyme is specific for hydrolyzing poly-beta-D-1,4-mannuronate in alginate
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alginate
algino-monosaccharides + algino-disaccharides
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alginate
algino-monosaccharides + algino-disaccharides
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alginate
algino-monosaccharides + algino-disaccharides
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alginate
oligouronides
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alginate
oligouronides
alginate rich in mannuronic acids, the enzyme cleaves beta-D-mannuronic acid-beta-D-mannuronic acid bonds and beta-D-mannuronic acid-alpha-L-guluronic acid bonds but not alpha-L-guluronic acid-beta-D-mannuronic acid bonds and alpha-L-guluronic acid-alpha-L-guluronic acid-bonds
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alginate
oligouronides
isoform AlgE7 degrades M-rich alginates and a relatively G-rich alginate from the brown algae Macrocystis pyrifera most effectively, producing oligomers of 4 (mannuronan) to 7 units. The sequences cleaved are mainly G-MM and/or G-GM. G-moieties dominate at the reducing ends even when mannuronan is used as substrate, so the AlgE7 lyase/epimerase probably stimulates the lyase pathway, indicating a complex interplay between the two activities
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alginate
oligouronides
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a series of oligouronides each containing a terminal 4-deoxy-alpha-L-erythrohex-4-enopyranuronosyl residue
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alginate
oligouronides
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alginate
oligouronides
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alginate
oligouronides
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mannuronic acid-rich alginate, the degree of degradation of alginate is roughly proportional to the mannuronic acid content
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alginate
oligouronides
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degradation of a greater percentage of the mannuronic acid-rich fractions than of glucuronic acid-rich fractions or the original alginate
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alginate
oligouronides
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degradation of a greater percentage of the mannuronic acid-rich fractions than of glucuronic acid-rich fractions or the original alginate
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alginate
oligouronides
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splits glycosidic bonds only between two mannuronic acid residues
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alginate
oligouronides
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preferential splitting of the glycosidic bond between two mannuronide residues in the alginic acid
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alginate
oligouronides
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high affinity towards mannuronate-rich domains
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alginate
oligouronides
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mannuronate blocks in alginate
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alginate
oligouronides
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alginate
oligouronides
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mannuronate blocks in alginate
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alginate
oligouronides
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attacks preferentially mannuronate-rich moieties of the alginate molecule
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alginate
oligouronides
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high affinity towards mannuronate-rich domains
unsaturated oligomers mostly composed of mannuronic acid as final product
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alginate
oligouronides
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cleavage of mannuronate blocks in exo manner, 11fold preference for mannuronate blocks over guluronate blocks
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alginate
oligouronides
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high-molecular weight alginate
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alginate
oligouronides
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1,4-beta-D-mannuronan block regions of alginate
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alginate
oligouronides
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dimeric through hexameric uronides possessing DELTA-4,5-unsaturated nonreducing terminal residues
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alginate
unsaturated algino-oligosaccharides
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alginate
unsaturated algino-oligosaccharides
the enzyme degrades alginate by endo fashion, the enzyme degrades favorably mannuronate-guluronate and guluronate-rich fragments in alginate, shows substrate specificity toward beta-D-mannuronic acid blocks of hydrolysed alginate
4-deoxy-L-erythro-hex-4-enopyranosyluronic acids as the non-reducing terminal moiety are contained in the products
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alginate
unsaturated algino-oligosaccharides
the enzyme degrades alginate by endo fashion, the enzyme degrades favorably mannuronate-guluronate and guluronate-rich fragments in alginate, shows substrate specificity toward beta-D-mannuronic acid blocks of hydrolysed alginate
4-deoxy-L-erythro-hex-4-enopyranosyluronic acids as the non-reducing terminal moiety are contained in the products
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alginate
unsaturated algino-oligosaccharides
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alginate
unsaturated algino-oligosaccharides
Alginovibrio aquatilis
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endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
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alginate
unsaturated algino-oligosaccharides
Alginovibrio aquatilis
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a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
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alginate
unsaturated algino-oligosaccharides
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a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
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alginate
unsaturated algino-oligosaccharides
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a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
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alginate
unsaturated algino-oligosaccharides
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alginate
unsaturated algino-oligosaccharides
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a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
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alginate
unsaturated algino-oligosaccharides
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a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
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alginate
unsaturated algino-oligosaccharides
endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
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?
alginate
unsaturated algino-oligosaccharides
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
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?
alginate
unsaturated algino-oligosaccharides
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a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
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?
alginate
unsaturated algino-oligosaccharides
Azotobacter phage A31
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a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
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?
alginate
unsaturated algino-oligosaccharides
Azotobacter phage A31
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a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
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alginate
unsaturated algino-oligosaccharides
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alginate
unsaturated algino-oligosaccharides
a complex heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
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alginate
unsaturated algino-oligosaccharides
a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
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alginate
unsaturated algino-oligosaccharides
a heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
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alginate
unsaturated algino-oligosaccharides
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
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?
alginate
unsaturated algino-oligosaccharides
enzyme cleaves beta-D-mannuronic acid-beta-D-mannuronic acid and beta-D-mannuronic acid-alpha-L-guluronic acid bonds but not alpha-L-guluronic acid-alpha-L-guluronic acid or alpha-L-guluronic acid-beta-D-mannuronic acid bonds
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alginate
unsaturated algino-oligosaccharides
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isoforms AlyA1, AlyA2, and AlyA3 preferably cleave the bond between guluronic acid and mannuronic acid, resulting in a guluronic acid residue at the new reducing end, but isoform AlyA3 also degrades the other three possible bonds in alginate
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alginate
unsaturated algino-oligosaccharides
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endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
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?
alginate
unsaturated algino-oligosaccharides
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a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
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?
alginate
unsaturated algino-oligosaccharides
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endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
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?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
?
alginate
unsaturated algino-oligosaccharides
a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
weak activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
Dollabella auricola
-
endolytic activity, preference for M-M linkages, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
Dollabella auricola
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
?
alginate
unsaturated algino-oligosaccharides
-
when alginate is added at an initial concentration of more than 0.8%, the maximal degradation rate of alginate is obtained
-
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
?
alginate
unsaturated algino-oligosaccharides
Fucus spp.
-
a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
Fucus spp.
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
-
?
alginate
unsaturated algino-oligosaccharides
-
endolytic activity, a complex heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
?
alginate
unsaturated algino-oligosaccharides
-
recombinant Aly has the capacity to degrade alginate components for protoplast isolation
-
-
?
alginate
unsaturated algino-oligosaccharides
-
the enzyme preferably degrades poly-beta-D-mannuronic acid-rich substrate, is also able to degrade poly-beta-D-mannuronic acid/poly-alpha-L-guluronic acid block but hardly poly-alpha-L-guluronic acid block
-
-
?
alginate
unsaturated algino-oligosaccharides
-
the enzyme preferably degrades poly-beta-D-mannuronic acid-rich substrate, is also able to degrade poly-beta-D-mannuronic acid/poly-alpha-L-guluronic acid block but hardly poly-alpha-L-guluronic acid block
-
-
?
alginate
unsaturated algino-oligosaccharides
-
endolyticc activity, enzyme prefers to cleave G-M and M-M linkages, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
Ishige sp.
-
a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
Ishige sp.
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
?
alginate
unsaturated algino-oligosaccharides
-
endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
the enzyme preferably degrades poly-beta-D-mannuronic acid-rich substrate, is also able to degrade poly-beta-D-mannuronic acid/poly-alpha-L-guluronic acid block but hardly poly-alpha-L-guluronic acid block
-
-
?
alginate
unsaturated algino-oligosaccharides
-
endolytic activity, preference for M-M linkages, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
-
?
alginate
unsaturated algino-oligosaccharides
-
endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
about 30% of the activity with poly(beta-1,4-D-mannuronate)
-
-
?
alginate
unsaturated algino-oligosaccharides
-
the enzyme preferably degrades poly-beta-D-mannuronic acid-rich substrate, is also able to degrade poly-beta-D-mannuronic acid/poly-alpha-L-guluronic acid block but hardly poly-alpha-L-guluronic acid block
-
-
?
alginate
unsaturated algino-oligosaccharides
-
a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
endolytic activity, a complex heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
weak activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
best substrate
-
-
?
alginate
unsaturated algino-oligosaccharides
endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
the substrates is depolymerized mainly into the dimer to tetramer forms
-
-
?
alginate
unsaturated algino-oligosaccharides
-
the substrates is depolymerized mainly into the dimer to tetramer forms
-
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
-
?
alginate
unsaturated algino-oligosaccharides
endolytic activity, intracellular isozymes also show hydrolase activity on alginate, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
-
?
alginate
unsaturated algino-oligosaccharides
-
endolytic activity, a complex heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
AlgL plays a main role in alginate depolymerization
-
-
?
alginate
unsaturated algino-oligosaccharides
-
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
-
-
?
alginate
unsaturated algino-oligosaccharides
-
the enzyme is involved in alginate production
-
-
?
alginate
unsaturated algino-oligosaccharides
-
protein PA1167 acts preferably on heteropolymeric regions endolytically
-
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
-
?
alginate
unsaturated algino-oligosaccharides
-
AlgL plays a main role in alginate depolymerization
-
-
?
alginate
unsaturated algino-oligosaccharides
-
protein PA1167 acts preferably on heteropolymeric regions endolytically
-
-
?
alginate
unsaturated algino-oligosaccharides
-
endolytic activity, a complex heteropolymer consisiting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
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
-
-
?
alginate
unsaturated algino-oligosaccharides
-
endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
?
alginate
unsaturated algino-oligosaccharides
-
a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
-
?
alginate
unsaturated algino-oligosaccharides
-
about 50% of the activity with poly(alpha-1,4-L-guluronate)
-
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
-
?
alginate
unsaturated algino-oligosaccharides
-
endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
isozyme A1-II and A1-I: endolytic cleavage of the glycosidic bonds, beta-elimination reaction, A1-II shows a preference for polyguluronate instead of polymannuronate
A1-I produces mainly di- and trisaccharides, A1-II produces mainly tri- and tetrasaccharides
?
alginate
unsaturated algino-oligosaccharides
-
isozyme A1-II performs endolytic cleavage of the glycosidic bonds, beta-elimination reaction, and shows a preference for polyguluronate instead of polymannuronate
isozyme A1-II produces mainly tri- and tetrasaccharides
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
Arg146, Gln189, His191, and Tyr284 form an active center
-
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
?
alginate
unsaturated algino-oligosaccharides
-
endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
enzyme lyase appears to be poly-guluronate lyase degrading poly-G block preferentially than poly-M block. The degraded products are determined to be di-, tri-, tetra- and pentasaccharides
-
-
?
alginate
unsaturated algino-oligosaccharides
-
enzyme prefers to cleave M-M linkages, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
endolytic activity, a complex heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid, depolymerization, substrate structure, overview
-
?
alginate
unsaturated algino-oligosaccharides
-
a heteropolymer consisting of beta1,4-D-mannuronic acid and alpha1,4-L-guluronic acid
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
?
alginate
unsaturated algino-oligosaccharides
-
-
di-, tri-, tetra-, and pentasaccharide fragments
-
?
alginate
unsaturated algino-oligosaccharides
isoform A9mT favorably degrades mannuronate polymer in alginate, the relative activities for alginate, beta-D-mannuronic acid, 1,4 linked alpha-L-guluronic acid, and 1,4 linked alpha-L-guluronic acid/beta-D-mannuronic acid blocks are 100%, 75%, 21%, and 15%, respectively, under the standard assay conditions at pH 7.5
-
-
?
alginate
unsaturated algino-oligosaccharides
-
-
di-, tri-, tetra-, and pentasaccharide fragments
-
?
alginate
unsaturated algino-oligosaccharides
isoform A9mT favorably degrades mannuronate polymer in alginate, the relative activities for alginate, beta-D-mannuronic acid, 1,4 linked alpha-L-guluronic acid, and 1,4 linked alpha-L-guluronic acid/beta-D-mannuronic acid blocks are 100%, 75%, 21%, and 15%, respectively, under the standard assay conditions at pH 7.5
-
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
?
alginate
unsaturated algino-oligosaccharides
-
-
-
?
alpha-L-mannuronyl linkage in alginate
?
-
-
-
-
?
alpha-L-mannuronyl linkage in alginate
?
-
-
enzyme shows activities toward both polyG, i.e.alpha-L-guluronic acid, and polyM, i.e. beta-D-mannuronic acid
-
?
alpha-L-mannuronyl linkage in alginate
?
-
alginate lyases A and B have the activities for both M and G blocks. For isoform A, the enzyme activity acting on M block is much more than that of G block, for alginate lyase B, the enzyme activity on M block is slightly higher than that on G block and there is no obvious substrate specificity difference between them
-
-
?
alpha-L-mannuronyl linkage in alginate
?
-
alginate lyases A and B have the activities for both M and G blocks. For isoform A, the enzyme activity acting on M block is much more than that of G block, for alginate lyase B, the enzyme activity on M block is slightly higher than that on G block and there is no obvious substrate specificity difference between them
-
-
?
alpha-L-mannuronyl linkage in alginate
?
-
-
products are six different di-and trisaccharides. The enzymatic hydrolysis occurs between two random guluronic acid or/and mannuronic acid residues, and produces one G residue or M residue on the reducing end and an unsaturated residue on the non-reducing end for all products
-
?
alpha-L-mannuronyl linkage in alginate
?
-
-
products are six different di-and trisaccharides. The enzymatic hydrolysis occurs between two random guluronic acid or/and mannuronic acid residues, and produces one G residue or M residue on the reducing end and an unsaturated residue on the non-reducing end for all products
-
?
beta-D-mannuronyl linkage in alginate
?
-
final degradation products are alginate monosaccharides
-
?
beta-D-mannuronyl linkage in alginate
?
-
final degradation products are alginate monosaccharides
-
?
beta-D-mannuronyl linkage in alginate
?
preferably degrades the M block over the G block in alginate
-
-
?
beta-D-mannuronyl linkage in alginate
?
preferably degrades the M block over the G block in alginate
-
-
?
disaccharides of alginate
monosaccharides of alginate
-
oligoalginate lyase
-
?
disaccharides of alginate
monosaccharides of alginate
-
oligoalginate lyase, complete depolymerization of alginate
-
?
hepta-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
-
-
-
?
hepta-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
-
-
-
?
hepta-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
-
-
-
?
hepta-beta1,4-D-mannuronic acid
D-mannuronic acid
-
-
-
?
hepta-beta1,4-D-mannuronic acid
D-mannuronic acid
-
-
-
?
hexa-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
-
-
-
?
hexa-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
-
-
-
?
hexa-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
-
-
-
?
hexa-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
-
-
-
?
hexa-beta1,4-D-mannuronic acid
D-mannuronic acid
-
-
-
?
hexa-beta1,4-D-mannuronic acid
D-mannuronic acid
-
-
-
?
oligomannuronate
?
-
hexameric oligomannuronate is the preferred substrate, pentameric oligomannuronates are still accepted, no activity with oligomers shorter than pentamer
-
-
?
oligomannuronate
?
-
hexameric oligomannuronate is the preferred substrate, pentameric oligomannuronates are still accepted, no activity with oligomers shorter than pentamer
-
-
?
penta-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
-
-
-
?
penta-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
-
-
-
?
penta-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
-
-
-
?
penta-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
-
-
-
?
penta-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
-
-
?
penta-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
-
-
?
poly(alpha-(1,4)-L-guluronate)
4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
reaction of EC 4.2.2.11
-
-
?
poly(alpha-(1,4)-L-guluronate)
4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
-
reaction of EC 4.2.2.11
-
-
?
poly(alpha-(1,4)-L-guluronate)
4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
reaction of EC 4.2.2.11
-
-
?
poly(alpha-(1,4)-L-guluronate)
4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
reaction of EC 4.2.2.11, about 15% of the activity with poly(beta-(1,4)-D-mannuronate)
-
-
?
poly(alpha-(1,4)-L-guluronate)
4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
-
-
-
?
poly(alpha-(1,4)-L-guluronate)
4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
reaction of EC 4.2.2.11
-
-
?
poly(alpha-(1,4)-L-guluronate)
4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
reaction of EC 4.2.2.11
-
-
?
poly(alpha-(1,4)-L-guluronate)
4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
reaction of EC 4.2.2.11
-
-
?
poly(alpha-(1,4)-L-guluronate)
4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
reaction of EC 4.2.2.11
-
-
?
poly(alpha-(1,4)-L-guluronate)
4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
reaction of EC 4.2.2.11
-
-
?
poly(alpha-(1,4)-L-guluronic acid)
4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
reaction of EC 4.2.2.11
-
-
?
poly(alpha-(1,4)-L-guluronic acid)
4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
reaction of EC 4.2.2.11
-
-
?
poly(alpha-1,4-L-guluronate)
4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
reaction of EC 4.2.2.11
-
-
?
poly(alpha-1,4-L-guluronate)
4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
-
reaction of EC 4.2.2.11
-
-
?
poly(alpha-1,4-L-guluronate)
4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
-
reaction of EC 4.2.2.11, about 60% of the activity with alginate
-
-
?
poly(alpha-1,4-L-guluronate)
4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
-
reaction of EC 4.2.2.11
-
-
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
-
-
-
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
-
-
-
-
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
-
-
-
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
-
-
-
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
-
-
-
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
-
-
-
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
-
-
-
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
-
-
-
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
-
-
-
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
-
-
-
?
poly(beta-(1,4)-D-mannuronate/alpha-(1,4)-L-guluronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate) + 4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
-
-
-
?
poly(beta-(1,4)-D-mannuronate/alpha-(1,4)-L-guluronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate) + 4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
-
-
-
-
?
poly(beta-(1,4)-D-mannuronate/alpha-(1,4)-L-guluronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate) + 4-O-(4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl)-(1,4)-alpha-oligo(alpha-(1,4)-L-guluronate)
-
-
-
?
poly(beta-(1,4)-D-mannuronic acid)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
-
-
-
?
poly(beta-(1,4)-D-mannuronic acid)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
-
-
-
?
poly(beta-(1->4)-D-mannuronate)
?
-
-
-
-
?
poly(beta-(1->4)-D-mannuronate)
?
-
-
-
-
?
poly(beta-(1->4)-D-mannuronate)
?
-
-
-
-
?
poly(beta-(1->4)-D-mannuronic acid)
?
190% of the activity with alginate
-
-
?
poly(beta-(1->4)-D-mannuronic acid)
?
190% of the activity with alginate
-
-
?
poly(beta-(1->4)-D-mannuronic acid/alpha-(1->4)-L-guluronic acid)
?
45% of the activity with alginate
-
-
?
poly(beta-(1->4)-D-mannuronic acid/alpha-(1->4)-L-guluronic acid)
?
alternating structure of alpha-L-guluronic acid and beta-D-mannuronic acid. 120% of the activity with alginate
-
-
?
poly(beta-(1->4)-D-mannuronic acid/alpha-(1->4)-L-guluronic acid)
?
alternating structure of alpha-L-guluronic acid and beta-D-mannuronic acid. 120% of the activity with alginate
-
-
?
poly(beta-(1->4)-D-mannuronic acid/alpha-L-guluronic acid)
?
-
alternating structure of alpha-L-guluronic acid and beta-D-mannuronic acid. In wild-type, ratio of activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) to poly(alpha-L-guluronic acid) is 1.2
-
-
?
poly(beta-(1->4)-D-mannuronic acid/alpha-L-guluronic acid)
?
-
alternating structure of alpha-L-guluronic acid and beta-D-mannuronic acid. In wild-type, ratio of activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) to poly(alpha-L-guluronic acid) is 1.2
-
-
?
poly(beta-1,4-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
-
-
-
?
poly(beta-1,4-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
-
-
-
?
poly(beta-1,4-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
-
about 50% of the activity with poly(alpha-1,4-L-guluronate) or alginate
-
-
?
poly(beta-1,4-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
-
about 30% of the activity with alginate
-
-
?
poly(beta-1,4-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
-
about 20% of the activity with poly(alpha-1,4-L-guluronate)
-
-
?
poly(beta-D-mannuronate)
?
-
-
-
?
poly(beta-D-mannuronate)
?
-
-
-
?
poly(beta-D-mannuronate)
?
AB489222
-
-
-
?
poly(beta-D-mannuronate)
?
AB489222
-
-
-
?
poly(beta-D-mannuronate)
?
the region including T121 of LbAly28 is the recognition of poly(MG) region of alginate
-
-
?
poly(beta-D-mannuronate)
?
-
-
-
-
?
poly(beta-D-mannuronate)
?
-
about 30% activity compared to alginate
-
-
?
poly(beta-D-mannuronate)
?
-
about 30% activity compared to alginate
-
-
?
poly(beta-D-manuronate)
?
AlyDW11 prefers poly(beta-D-mannuronate) as a substrate over poly(alpha-L-guluronate)
-
-
?
poly(beta-D-manuronate)
?
-
-
-
?
poly(beta-D-manuronate)
?
-
-
-
?
poly-acetyl-beta1,4-D-mannuronic acid
?
Azotobacter phage A31
-
-
-
?
poly-acetyl-beta1,4-D-mannuronic acid
?
-
-
?
poly-acetyl-beta1,4-D-mannuronic acid
?
-
-
-
?
poly-acetyl-beta1,4-D-mannuronic acid
?
-
-
-
?
poly-acetyl-beta1,4-D-mannuronic acid
?
-
-
-
?
poly-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
-
-
?
poly-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
-
-
-
?
poly-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
-
-
-
?
poly-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
-
-
-
?
poly-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
-
-
-
?
poly-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
-
-
-
?
poly-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
Ishige sp.
-
-
-
?
poly-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
-
weak activity in strain 1351
-
?
poly-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
-
heteropolymers and homopolymers, bifunctional enzyme AAlyase, preference for
-
?
poly-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
-
heteropolymers and homopolymers, bifunctional enzyme AAlyase, preference for
-
?
poly-alpha1,4-L-guluronic acid
?
-
competitive to poly-beta1,4-D-mannuronic acid
-
?
poly-alpha1,4-L-guluronic acid
?
endolytic activity, extra- and intracellular isozymes
-
?
poly-alpha1,4-L-guluronic acid
alpha-D-glucuronate + ?
-
-
-
?
poly-alpha1,4-L-guluronic acid
alpha-D-glucuronate + ?
-
-
-
?
poly-beta-D-mannuronate
?
-
-
-
?
poly-beta-D-mannuronate
?
-
poly-beta-D-mannuronate can be much more easily hydrolyzed by the displayed alginate lyase than poly-alpha-L-guluronic acid and sodium alginate
-
-
?
poly-beta1,4-D-mannuronate
beta-D-mannuronate
-
the substrates is depolymerized mainly into the dimer to tetramer forms
-
-
?
poly-beta1,4-D-mannuronate
beta-D-mannuronate
-
the substrates is depolymerized mainly into the dimer to tetramer forms
-
-
?
poly-beta1,4-D-mannuronate
beta-D-mannuronate
-
-
-
?
poly-beta1,4-D-mannuronate
beta-D-mannuronate
-
-
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
-
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
endolytic activity
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
deacetylated
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
deacetylated
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
weak activity
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
-
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
-
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
Dollabella auricola
-
preference for M-M linkages
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
-
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
-
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
-
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
-
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
Ishige sp.
-
-
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
low activity
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
preference for M-M linkages
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
strain JBH2: deacetylated
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
strain JBH2: deacetylated
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
-
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
weak activity
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
heteropolymers and homopolymers, bifunctional enzyme AAlyase
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
heteropolymers and homopolymers, bifunctional enzyme AAlyase
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
nonacetylated
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
nonacetylated
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
-
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
-
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
-
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
-
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
-
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
-
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
-
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
-
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
endolytic activity
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
-
-
?
poly-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-oligo-D-mannuronate + D-mannuronate
-
-
-
?
poly-beta1,4-D-mannuronic acid
?
-
competitive to poly-alpha1,4L-guluronic acid
-
?
poly-beta1,4-D-mannuronic acid
?
endolytic activity, extra- and intracellular isozymes
-
?
polymannuronate
4,5-unsaturated oligomannuronic acids
-
-
-
-
?
polymannuronate
4,5-unsaturated oligomannuronic acids
-
-
-
-
?
polymannuronate
4,5-unsaturated oligomannuronic acids
-
-
production of a wide range of 4,5-unsaturated oligomannuronic acids, that are further degraded to unsaturated monomer and dimer as final products
?
polymannuronate
4,5-unsaturated oligomannuronic acids
-
-
-
-
?
polymannuronate
4,5-unsaturated oligomannuronic acids
-
-
-
-
?
sodium alginate
?
-
endo-type manner
-
?
sodium alginate
?
-
-
-
?
sodium alginate
?
profiles of alginate oligomers are obtained by digestion of alginate with an alginate lyase AlyDW11, overview. The enzyme has endolytic activity and prefers poly(beta-D-mannuronate) over poly(alpha-L-guluronate)
-
-
?
sodium alginate
?
-
-
-
?
sodium alginate
?
-
-
-
?
sodium alginate
?
brown seaweed alginate (BSWA) as model substrate or baterial alginate purified from the mucoid Pseudomonas aeruginosa clinical isolate FRD1
-
-
?
sodium alginate
?
-
high activity
-
-
?
sodium alginate
?
-
high activity
-
-
?
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
-
-
?
sodium alginate
?
LC mass and NMR spectrometris product analysis
-
-
?
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
-
-
?
sodium alginate
?
LC mass and NMR spectrometris product analysis
-
-
?
tetra-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
-
-
-
?
tetra-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
-
-
-
?
tetra-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
-
-
-
?
tetra-alpha1,4-L-guluronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-alpha-1,4-oligo-L-guluronate + L-guluronate
-
-
-
?
tetra-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-D-mannuronoyl-beta-1,4-D-mannuranote + D-mannuronate
-
-
-
?
tetra-beta1,4-D-mannuronic acid
4-deoxy-alpha-L-erythro-hex-4-enuronosyl-beta-1,4-D-mannuronoyl-beta-1,4-D-mannuranote + D-mannuronate
-
-
-
?
trisaccharides of alginate
monosaccharides of alginate
-
oligoalginate lyase
-
?
trisaccharides of alginate
monosaccharides of alginate
-
oligoalginate lyase, complete depolymerization of alginate
-
?
additional information
?
-
Alginovibrio aquatilis
-
biological function of the enzyme
-
?
additional information
?
-
-
no activity with triguluronate and trimannuronate, but with tetramers or substrates with longer chain length
-
?
additional information
?
-
-
no activity with triguluronate and trimannuronate, but with tetramers or substrates with longer chain length
-
?
additional information
?
-
-
biological function of the enzyme
-
?
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
-
-
?
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
-
-
?
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
major reaction products are tri- and disaccharide along with various sizes of intermediary oligosaccharides
-
?
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. Aly28 hardly degrades oligosaccharides smaller than tetrasaccharide
-
-
?
additional information
?
-
substrate is sodium alginate originating from Macrocystis pyrifera, preparation of poly(M)-rich, poly(G)-rich, and random substrates thereof
-
-
?
additional information
?
-
-
substrate is sodium alginate originating from Macrocystis pyrifera, preparation of poly(M)-rich, poly(G)-rich, and random substrates thereof
-
-
?
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
-
-
?
additional information
?
-
-
biological function of the enzyme
-
?
additional information
?
-
-
assay methods, overview
-
?
additional information
?
-
assay methods, overview
-
?
additional information
?
-
-
biological function of the enzyme
-
?
additional information
?
-
biological function of the enzyme
-
?
additional information
?
-
-
assay methods, overview
-
?
additional information
?
-
-
biological function of the enzyme
-
?
additional information
?
-
Azotobacter phage A22
-
biological function of the enzyme
-
?
additional information
?
-
Azotobacter phage A31
-
biological function of the enzyme
-
?
additional information
?
-
-
substrate specificity
-
?
additional information
?
-
substrate specificity
-
?
additional information
?
-
assay methods, overview, cleaves M-M and M-G linkages, but not G-GM linkages
-
?
additional information
?
-
assay methods, overview, cleaves M-M and M-G linkages, but not G-GM linkages
-
?
additional information
?
-
cleaves G-MM and G-GM linkages, but nt G-GM linkages
-
?
additional information
?
-
cleaves G-MM and G-GM linkages, but nt G-GM linkages
-
?
additional information
?
-
biological function of the enzyme
-
?
additional information
?
-
biological function of the enzyme
-
?
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
-
-
?
additional information
?
-
-
endolytic activity
-
?
additional information
?
-
-
biological function of the enzyme
-
?
additional information
?
-
-
biological function of the enzyme
-
?
additional information
?
-
-
biological function of the enzyme
-
?
additional information
?
-
assay methods, overview
-
?
additional information
?
-
no activity with chitin, chitosan, cellulose, and pectin
-
?
additional information
?
-
-
no activity with chitin, chitosan, cellulose, and pectin
-
?
additional information
?
-
biological function of the enzyme
-
?
additional information
?
-
-
-
-
?
additional information
?
-
biological function of the enzyme
-
?
additional information
?
-
-
biological function of the enzyme
-
?
additional information
?
-
-
biological function of the enzyme
-
?
additional information
?
-
-
biological function of the enzyme
-
?
additional information
?
-
Dollabella auricola
-
assay methods, overview
-
?
additional information
?
-
Dollabella auricola
-
biological function of the enzyme
-
?
additional information
?
-
-
biological function of the enzyme
-
?
additional information
?
-
-
biological function of the enzyme
-
?
additional information
?
-
Aly1 is a bifunctional alginate lyase and prefers L-guluronate to D-mannuronate. Tetrasaccharide-size fractions are the smallest substrates, and D-mannuronate, L-guluronate, and UDP2 fractions are the minimal product types. Products are a series of small size-defined saturated oligosaccharide products from the nonreducing ends of single or different saturated sugar chains and yielding unsaturated products in distinct but restricted pattern. No substrates: chondroitin, chondroitin sulfate, dermantan sulfate B, hyaluronan, heparin, or heparin sulfate
-
-
?
additional information
?
-
enzyme shows high activities toward both poly(beta-D-mannuronate) and poly(alpha-L-guluronate), reactions of EC 4.2.2.3 and 4.2.2.11, respectively
-
-
?
additional information
?
-
-
treatment of the supermucoid biofilm of the supermucoid Pseudomonas aeruginosa strain PDO300DELTAalg8(pBBR1MCS-5:alg8) with alginate lyase results in the breakdown of the microcolony structure, but this treatment had little effect on the mucoid and nonmucoid biofilms
-
-
?
additional information
?
-
enzyme prefers poly-D-mannuronate blocks over poly-L-guluronate blocks
-
-
?
additional information
?
-
Fucus spp.
-
biological function of the enzyme
-
?
additional information
?
-
no substrate: poly(alpha-1,4-L-guluronate)
-
-
?
additional information
?
-
-
the enzyme possesses 5 subsites in its catalytic center, assay methods, overview
-
?
additional information
?
-
-
biological function of the enzyme
-
?
additional information
?
-
Ishige sp.
-
biological function of the enzyme
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
assay methods, overview
-
?
additional information
?
-
-
biological function of the enzyme
-
?
additional information
?
-
the enzyme is an endolytic polymannuronate lyase
-
-
?
additional information
?
-
-
the enzyme is an endolytic polymannuronate lyase
-
-
?
additional information
?
-
-
assay methods, overview
-
?
additional information
?
-
-
biological function of the enzyme
-
?
additional information
?
-
-
induced by native alginate
-
-
?
additional information
?
-
-
endolytic activity
-
?
additional information
?
-
-
biological function of the enzyme
-
?
additional information
?
-
-
biological function of the enzyme
-
?
additional information
?
-
-
biological function of the enzyme
-
?
additional information
?
-
-
assay methods, overview
-
?
additional information
?
-
-
biological function of the enzyme
-
?
additional information
?
-
-
biological function of the enzyme
-
?
additional information
?
-
assay methods, overview
-
?
additional information
?
-
biological function of the enzyme
-
?
additional information
?
-
the enzyme from strain H-4 shows multiple substrate specificities, assay methods, overview
-
?
additional information
?
-
biological function of the enzyme
-
?
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
-
-
?
additional information
?
-
-
assay methods, overview, enzyme from strain CFI/MI possesses 6 subsites and preferably cleaves M-M linkages
-
?
additional information
?
-
-
enzyme from strain CFI/MI possesses 6 subsites and preferably cleaves M-M linkages
-
?
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
-
?
additional information
?
-
-
activity of AlgL is required for alginate production
-
-
?
additional information
?
-
-
the alginate-degrading protein AlgL transports the growing alginate polymer chain through the periplasm
-
-
?
additional information
?
-
the alginate-degrading protein AlgL transports the growing alginate polymer chain through the periplasm
-
-
?
additional information
?
-
-
AlgL is a vital part of the alginate transport scaffold, as well as having a role in degrading alginate as a lyase
-
-
?
additional information
?
-
AlgL is a vital part of the alginate transport scaffold, as well as having a role in degrading alginate as a lyase
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
additional information
?
-
AlgL is an endolytic enzyme that cleaves the 1-4 glycosidic linkage, resulting in disaccharides and trisaccharides as its major products. Several residues, including His202 and Tyr256, play a role in AlgL activity
-
-
?
additional information
?
-
substrates are medium-viscosity brown seaweed alginate (BSWA) and bacterial (FRD1) alginate substrates from mucoid FRD1 biofilms
-
-
?
additional information
?
-
-
substrates are medium-viscosity brown seaweed alginate (BSWA) and bacterial (FRD1) alginate substrates from mucoid FRD1 biofilms
-
-
?
additional information
?
-
-
assay methods, overview, enzyme from strain CFI/MI possesses 6 subsites and preferably cleaves M-M linkages
-
?
additional information
?
-
-
enzyme from strain CFI/MI possesses 6 subsites and preferably cleaves M-M linkages
-
?
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
-
?
additional information
?
-
biological function of the enzyme
-
?
additional information
?
-
-
hydrolysis of the crude alginate since beta-elimination on beta-D-mannuronosyluronate or on alpha-L-gulupyranosyluronate produces, in both cases, the nonreducing end 4-deoxy-L-erythro-hex-4-enepyranosyluronate. Products are mainly trisaccharides, followed by tetrasaccharides, disaccharides, and pentasaccharides in descending order, gel filtration, and mass and NMR spectrometric analyses, overview
-
-
?
additional information
?
-
-
hydrolysis of the crude alginate since beta-elimination on beta-D-mannuronosyluronate or on alpha-L-gulupyranosyluronate produces, in both cases, the nonreducing end 4-deoxy-L-erythro-hex-4-enepyranosyluronate. Products are mainly trisaccharides, followed by tetrasaccharides, disaccharides, and pentasaccharides in descending order, gel filtration, and mass and NMR spectrometric analyses, overview
-
-
?
additional information
?
-
biological function of the enzyme
-
?
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
-
-
?
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
-
-
?
additional information
?
-
-
biological function of the enzyme
-
?
additional information
?
-
enzyme mainly and endolytically depolymerizes polymannuronate by beta-elimination into oligosaccharides with degrees of polymerization of 2-5
-
-
?
additional information
?
-
-
assay methods, overview
-
?
additional information
?
-
substrate specificity, residues His204 and Trp207 are critical for enzyme activity
-
?
additional information
?
-
-
substrate specificity, residues His204 and Trp207 are critical for enzyme activity
-
?
additional information
?
-
-
biological function of the enzyme
-
?
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
-
-
?
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
-
-
?
additional information
?
-
recombinant Alg17C preferentially acts on oligoalginates with degrees of polymerization higher than 2 to produce the alginate monomer, 4-deoxy-L-erythro-5-hexoseulose uronic acid. The enzyme can produce a monomeric sugar acid from alginate by the concerted action of an endo-type alginate lyase and exo-type alginate lyase Alg17C, substrate specificity of Alg17C, overview
-
-
?
additional information
?
-
-
the enzyme is active on poly(beta-D-mannuronate) and poly(alpha-L-guluronate), cf. EC 4.2.2.11
-
-
?
additional information
?
-
the enzyme is active on poly-MM, poly-GG, and poly-MG substrates. Exolytic depolymerization of these polysaccharides by alginate lyase yields a monosaccharide and a product containing a DELTA-(4,5)-unsaturated uronic acid moiety. A mixture of alginate di-, tri-, and tetrasaccharides are processed into mono- and disaccharides in the presence of Alg17c. An alginate trisaccharide represents the minimal length substrate for Alg17c, complete processing only of the tri- and tetrasaccharide substrates, substrate specificity and binding structure, Fourier electron density map, overview
-
-
?
additional information
?
-
-
the enzyme is active on poly-MM, poly-GG, and poly-MG substrates. Exolytic depolymerization of these polysaccharides by alginate lyase yields a monosaccharide and a product containing a DELTA-(4,5)-unsaturated uronic acid moiety. A mixture of alginate di-, tri-, and tetrasaccharides are processed into mono- and disaccharides in the presence of Alg17c. An alginate trisaccharide represents the minimal length substrate for Alg17c, complete processing only of the tri- and tetrasaccharide substrates, substrate specificity and binding structure, Fourier electron density map, overview
-
-
?
additional information
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recombinant Alg17C preferentially acts on oligoalginates with degrees of polymerization higher than 2 to produce the alginate monomer, 4-deoxy-L-erythro-5-hexoseulose uronic acid. The enzyme can produce a monomeric sugar acid from alginate by the concerted action of an endo-type alginate lyase and exo-type alginate lyase Alg17C, substrate specificity of Alg17C, overview
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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
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the enzyme is active on poly-MM, poly-GG, and poly-MG substrates. Exolytic depolymerization of these polysaccharides by alginate lyase yields a monosaccharide and a product containing a DELTA-(4,5)-unsaturated uronic acid moiety. A mixture of alginate di-, tri-, and tetrasaccharides are processed into mono- and disaccharides in the presence of Alg17c. An alginate trisaccharide represents the minimal length substrate for Alg17c, complete processing only of the tri- and tetrasaccharide substrates, substrate specificity and binding structure, Fourier electron density map, overview
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biological function of the enzyme
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assay methods, overview
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no activity with gellan, xanthan, and pectin of A1-I and A1-II
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oligoalginate lyase substrate specificity
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biological function of the enzyme
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A1-1V' has no significant role in alginate metabolism
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substrate specificity of recombinant oligoalginate lyase, overview. Analysis of the final degradation products, overview
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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
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substrates are medium-viscosity brown seaweed alginate (BSWA) and bacterial (FRD1) alginate substrates from mucoid FRD1 biofilms
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enzyme prefers poly-L-guluronate blocks over poly-D-mannuronate blocks
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substrate specificity of recombinant oligoalginate lyase, overview. Analysis of the final degradation products, overview
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assay methods, overview
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biological function of the enzyme
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assay methods, overview
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biological function of the enzyme
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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
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alginate, poly-mannuronate-, poly-guluronate-, and poly-mannuronate-guluronate-block substrates are used, substrate specificity, cf. EC 4.2.2.11, overview. No or poor activity with chondroitin B, agarose, agar, starch, and pectin
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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
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alginate, poly-mannuronate-, poly-guluronate-, and poly-mannuronate-guluronate-block substrates are used, substrate specificity, cf. EC 4.2.2.11, overview. No or poor activity with chondroitin B, agarose, agar, starch, and pectin
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endolytic activity, the enzyme possesses 5 subsites in its catalytic center, assay methods, overview
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biological function of the enzyme
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assay methods, overview
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biological function of the enzyme
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biological function of the enzyme
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preference of M-MM or MM-M cleavage sequences
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biological function of the enzyme
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preference of M-MM or MM-M cleavage sequences
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biological function of the enzyme
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the relative activities for alginate, M, G, and GM blocks are 100%, 75%, 21%, and 15%, respectively
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the relative activities for alginate, M, G, and GM blocks are 100%, 75%, 21%, and 15%, respectively
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the relative activities for alginate, M, G, and GM blocks are 100%, 75%, 21%, and 15%, respectively
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the relative activities for alginate, M, G, and GM blocks are 100%, 75%, 21%, and 15%, respectively
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AlyV5 shows activities towards both polyguluronate and polymannuronate, but degrades the former more efficiently. AlyV5 mainly produces disaccharide, trisaccharide and tetrasaccharide from polyguluronate, trisaccharide, tetrasaccharide and pentasaccharide from polymannuronate
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the relative activities for alginate, M, G, and GM blocks are 100%, 75%, 21%, and 15%, respectively
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additional information
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the relative activities for alginate, M, G, and GM blocks are 100%, 75%, 21%, and 15%, respectively
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additional information
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the relative activities for alginate, M, G, and GM blocks are 100%, 75%, 21%, and 15%, respectively
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additional information
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the relative activities for alginate, M, G, and GM blocks are 100%, 75%, 21%, and 15%, respectively
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AlyV5 shows activities towards both polyguluronate and polymannuronate, but degrades the former more efficiently. AlyV5 mainly produces disaccharide, trisaccharide and tetrasaccharide from polyguluronate, trisaccharide, tetrasaccharide and pentasaccharide from polymannuronate
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AlgB mainly releases oligosaccharides with a degree of polymersiation of 2-5 from the different kinds of substrates in an endolytic manner
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isoforms AlyA and AlyB principally cleave the beta-1,4 bonds between beta-D-mannuronate and alpha-L-guluronate and subunits
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isoforms AlyA and AlyB principally cleave the beta-1,4 bonds between beta-D-mannuronate and alpha-L-guluronate and subunits
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isoforms AlyD and AlyE principally cleave the alpha-1,4 bonds involving alpha-L-guluronate subunits
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isoforms AlyD and AlyE principally cleave the alpha-1,4 bonds involving alpha-L-guluronate subunits
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isoforms AlyA and AlyB principally cleave the beta-1,4 bonds between beta-D-mannuronate and alpha-L-guluronate and subunits
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isoforms AlyA and AlyB principally cleave the beta-1,4 bonds between beta-D-mannuronate and alpha-L-guluronate and subunits
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isoforms AlyD and AlyE principally cleave the alpha-1,4 bonds involving alpha-L-guluronate subunits
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isoforms AlyD and AlyE principally cleave the alpha-1,4 bonds involving alpha-L-guluronate subunits
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the enzyme has a broad substrate tolerance and can cleave mannuronate-mannuronate, mannuronate-guluronate, and guluronate-guluronate linkages at the nonreducing end. The activity is depending on the block structure
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the enzyme has a broad substrate tolerance and can cleave mannuronate-mannuronate, mannuronate-guluronate, and guluronate-guluronate linkages at the nonreducing end. The activity is depending on the block structure
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the enzyme has a broad substrate tolerance and can cleave mannuronate-mannuronate, mannuronate-guluronate, and guluronate-guluronate linkages at the nonreducing end. The activity is depending on the block structure
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