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acetylated alginate
?
-
Substrates: -
Products: -
?
acetylated alginate
acetylated algino-oligosaccharides
Substrates: -
Products: -
?
acetylated poly-(beta-(1->4)-D-mannuronan)
?
-
Substrates: -
Products: -
?
alginate
alpha-L-guluronate + beta-D-mannuronate + algino-disaccharides
-
Substrates: -
Products: -
?
alginate
disaccharides + trisaccharides
A0A7G4RN99
Substrates: 100% activity
Products: -
?
alginate
disaccharides + trisaccharides + tetrasaccharides
-
Substrates: -
Products: -
?
alginate
disaccharides + trisaccharides + tetrasaccharides + pentasaccharides + hexasaccharides
-
Substrates: -
Products: -
?
alginate
unsaturated algino-oligosaccharides
alpha-L-guluronosyl linkage in alginate
?
penta(alpha-(1->4)-L-guluronate)
disaccharides + trisaccharides
A0A1Z2QRI2
Substrates: the pentasaccharide is the shortest chain that can be recognized and cleaved by the enzyme
Products: -
?
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)
disaccharides + trisaccharides + tetrasaccharides
A0A1Z2QRI2
Substrates: highest activity
Products: -
?
poly(alpha-(1->4)-L-guluronate)
monosaccharides + disaccharides + trisaccharides
A0A1B1FUS6
Substrates: the enzyme prefers poly(alpha-(1->4)-L-guluronate) to poly(beta-(1->4)-D-mannuronate)
Products: -
?
poly(alpha-(1->4)-L-guluronate)
trisaccharides
poly(alpha-(1->4)-L-guluronate)
trisaccharides + tetrasaccharides
poly(alpha-(1->4)-L-guluronic acid)
?
poly(alpha-(1->4)-L-guluronic acid)
disaccharides + trisaccharides
poly(alpha-(1->4)-L-guluronic acid)
disaccharides + trisaccharides + tetrasaccharides
-
Substrates: about 45% activity compared to sodium alginate
Products: -
?
poly(alpha-(1->4)-L-guluronic acid)
disaccharides + trisaccharides + tetrasaccharides + pentasaccharides
poly(alpha-(1->4)-L-guluronic acid)
disaccharides + trisaccharides + tetrasaccharides + pentasaccharides + hexasaccharides
-
Substrates: preferred substrate
Products: -
?
poly(alpha-(1->4)-L-guluronic acid)
monosaccharides + disaccharides + low molecular weight oligosaccharides
Substrates: -
Products: -
?
poly(alpha-(1->4)-L-guluronic acid)
monosaccharides + disaccharides + trisaccharides
poly(alpha-(1->4)-L-guluronic acid)
monosaccharides + disaccharides + trisaccharides + tetrasaccharides + pentasaccharides
A0A650FAR8
Substrates: about 95% activity compared to alginate
Products: -
?
poly(alpha-(1->4)-L-guluronic acid)
trisaccharides + tetrasaccharides
A0A1Y0SY54
Substrates: substrate with highest degradation efficiency. About 110% activity compared to sodium alginate
Products: -
?
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)
A0A1B1FUW4
Substrates: -
Products: -
?
poly(alpha-L-guluronate)
?
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)
disaccharides + trisaccharides + tetrasaccharides
A0A1Z2QRI2
Substrates: -
Products: -
?
poly(beta-(1->4)-D-mannuronate)
monosaccharides + disaccharides + trisaccharides
A0A1B1FUS6
Substrates: -
Products: -
?
poly(beta-(1->4)-D-mannuronate)
trisaccharides + tetrasaccharides
poly(beta-(1->4)-D-mannuronate/alpha-(1->4)-L-guluronate)
trisaccharides
poly(beta-(1->4)-D-mannuronic acid)
?
poly(beta-(1->4)-D-mannuronic acid)
disaccharides + trisaccharides
poly(beta-(1->4)-D-mannuronic acid)
disaccharides + trisaccharides + tetrasaccharides
-
Substrates: about 20% activity compared to sodium alginate
Products: -
?
poly(beta-(1->4)-D-mannuronic acid)
disaccharides + trisaccharides + tetrasaccharides + pentasaccharides
poly(beta-(1->4)-D-mannuronic acid)
disaccharides + trisaccharides + tetrasaccharides + pentasaccharides + hexasaccharides
-
Substrates: -
Products: -
?
poly(beta-(1->4)-D-mannuronic acid)
monosaccharides + disaccharides + low molecular weight oligosaccharides
Substrates: -
Products: -
?
poly(beta-(1->4)-D-mannuronic acid)
monosaccharides + disaccharides + trisaccharides
poly(beta-(1->4)-D-mannuronic acid)
monosaccharides + disaccharides + trisaccharides + tetrasaccharides + pentasaccharides
A0A650FAR8
Substrates: about 35% activity compared to alginate
Products: -
?
poly(beta-(1->4)-D-mannuronic acid)
trisaccharides + tetrasaccharides
poly(beta-(1->4)-D-mannuronic acid/alpha-(1->4)-L-guluronic acid)
?
poly(beta-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
A0A1B1FUW4
Substrates: -
Products: -
?
poly(beta-D-mannuronic acid/alpha-(1->4)-L-guluronic acid)
?
poly-(alpha-L-guluronate)
?
Substrates: -
Products: -
?
poly-(beta-(1->4)-D-mannuronan)
?
poly-alpha-L-guluronic acid
4-deoxy-erythro-hex-4-ene pyranosyluronate + ?
Substrates: degradation of alginate
Products: -
?
poly-alpha-L-guluronic acid
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
poly-beta1,4-D-mannuronan
?
saturated deca((1-4)-alpha-L-guluronan)
?
saturated hepta((1-4)-alpha-L-guluronan)
?
saturated hexa((1-4)-alpha-L-guluronan)
saturated di((1-4)-alpha-L-guluronan) + unsaturated tetra((1-4)-alpha-L-guluronan)
A0A0M4N5N7
Substrates: -
Products: -
?
saturated hexa((1-4)-alpha-L-guluronan)
unsaturated tetramer and a saturated dimer
saturated penta((1-4)-alpha-L-guluronan)
?
saturated penta((1-4)-alpha-L-guluronan)
saturated di((1-4)-alpha-L-guluronan) + unsaturated tri((1-4)-alpha-L-guluronan)
saturated tetra((1-4)-alpha-L-guluronan)
?
sodium alginate
disaccharides + trisaccharides
sodium alginate
disaccharides + trisaccharides + tetrasaccharides
sodium alginate
disaccharides + trisaccharides + tetrasaccharides + pentasaccharides
Substrates: 100% activity
Products: -
?
sodium alginate
monosaccharides + disaccharides + trisaccharides
sodium alginate
trisaccharides
sodium alginate
trisaccharides + tetrasaccharides
unsaturated hepta((1-4)-alpha-L-guluronan)
?
unsaturated hexa((1-4)-alpha-L-guluronan)
unsaturated triguluronic acid + unsaturated tetraguluronic acid
unsaturated pentaguluronan
?
additional information
?
-
alginate

?
-
Substrates: A1m preferably degrades the heteropolymeric MG and G blocks (1,4 linked alpha-L-guluronic acid) to the M block (beta-D-mannuronic acid). The relative activities for alginate, MG, G, and M blocks are 100%, 131.7%, 83.3%, and 27.3%, respectively
Products: -
?
alginate
?
Substrates: -
Products: high yields of penta-, hex-, and heptasaccharides in the hydrolysis products
?
alginate
?
-
Substrates: optimal conditions are 0.3-0.7% alginate content
Products: -
?
alginate
?
AB489222
Substrates: the bifunctional alginate lyase shows substrate specificity for poly(alpha-L-guluronate) and poly(beta-D-mannuronate) units in alginate molecules, cf. EC 4.2.2.3
Products: -
?
alginate
?
AB489222
Substrates: enzyme shows specificity for polyguluronate and polymannuronate units in alginate molecules
Products: -
?
alginate
?
-
Substrates: enzyme shows specificity for polyguluronate and polymannuronate units in alginate molecules
Products: -
?
alginate
?
AB489222
Substrates: the bifunctional alginate lyase shows substrate specificity for poly(alpha-L-guluronate) and poly(beta-D-mannuronate) units in alginate molecules, cf. EC 4.2.2.3
Products: -
?
alginate
?
-
Substrates: -
Products: -
?
alginate
?
Substrates: -
Products: enzyme cleaves the glycosidic linkages between two mannuronates (mannuronate-beta(1-4)-mannuronate) or mannuronate and guluronate (mannuronate-beta(1-4)-guluronate)
?
alginate
?
-
Substrates: the enzyme endolytically depolymerizes alginate by beta-elimination into oligo-alginates with degrees of polymerization of 2-5
Products: -
?
alginate
?
Substrates: AlgMytC is predicted to preferably degrade guluronate-blocks because of the presence of the QIH motif in the conserved signature of the amino acid sequence
Products: -
?
alginate
?
G3LI08
Substrates: -
Products: enzyme degrades alginate into a mixture of products with molecular masses below 1000 Da
?
alginate
?
-
Substrates: 100% activity
Products: -
?
alginate
?
-
Substrates: -
Products: -
?
alginate
?
-
Substrates: -
Products: -
?
alginate
?
-
Substrates: -
Products: -
?
alginate

unsaturated algino-oligosaccharides
Substrates: -
Products: -
?
alginate
unsaturated algino-oligosaccharides
-
Substrates: -
Products: -
?
alginate
unsaturated algino-oligosaccharides
A0A1B1FUW4
Substrates: -
Products: -
?
alginate
unsaturated algino-oligosaccharides
A0A0M4N5N7
Substrates: -
Products: -
?
alginate
unsaturated algino-oligosaccharides
Substrates: -
Products: -
?
alginate
unsaturated algino-oligosaccharides
Substrates: -
Products: -
?
alginate
unsaturated algino-oligosaccharides
Substrates: -
Products: -
?
alginate
unsaturated algino-oligosaccharides
Substrates: -
Products: -
?
alginate
unsaturated algino-oligosaccharides
-
Substrates: -
Products: -
?
alginate
unsaturated algino-oligosaccharides
A0A3B6UEP6
Substrates: best substrate
Products: -
?
alginate
unsaturated algino-oligosaccharides
-
Substrates: about 50% of the activity with poly(alpha-(1,4)-L-guluronate)
Products: -
?
alginate
unsaturated algino-oligosaccharides
-
Substrates: -
Products: -
?
alginate
unsaturated algino-oligosaccharides
-
Substrates: -
Products: -
?
alginate
unsaturated algino-oligosaccharides
Substrates: -
Products: -
?
alginate
unsaturated algino-oligosaccharides
A0A1Z2QRD5
Substrates: -
Products: -
?
alginate
unsaturated algino-oligosaccharides
Substrates: -
Products: -
?
alginate
unsaturated algino-oligosaccharides
Substrates: -
Products: -
?
alginate
unsaturated algino-oligosaccharides
A3UR44, A3UT33
Substrates: -
Products: -
?
alginate
unsaturated algino-oligosaccharides
A3UR44, A3UT33
Substrates: -
Products: -
?
alginate
unsaturated algino-oligosaccharides
Substrates: -
Products: -
?
alpha-L-guluronosyl linkage in alginate

?
Substrates: -
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
-
Substrates: -
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
-
Substrates: endolyase
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
-
Substrates: 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
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
-
Substrates: endolyase
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
Substrates: endolyase
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
-
Substrates: endolyase
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
-
Substrates: -
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
-
Substrates: endolyase
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
-
Substrates: significant activity is found not only on guluronate-guluronate linkages but also on guluronate-mannuronate linkages
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
-
Substrates: endolyase
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
-
Substrates: significant activity is found not only on guluronate-guluronate linkages but also on guluronate-mannuronate linkages
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
-
Substrates: -
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
-
Substrates: -
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
-
Substrates: -
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
-
Substrates: activity is highest on short-chain poly-guluronic acid blocks and guluronic-rich alginate, intracellular and extracellular enzymes are endo-lyases, O-acetylation and carboxyl esterification of alginate substrate inhibits intracellular enzyme action
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
-
Substrates: -
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
-
Substrates: significant activity is found not only on guluronate-guluronate linkages but also on guluronate-mannuronate linkages
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
Substrates: endolyase
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
-
Substrates: -
Products: enzyme shows activities toward both polyG, i.e. poly-alpha-(1->4)-L-guluronic acid, and polyM, i.e. poly-beta-D-mannuronic acid
?
alpha-L-guluronosyl linkage in alginate
?
-
Substrates: alginate lyase isoform C has the specificity for G block while 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
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
-
Substrates: alginate lyase isoform C has the specificity for G block while 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
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
-
Substrates: -
Products: 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-guluronosyl linkage in alginate
?
-
Substrates: -
Products: 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-guluronosyl linkage in alginate
?
-
Substrates: -
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
-
Substrates: endolyase
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
-
Substrates: endolyase
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
-
Substrates: -
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
Substrates: -
Products: final degradation products are alginate monosaccharides
?
alpha-L-guluronosyl linkage in alginate
?
Substrates: preferably degrades the M block to the G block in alginate
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
Substrates: preferably degrades G blocks
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
Substrates: preferably degrades G blocks
Products: -
?
alpha-L-guluronosyl linkage in alginate
?
Substrates: preferably degrades the M block to the G block in alginate
Products: -
?
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)
-
Substrates: -
Products: -
?
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)
Substrates: reaction of EC 4.2.2.11
Products: -
?
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)
Substrates: -
Products: -
?
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)
Substrates: -
Products: -
?
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)
Substrates: -
Products: -
?
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)
-
Substrates: -
Products: -
?
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)
A0A3B6UEP6
Substrates: about 60% of the activity with alginate
Products: -
?
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)
-
Substrates: -
Products: -
?
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)
-
Substrates: -
Products: -
?
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)
Substrates: -
Products: -
?
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)
A0A1Z2QRD5
Substrates: -
Products: -
?
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)
Substrates: -
Products: -
?
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)
Substrates: -
Products: -
?
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)
Substrates: -
Products: -
?
poly(alpha-(1->4)-L-guluronate)

trisaccharides
A0A2S7V3I3
Substrates: -
Products: -
?
poly(alpha-(1->4)-L-guluronate)
trisaccharides
A0A2S7V3I3
Substrates: -
Products: -
?
poly(alpha-(1->4)-L-guluronate)

trisaccharides + tetrasaccharides
-
Substrates: 55.2% activity compared to sodium alginate
Products: -
?
poly(alpha-(1->4)-L-guluronate)
trisaccharides + tetrasaccharides
-
Substrates: 55.2% activity compared to sodium alginate
Products: -
?
poly(alpha-(1->4)-L-guluronic acid)

?
Substrates: preferred over poly-(beta1,4-D-mannuronan)
Products: -
?
poly(alpha-(1->4)-L-guluronic acid)
?
-
Substrates: -
Products: -
?
poly(alpha-(1->4)-L-guluronic acid)
?
-
Substrates: -
Products: -
?
poly(alpha-(1->4)-L-guluronic acid)
?
-
Substrates: -
Products: -
?
poly(alpha-(1->4)-L-guluronic acid)
?
-
Substrates: -
Products: -
?
poly(alpha-(1->4)-L-guluronic acid)
?
Substrates: 90% of the activity with alginate
Products: -
?
poly(alpha-(1->4)-L-guluronic acid)
?
G3LI08
Substrates: -
Products: -
?
poly(alpha-(1->4)-L-guluronic acid)
?
-
Substrates: 98% activity compared to alginate
Products: -
?
poly(alpha-(1->4)-L-guluronic acid)
?
-
Substrates: 108% of the activity with alginate
Products: main products are disaccharide, trisaccharide and tetrasaccharide
?
poly(alpha-(1->4)-L-guluronic acid)
?
-
Substrates: 108% of the activity with alginate
Products: main products are disaccharide, trisaccharide and tetrasaccharide
?
poly(alpha-(1->4)-L-guluronic acid)

disaccharides + trisaccharides
A0A7G4RN99
Substrates: about 150% activity compared to alginate
Products: -
?
poly(alpha-(1->4)-L-guluronic acid)
disaccharides + trisaccharides
-
Substrates: preferred substrate. Pentaguluronic acid is the smallest substrate that can be degraded by the enzyme
Products: -
?
poly(alpha-(1->4)-L-guluronic acid)
disaccharides + trisaccharides
-
Substrates: 100% activity
Products: -
?
poly(alpha-(1->4)-L-guluronic acid)
disaccharides + trisaccharides
-
Substrates: preferred substrate
Products: -
?
poly(alpha-(1->4)-L-guluronic acid)
disaccharides + trisaccharides
Substrates: highest activity
Products: -
?
poly(alpha-(1->4)-L-guluronic acid)

disaccharides + trisaccharides + tetrasaccharides + pentasaccharides
Substrates: about 120% activity compared to sodium alginate
Products: -
?
poly(alpha-(1->4)-L-guluronic acid)
disaccharides + trisaccharides + tetrasaccharides + pentasaccharides
Substrates: about 70% activity compared to sodium alginate
Products: -
?
poly(alpha-(1->4)-L-guluronic acid)

monosaccharides + disaccharides + trisaccharides
-
Substrates: 134.2% activity compared to sodium alginate
Products: -
?
poly(alpha-(1->4)-L-guluronic acid)
monosaccharides + disaccharides + trisaccharides
-
Substrates: 134.2% activity compared to sodium alginate
Products: -
?
poly(alpha-L-guluronate)

?
AB489222
Substrates: -
Products: -
?
poly(alpha-L-guluronate)
?
AB489222
Substrates: -
Products: -
?
poly(alpha-L-guluronate)
?
-
Substrates: -
Products: -
?
poly(alpha-L-guluronate)
?
-
Substrates: -
Products: -
?
poly(alpha-L-guluronate)
?
-
Substrates: -
Products: -
?
poly(alpha-L-guluronate)
?
-
Substrates: best substrate
Products: -
?
poly(alpha-L-guluronate)
?
-
Substrates: best substrate
Products: -
?
poly(alpha-L-guluronate)
?
Substrates: -
Products: -
?
poly(alpha-L-guluronate)
?
Substrates: unmodified substrate poly-G blocks and substrate that with its reducing end being reduced using sodium borohydride prior to the digestion
Products: -
?
poly(alpha-L-guluronate)
?
Substrates: -
Products: -
?
poly(alpha-L-guluronate)
?
Substrates: unmodified substrate poly-G blocks and substrate that with its reducing end being reduced using sodium borohydride prior to the digestion
Products: -
?
poly(beta-(1,4)-D-mannuronate)

4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
-
Substrates: reaction of EC 4.2.2.3
Products: -
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
Substrates: -
Products: -
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
Substrates: reaction of EC 4.2.2.3
Products: -
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
Substrates: reaction of EC 4.2.2.3
Products: -
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
Substrates: reaction of EC 4.2.2.3
Products: -
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
-
Substrates: reaction of EC 4.2.2.3, about 50% of the activity with poly(alpha-(1,4)-L-guluronate) or alginate
Products: -
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
A0A3B6UEP6
Substrates: reaction of EC 4.2.2.3, about 30% of the activity with alginate
Products: -
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
-
Substrates: reaction of EC 4.2.2.3, about 20% of the activity with poly(alpha-(1,4)-L-guluronate)
Products: -
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
Substrates: reaction of EC 4.2.2.3
Products: -
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
A0A1Z2QRD5
Substrates: reaction of EC 4.2.2.3
Products: -
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
Substrates: reaction of EC 4.2.2.3
Products: -
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
Substrates: -
Products: -
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
Substrates: reaction of EC 4.2.2.3
Products: -
?
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)
-
Substrates: -
Products: -
?
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)
-
Substrates: about 30% of the activity with poly(alpha-(1,4)-L-guluronate)
Products: -
?
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)
Substrates: -
Products: -
?
poly(beta-(1->4)-D-mannuronate)

trisaccharides + tetrasaccharides
-
Substrates: about 30% activity compared to sodium alginate
Products: -
?
poly(beta-(1->4)-D-mannuronate)
trisaccharides + tetrasaccharides
-
Substrates: about 30% activity compared to sodium alginate
Products: -
?
poly(beta-(1->4)-D-mannuronate/alpha-(1->4)-L-guluronate)

trisaccharides
A0A2S7V3I3
Substrates: -
Products: -
?
poly(beta-(1->4)-D-mannuronate/alpha-(1->4)-L-guluronate)
trisaccharides
A0A2S7V3I3
Substrates: -
Products: -
?
poly(beta-(1->4)-D-mannuronic acid)

?
G3LI08
Substrates: preferred over poly(alpha-(1->4)-L-guluronic acid)
Products: -
?
poly(beta-(1->4)-D-mannuronic acid)
?
-
Substrates: 40% activity compared to alginate
Products: -
?
poly(beta-(1->4)-D-mannuronic acid)

disaccharides + trisaccharides
A0A7G4RN99
Substrates: about 60% activity compared to alginate
Products: -
?
poly(beta-(1->4)-D-mannuronic acid)
disaccharides + trisaccharides
-
Substrates: about 40% activity compared to poly(alpha-(1->4)-L-guluronic acid)
Products: -
?
poly(beta-(1->4)-D-mannuronic acid)
disaccharides + trisaccharides
-
Substrates: -
Products: -
?
poly(beta-(1->4)-D-mannuronic acid)
disaccharides + trisaccharides
Substrates: lowest activity
Products: -
?
poly(beta-(1->4)-D-mannuronic acid)

disaccharides + trisaccharides + tetrasaccharides + pentasaccharides
Substrates: about 95% activity compared to sodium alginate
Products: -
?
poly(beta-(1->4)-D-mannuronic acid)
disaccharides + trisaccharides + tetrasaccharides + pentasaccharides
Substrates: about 40% activity compared to sodium alginate
Products: -
?
poly(beta-(1->4)-D-mannuronic acid)

monosaccharides + disaccharides + trisaccharides
-
Substrates: 53.88% activity compared to sodium alginate
Products: -
?
poly(beta-(1->4)-D-mannuronic acid)
monosaccharides + disaccharides + trisaccharides
-
Substrates: 53.88% activity compared to sodium alginate
Products: -
?
poly(beta-(1->4)-D-mannuronic acid)

trisaccharides + tetrasaccharides
A0A1Y0SY54
Substrates: substrate with lowest degradation efficiency. About 55% activity compared to sodium alginate
Products: -
?
poly(beta-(1->4)-D-mannuronic acid)
trisaccharides + tetrasaccharides
-
Substrates: pentamannuronic acid is the smallest substrate that can be degraded by the enzyme
Products: -
?
poly(beta-(1->4)-D-mannuronic acid/alpha-(1->4)-L-guluronic acid)

?
Substrates: -
Products: -
?
poly(beta-(1->4)-D-mannuronic acid/alpha-(1->4)-L-guluronic acid)
?
Substrates: alternating structure of alpha-L-guluronic acid and beta-D-mannuronic acid. 120% of the activity with alginate
Products: -
?
poly(beta-D-mannuronic acid/alpha-(1->4)-L-guluronic acid)

?
-
Substrates: 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
Products: -
?
poly(beta-D-mannuronic acid/alpha-(1->4)-L-guluronic acid)
?
-
Substrates: 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
Products: -
?
poly-(beta-(1->4)-D-mannuronan)

?
Substrates: -
Products: -
?
poly-(beta-(1->4)-D-mannuronan)
?
-
Substrates: Km value decreases with increasing substrate length, and kcat/Km increases. Oligomers containing fewer than 9-10 residues are not substrates
Products: -
?
poly-(beta-(1->4)-D-mannuronan)
?
-
Substrates: 30% of the activity with alginate
Products: main products are trisaccharide, tetrasaccharide and pentasaccharide
?
poly-(beta-(1->4)-D-mannuronan)
?
-
Substrates: 30% of the activity with alginate
Products: main products are trisaccharide, tetrasaccharide and pentasaccharide
?
poly-alpha-L-guluronic acid

?
-
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
?
-
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
?
-
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
?
-
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
?
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
?
-
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
?
-
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
?
-
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
?
-
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
?
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
?
-
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
?
-
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
?
-
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
?
-
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
?
-
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
?
-
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid

unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
Substrates: -
Products: with a smaller proportion of the homologous tetrasaccharide
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
Substrates: -
Products: -
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
Substrates: -
Products: -
?
poly-beta1,4-D-mannuronan

?
-
Substrates: competitive to poly-alpha1,4-L-guluronan
Products: -
?
poly-beta1,4-D-mannuronan
?
-
Substrates: -
Products: -
?
poly-beta1,4-D-mannuronan
?
-
Substrates: seems to have slight activity on poly-mannuronan
Products: -
?
poly-beta1,4-D-mannuronan
?
-
Substrates: seems to have slight activity on poly-mannuronan
Products: -
?
poly-beta1,4-D-mannuronan
?
-
Substrates: -
Products: -
?
poly-beta1,4-D-mannuronan
?
-
Substrates: -
Products: -
?
poly-beta1,4-D-mannuronan
?
Substrates: -
Products: -
?
saturated deca((1-4)-alpha-L-guluronan)

?
-
Substrates: -
Products: -
?
saturated deca((1-4)-alpha-L-guluronan)
?
-
Substrates: -
Products: -
?
saturated hepta((1-4)-alpha-L-guluronan)

?
-
Substrates: -
Products: -
?
saturated hepta((1-4)-alpha-L-guluronan)
?
-
Substrates: -
Products: -
?
saturated hepta((1-4)-alpha-L-guluronan)
?
-
Substrates: -
Products: -
?
saturated hexa((1-4)-alpha-L-guluronan)

unsaturated tetramer and a saturated dimer
-
Substrates: -
Products: -
?
saturated hexa((1-4)-alpha-L-guluronan)
unsaturated tetramer and a saturated dimer
-
Substrates: rapidly degraded in the endolytic mode, enzyme has a subsite corresponding to hexa((1-4)-alpha-L-guluronan) units, cleaving the substrate between subsites two and three from the non-reducing end
Products: main products, the catalytic site is matched to the linkage between the second and the third uronic residue from the non-reducing end, the degradation of tri((1-4)-alpha-L-guluronan) does not apparently occur
?
saturated hexa((1-4)-alpha-L-guluronan)
unsaturated tetramer and a saturated dimer
Substrates: rapidly degraded in the endolytic mode, enzyme has a subsite corresponding to hexa((1-4)-alpha-L-guluronan) units, cleaving the substrate between subsites two and three from the non-reducing end
Products: -
?
saturated hexa((1-4)-alpha-L-guluronan)
unsaturated tetramer and a saturated dimer
-
Substrates: rapidly degraded in the endolytic mode, enzyme has a subsite corresponding to hexa((1-4)-alpha-L-guluronan) units, cleaving the substrate between subsites two and three from the non-reducing end
Products: main products, the catalytic site is matched to the linkage between the second and the third uronic residue from the non-reducing end, the degradation of tri((1-4)-alpha-L-guluronan) does not apparently occur
?
saturated penta((1-4)-alpha-L-guluronan)

?
-
Substrates: -
Products: -
?
saturated penta((1-4)-alpha-L-guluronan)
?
-
Substrates: degraded slower than unsaturated oligoguluronans with the same degree of polymerization, completely different cleavage pattern
Products: -
?
saturated penta((1-4)-alpha-L-guluronan)
?
-
Substrates: degraded slower than unsaturated oligoguluronans with the same degree of polymerization, completely different cleavage pattern
Products: -
?
saturated penta((1-4)-alpha-L-guluronan)

saturated di((1-4)-alpha-L-guluronan) + unsaturated tri((1-4)-alpha-L-guluronan)
-
Substrates: -
Products: -
?
saturated penta((1-4)-alpha-L-guluronan)
saturated di((1-4)-alpha-L-guluronan) + unsaturated tri((1-4)-alpha-L-guluronan)
A0A0M4N5N7
Substrates: -
Products: -
?
saturated tetra((1-4)-alpha-L-guluronan)

?
-
Substrates: only reactive in a high concentration of enzyme, and for a prolonged reaction time
Products: -
?
saturated tetra((1-4)-alpha-L-guluronan)
?
-
Substrates: -
Products: -
?
saturated tetra((1-4)-alpha-L-guluronan)
?
-
Substrates: -
Products: -
?
sodium alginate

?
Substrates: Alg2A prefers poly-(alpha-L-guluronate) as a substrate over poly-(beta-D-mannuronate), substrate specificity, overview
Products: -
?
sodium alginate
?
Substrates: -
Products: -
?
sodium alginate
?
-
Substrates: -
Products: -
?
sodium alginate
?
-
Substrates: high activity
Products: -
?
sodium alginate
?
-
Substrates: high activity
Products: -
?
sodium alginate
?
Substrates: AlyA1PL7 is an endolytic guluronate lyase that preferentially cleaves guluronate stretches
Products: -
?
sodium alginate
?
Substrates: 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 4.2.2.3
Products: -
?
sodium alginate
?
Substrates: AlyA1PL7 is an endolytic guluronate lyase that preferentially cleaves guluronate stretches, no activity with poly-(mannuronate-guluronate) and poly-(mannuronate-mannuronate), minimal recognition pattern of AlyA1PL7, overview
Products: mainly trisaccharide and tetrasaccharide oligomers of alginate with a total content of 41% and 36%, respectively, around 19% disaccharide and only a small amount of pentamers and hexamers, LC mass and NMR spectrometric product analysis
?
sodium alginate
?
Substrates: LC mass and NMR spectrometris product analysis
Products: -
?
sodium alginate
?
Substrates: AlyA1PL7 is an endolytic guluronate lyase that preferentially cleaves guluronate stretches
Products: -
?
sodium alginate
?
Substrates: AlyA1PL7 is an endolytic guluronate lyase that preferentially cleaves guluronate stretches, no activity with poly-(mannuronate-guluronate) and poly-(mannuronate-mannuronate), minimal recognition pattern of AlyA1PL7, overview
Products: mainly trisaccharide and tetrasaccharide oligomers of alginate with a total content of 41% and 36%, respectively, around 19% disaccharide and only a small amount of pentamers and hexamers, LC mass and NMR spectrometric product analysis
?
sodium alginate
?
Substrates: 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 4.2.2.3
Products: -
?
sodium alginate
?
Substrates: LC mass and NMR spectrometris product analysis
Products: -
?
sodium alginate

disaccharides + trisaccharides
-
Substrates: about 50% activity compared to poly(alpha-(1->4)-L-guluronic acid)
Products: -
?
sodium alginate
disaccharides + trisaccharides
-
Substrates: -
Products: -
?
sodium alginate
disaccharides + trisaccharides
Substrates: -
Products: -
?
sodium alginate

disaccharides + trisaccharides + tetrasaccharides
-
Substrates: -
Products: -
?
sodium alginate
disaccharides + trisaccharides + tetrasaccharides
-
Substrates: -
Products: -
?
sodium alginate
disaccharides + trisaccharides + tetrasaccharides
A0A650FAR8
Substrates: 100% activity
Products: -
?
sodium alginate
disaccharides + trisaccharides + tetrasaccharides
-
Substrates: 100% activity
Products: -
?
sodium alginate
disaccharides + trisaccharides + tetrasaccharides
A0A1Z2QRI2
Substrates: -
Products: -
?
sodium alginate

monosaccharides + disaccharides + trisaccharides
A0A1B1FUS6
Substrates: best substrate. The enzyme is guluronate-preferring, endolytic and monosaccharide-producing
Products: -
?
sodium alginate
monosaccharides + disaccharides + trisaccharides
Substrates: the enzyme can recognize the tetrasaccharide as the minimal substrate and cleave the glycosidic bonds between the subsites of -3 and +1. The degradation products of pentasaccharide, hexasaccharide, heptasaccharide, and octasaccharide are all similar, including oligosaccharides with degree of polymerization of 1-4
Products: -
?
sodium alginate
monosaccharides + disaccharides + trisaccharides
-
Substrates: 100% activity
Products: -
?
sodium alginate
monosaccharides + disaccharides + trisaccharides
-
Substrates: 100% activity
Products: -
?
sodium alginate

trisaccharides
A0A2S7V3I3
Substrates: -
Products: -
?
sodium alginate
trisaccharides
A0A2S7V3I3
Substrates: -
Products: -
?
sodium alginate

trisaccharides + tetrasaccharides
A0A1Y0SY54
Substrates: 100% activity
Products: -
?
sodium alginate
trisaccharides + tetrasaccharides
-
Substrates: 100% activity
Products: -
?
sodium alginate
trisaccharides + tetrasaccharides
-
Substrates: 100% activity
Products: -
?
unsaturated hepta((1-4)-alpha-L-guluronan)

?
-
Substrates: -
Products: -
?
unsaturated hepta((1-4)-alpha-L-guluronan)
?
-
Substrates: -
Products: -
?
unsaturated hexa((1-4)-alpha-L-guluronan)

unsaturated triguluronic acid + unsaturated tetraguluronic acid
-
Substrates: the enzyme degrades unsaturated hexaguluronans faster than saturated hexaguluronans, its subsite number appears to be seven
Products: unsaturated trimers are the mayor product
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unsaturated hexa((1-4)-alpha-L-guluronan)
unsaturated triguluronic acid + unsaturated tetraguluronic acid
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Substrates: the enzyme degrades unsaturated hexaguluronans faster than saturated hexaguluronans, its subsite number appears to be seven
Products: unsaturated trimers are the mayor product
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unsaturated pentaguluronan

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Substrates: also degrades unsaturated hexa- and hepta-guluronans, not unsaturated oligoguluronans with degree of polymerization less than four, cleaves the second glycosidic linkage from the non-reducing end of unsaturated pentaguluronans and heptaguluronans
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unsaturated pentaguluronan
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Substrates: also degrades unsaturated hexa- and hepta-guluronans, not unsaturated oligoguluronans with degree of polymerization less than four, cleaves the second glycosidic linkage from the non-reducing end of unsaturated pentaguluronans and heptaguluronans
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additional information

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Substrates: no action on trimeric guluronan and mannuronan, but on tetramers or more, the enzyme is most likely beta-structure, the subsite number is most likely six for both guluronate and mannuronate units, the catalytic site of this enzyme is located at the midpoint of the subsite
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additional information
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Substrates: a simple and highly sensitive method for determining if the alginate lyase is poly-mannuronan specific or poly-((1-4)-alpha-L-guluronan) specific based in the interaction between calcium ions and depolymerized alginates is available
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additional information
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Substrates: -
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additional information
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Substrates: -
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additional information
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Substrates: nine amino acid block conserved in the N-terminus
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additional information
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Substrates: nine amino acid block conserved in the N-terminus
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additional information
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Substrates: nine amino acid conserved block at the C-termini, unrelated to substrate recognition but to maintenance of the stable three-dimensional conformation
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additional information
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Substrates: nine amino acid conserved block at the C-termini, unrelated to substrate recognition but to maintenance of the stable three-dimensional conformation
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additional information
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Substrates: the first twenty amino acids are completely identical in Klebsiella pneumoniae and in Enterobacter cloacae, N-terminus
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additional information
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A0A1B1FUW4
Substrates: Aly1 is a bifunctional alginate lyase and prefers G to M. 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
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additional information
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Substrates: 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
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additional information
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Substrates: alginate disaccharides and trisaccharides cannot be further degraded by the enzyme with even higher concentration and longer incubation time
Products: -
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additional information
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Substrates: a simple and highly sensitive method for determining if the alginate lyase is poly-mannuronan specific or poly-((1-4)-alpha-L-guluronan) specific based in the interaction between calcium ions and depolymerized alginates is available
Products: -
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additional information
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Substrates: Alg2A has a different endolytic reaction mode from both the two commercial alginate lyases and other alginate lyases from polysaccharide lyase family 7 owing to high yields of penta-, hex-, and hepta-saccharides in the hydrolysis products of Alg2A
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additional information
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Substrates: the enzyme shows low activity with poly(beta-D-mannuronate), reaction of EC 4.2.2.3
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additional information
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Substrates: enzyme prefers polyM blocks over polyG blocks
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additional information
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Substrates: no substrats: pectin, xanthan, guar gum, arabic gum, sesbania gum, guar gum and carrageenan
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additional information
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AB489222
Substrates: no substrats: pectin, xanthan, guar gum, arabic gum, sesbania gum, guar gum and carrageenan
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additional information
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Substrates: no substrats: pectin, xanthan, guar gum, arabic gum, sesbania gum, guar gum and carrageenan
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additional information
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Substrates: requires high salt concentrations for maximal activity, no action on: laminarin, dextran, heparin, chondroitin sulfate, pullulan, yeast mannan, lichenin or porphyran, slight amylase activity with amylose and glycogen, beta-elimination mechanism, three-step reaction
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additional information
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Substrates: requires high salt concentrations for maximal activity, no action on: laminarin, dextran, heparin, chondroitin sulfate, pullulan, yeast mannan, lichenin or porphyran, slight amylase activity with amylose and glycogen, beta-elimination mechanism, three-step reaction
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additional information
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Substrates: requires high salt concentrations for maximal activity, no action on: laminarin, dextran, heparin, chondroitin sulfate, pullulan, yeast mannan, lichenin or porphyran, slight amylase activity with amylose and glycogen, beta-elimination mechanism, three-step reaction
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additional information
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Substrates: nine amino acid block conserved in the N-terminus
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additional information
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Substrates: the first twenty amino acids are completely identical in Klebsiella pneumoniae and in Enterobacter cloacae, N-terminus
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additional information
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Substrates: L-tryptophan, L-histidine and L-lysine residues play an important role in enzymatic activity
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additional information
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A0A650FAR8
Substrates: the enzyme is an endo-type alginate lyase
Products: -
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additional information
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Substrates: nine amino acid conserved block at the C-termini, unrelated to substrate recognition but to maintenance of the stable three-dimensional conformation
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additional information
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Substrates: no activity with agar, agarose, and chondroitin B
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additional information
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Substrates: operates in a processive manner. It is able to catalyze cleavage adjacent to either mannuronate or guluronate residues in alginate
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additional information
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Substrates: 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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additional information
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Substrates: 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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additional information
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Substrates: the enzyme is active on poly(alpha-L-guluronate) and poly(beta-D-mannuronate), cf. EC 4.2.2.3
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additional information
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Substrates: 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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additional information
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Substrates: 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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additional information
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Substrates: 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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additional information
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Substrates: 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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additional information
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Substrates: exolytic and endolytic activity
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additional information
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Substrates: enzyme acts only on poly-guluronate
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additional information
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Substrates: enzyme prefers polyG blocks over polyM blocks
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additional information
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Substrates: isoform ZH0-I is an endo-type alginate lyase
Products: -
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additional information
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Substrates: isoform ZH0-I is an endo-type alginate lyase
Products: -
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additional information
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Substrates: isoform ZH0-II is an endo-type alginate lyase
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additional information
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Substrates: isoform ZH0-II is an endo-type alginate lyase
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additional information
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Substrates: 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
Products: -
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additional information
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Substrates: alginate, poly-mannuronate-, poly-guluronate-, and poly-mannuronate-guluronate-block substrates are used, substrate specificity, cf. EC 4.2.2.3, overview. No or poor activity with chondroitin B, agarose, agar, starch, and pectin
Products: -
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additional information
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Substrates: 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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additional information
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Substrates: alginate, poly-mannuronate-, poly-guluronate-, and poly-mannuronate-guluronate-block substrates are used, substrate specificity, cf. EC 4.2.2.3, overview. No or poor activity with chondroitin B, agarose, agar, starch, and pectin
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additional information
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Substrates: the enzyme acts as an endo-type alginate lyase
Products: -
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additional information
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Substrates: 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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Substrates: 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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Substrates: 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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Substrates: 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
Products: -
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additional information
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Substrates: the relative activities for alginate, M, G, and GM blocks are 100%, 75%, 21%, and 15%, respectively
Products: -
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additional information
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Substrates: the relative activities for alginate, M, G, and GM blocks are 100%, 75%, 21%, and 15%, respectively
Products: -
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additional information
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Substrates: the relative activities for alginate, M, G, and GM blocks are 100%, 75%, 21%, and 15%, respectively
Products: -
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additional information
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Substrates: the enzyme's catalytic domain CD2 is polyguluronate-specific
Products: -
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additional information
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A0A1Z2QRI2
Substrates: the enzyme's action mode is endolytic
Products: -
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additional information
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Substrates: the enzyme's action mode is endolytic
Products: -
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additional information
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Substrates: AlgB mainly releases oligosaccharides with a degree of polymersiation of 2-5 from the different kinds of substrates in an endolytic manner
Products: -
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additional information
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A3UR44
Substrates: isoforms AlyD and AlyE principally cleave the alpha-1,4 bonds involving alpha-L-guluronate subunits
Products: -
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additional information
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A3UT33
Substrates: isoforms AlyD and AlyE principally cleave the alpha-1,4 bonds involving alpha-L-guluronate subunits
Products: -
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additional information
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A0A2S7V3I3
Substrates: very little activity with poly(beta-(1->4)-D-mannuronic acid)
Products: -
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additional information
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A3UR44
Substrates: isoforms AlyD and AlyE principally cleave the alpha-1,4 bonds involving alpha-L-guluronate subunits
Products: -
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additional information
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A3UT33
Substrates: isoforms AlyD and AlyE principally cleave the alpha-1,4 bonds involving alpha-L-guluronate subunits
Products: -
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additional information
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A0A2S7V3I3
Substrates: very little activity with poly(beta-(1->4)-D-mannuronic acid)
Products: -
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additional information
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Substrates: alginate pentasaccharides that can be cleaved by AlyA1PL7 are GGGGG, GGMGG, GGGMG, and GGMMG
Products: -
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additional information
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Substrates: alginate pentasaccharides that can be cleaved by AlyA1PL7 are GGGGG, GGMGG, GGGMG, and GGMMG
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additional information
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Substrates: alginate pentasaccharides that can be cleaved by AlyA1PL7 are GGGGG, GGMGG, GGGMG, and GGMMG
Products: -
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additional information
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Substrates: the enzyme has a broad substrate tolerance and can cleave M-M, M-G, and G-G linkages at the nonreducing end. The activity is depending on the block structure
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additional information
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Substrates: the enzyme has a broad substrate tolerance and can cleave M-M, M-G, and G-G linkages at the nonreducing end. The activity is depending on the block structure
Products: -
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additional information
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Substrates: the enzyme has a broad substrate tolerance and can cleave M-M, M-G, and G-G linkages at the nonreducing end. The activity is depending on the block structure
Products: -
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additional information
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Substrates: alginate pentasaccharides that can be cleaved by AlyA1PL7 are GGGGG, GGMGG, GGGMG, and GGMMG
Products: -
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additional information
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Substrates: the enzyme has a broad substrate tolerance and can cleave M-M, M-G, and G-G linkages at the nonreducing end. The activity is depending on the block structure
Products: -
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Nakagawa, A.; Ozaki, T.; Chubachi, K.; Hosoyama, T.; Okubo, T.; Iyobe, S.; Suzuki, T.
An effective method for isolating alginate lyase-producing Bacillus sp. ATB-1015 strain and purification and characterization of the lyase
J. Appl. Microbiol.
84
328-335
1998
Bacillus sp. (in: firmicutes), Bacillus sp. (in: firmicutes) ATB-1015
brenda
Boyd, J.; Turvey, J.R.
Isolation of poly-alpha-L-guluronate lyase from Klebsiella aerogenes
Carbohydr. Res.
57
163-171
1977
Klebsiella aerogenes
brenda
Gacesa, P.
Alginate-modifying enzymes. A proposed unified mechanism of action for the lyases and epimerases
FEBS Lett.
212
199-202
1987
Klebsiella aerogenes
-
brenda
Lange, B.; Wingender, J.; Winkler, U.K.
Isolation and characterization of an alginate lyase from Klebsiella aerogenes
Arch. Microbiol.
152
302-308
1989
Klebsiella aerogenes
brenda
Hisano, T.; Nishimura, M.; Yamashita, T.; Imanaka, T.; Muramatsu, T.; Kimura, A.; Murata, K.
A simple method for determination of substrate specificity of alginate lyases
J. Ferment. Bioeng.
78
182-184
1994
Flavobacterium sp., Bacillus sp. (in: firmicutes)
-
brenda
Nibu, Y.; Satoh, T.; Nishi, Y.; Takeuchi, T.; Murata, K.; Kusakabe, I.
Purification and characterization of extracellular alginate lyase from Enterobacter cloacae M-1
Biosci. Biotechnol. Biochem.
59
632-637
1995
Enterobacter cloacae, Enterobacter cloacae M-1intracellular
brenda
Takeuchi, T.; Nibu, Y.; Murata, K.; Kusakabe, I.
Purification and characterization of endo poly (alpha-L-guluronate) lyase in the enzyme system from Flavobacterium multivorum
Food Sci. Technol. Int.
3
22-26
1997
Sphingobacterium multivorum, Sphingobacterium multivorum K-11
-
brenda
Matsubara, Y.; Kawada, R.; Iwasaki, K.; Oda, T.; Muramatsu, T.
Extracellular poly(alpha-L-guluronate)lyase from Corynebacterium sp.: purification, characteristics, and conformational properties
J. Protein Chem.
17
29-36
1998
Corynebacterium sp., Corynebacterium sp. ALY-1
brenda
Matsubara, Y.; Iwasaki, K.I.; Muramatsu, T.
Action of poly(alpha-L-guluronate) lyase from Corynebacterium sp. ALY-1 strain on saturated oligoguluronates
Biosci. Biotechnol. Biochem.
62
1055-1060
1998
Corynebacterium sp., Corynebacterium sp. ALY-1
brenda
Ostgaard, K.; Knutsen, S.H.; Dyrset, N.; Aasen, I.M.
Production and characterization of guluronate lyase from Klebsiella pneumoniae for applications in seaweed biotechnology
Enzyme Microb. Technol.
15
756-763
1993
Klebsiella pneumoniae
brenda
Shimokawa, T.; Yoshida, S.; Kusakabe, I.
Effects of unsaturated uronic acid residues at non-reducing end on bond cleavage frequency of poly(1,4-alpha-L-guluronide) lyase from Enterobacter cloacae M-1
Biosci. Biotechnol. Biochem.
62
164-166
1998
Enterobacter cloacae, Enterobacter cloacae M-1intracellular, Sphingobacterium multivorum, Sphingobacterium multivorum K-11
-
brenda
Wong, T.Y.; Preston, L.A.; Schiller, N.L.
Alginate lyase: review of major sources and enzyme characteristics, structure-function analysis, biological roles, and applications
Annu. Rev. Microbiol.
54
289-340
2000
Bacillus sp. (in: firmicutes), Corynebacterium sp., Corynebacterium sp. (Q9RB42), Enterobacter cloacae, Klebsiella pneumoniae, Pseudoalteromonas distincta (Q9Z6D6), Pseudomonas aeruginosa, Pseudomonas sp., Sargassum sp., Sphingobacterium multivorum, Vibrio harveyi, Vibrio harveyi AL-128, Vibrio sp.
brenda
Iwamoto, Y.; Araki, R.; Iriyama, K.; Oda, T.; Fukuda, H.; Hayashida, S.; Muramatsu, T.
Purification and characterization of bifunctional alginate lyase from Alteromonas sp. strain no. 272 and its action on saturated oligomeric substrates
Biosci. Biotechnol. Biochem.
65
133-142
2001
Alteromonas sp., Alteromonas sp. 272
brenda
Miyazaki, M.; Obata, J.; Iwamoto, Y.; Oda, T.; Muramatsu, T.
Calcium-sensitive extracellular poly(alpha-L-guluronate) lyase from a marine bacterium Pseudomonas sp. strain F6: Purification and some properties
Fish. Sci.
67
956-964
2001
Pseudomonas sp., Pseudomonas sp. F6
-
brenda
Yamasaki, M.; Moriwaki, S.; Hashimoto, W.; Mikami, B.; Murata, K.
Crystallization and preliminary X-ray analysis of alginate lyase, a member of family PL-7, from Pseudomonas aeruginosa
Acta Crystallogr. Sect. D
59
1499-1501
2003
Pseudomonas aeruginosa
brenda
Yamasaki, M.; Ogura, K.; Moriwaki, S.; Hashimoto, W.; Murata, K.; Mikami, B.
Crystallization and preliminary X-ray analysis of alginate lyases A1-II and A1-II' from Sphingomonas sp. A1
Acta Crystallogr. Sect. F
61
288-290
2005
Sphingomonas sp.
brenda
Osawa, T.; Matsubara, Y.; Muramatsu, T.; Kimura, M.; Kakuta, Y.
Crystal structure of the alginate (poly alpha-l-guluronate) lyase from Corynebacterium sp. at 1.2 A resolution
J. Mol. Biol.
345
1111-1118
2005
Corynebacterium sp. (Q9RB42)
brenda
Coulson-Thomas, Y.M.; Coulson-Thomas, V.J.; Filippo, T.R.; Mortara, R.A.; da Silveira, R.B.; Nader, H.B.; Porcionatto, M.A.
Adult bone marrow-derived mononuclear cells expressing chondroitinase AC transplanted into CNS injury sites promote local brain chondroitin sulphate degradation
J. Neurosci. Methods
171
19-29
2008
Agarivorans sp.
brenda
Matsushima, R.; Danno, H.; Uchida, M.; Ishihara, K.; Suzuki, T.; Kaneniwa, M.; Ohtsubo, Y.; Nagata, Y.; Tsuda, M.
Analysis of extracellular alginate lyase and its gene from a marine bacterial strain, Pseudoalteromonas atlantica AR06
Appl. Microbiol. Biotechnol.
86
567-576
2010
Pseudoalteromonas atlantica (D1MX66), Pseudoalteromonas atlantica AR06 (D1MX66)
brenda
Ochiai, A.; Yamasaki, M.; Mikami, B.; Hashimoto, W.; Murata, K.
Crystal structure of exotype alginate lyase Atu3025 from Agrobacterium tumefaciens
J. Biol. Chem.
285
24519-24528
2010
Agrobacterium tumefaciens (A9CEJ9)
brenda
Uchimura, K.; Miyazaki, M.; Nogi, Y.; Kobayashi, T.; Horikoshi, K.
Cloning and sequencing of alginate lyase genes from deep-sea strains of Vibrio and Agarivorans and characterization of a new Vibrio enzyme
Mar. Biotechnol.
12
526-533
2010
Vibrio sp. (C4TJD4), Vibrio sp. (C4TJD2), Vibrio sp. (C4TJD3), Vibrio sp. A9m (C4TJD4), Vibrio sp. A9m (C4TJD2), Vibrio sp. A9m (C4TJD3)
brenda
Inoue, A.; Mashino, C.; Kodama, T.; Ojima, T.
Protoplast preparation from Laminaria japonica with recombinant alginate lyase and cellulase
Mar. Biotechnol.
13
256-263
2011
Haliotis discus hannai
brenda
Li, L.; Jiang, X.; Guan, H.; Wang, P.; Guo, H.
Three alginate lyases from marine bacterium Pseudomonas fluorescens HZJ216: Purification and characterization
Appl. Biochem. Biotechnol.
164
305-317
2011
Pseudomonas fluorescens, Pseudomonas fluorescens HZJ216
brenda
Li, L.; Jiang, X.; Guan, H.; Wang, P.
Preparation, purification and characterization of alginate oligosaccharides degraded by alginate lyase from Pseudomonas sp. HZJ 216
Carbohydr. Res.
346
794-800
2011
Pseudomonas sp., Pseudomonas sp. HZJ 216
brenda
Tang, J.; Zhou, Q.; Chu, H.; Nagata, S.
Characterization of alginase and elicitor-active oligosaccharides from Gracilibacillus A7 in alleviating salt stress for Brassica campestris L
J. Agric. Food Chem.
59
7896-7901
2011
Gracilibacillus sp.
brenda
Singh, R.; Gupta, V.; Kumari, P.; Kumar, M.; Reddy, C.; Prasad, K.; Jha, B.
Purification and partial characterization of an extracellular alginate lyase from Aspergillus oryzae isolated from brown seaweed
J. Appl. Phycol.
23
755-762
2011
Aspergillus oryzae
-
brenda
Tondervik, A.; Klinkenberg, G.; Aarstad, O.; Drablos, F.; Ertesvag, H.; Ellingsen, T.; Skjak-Brak, G.; Valla, S.; Sletta, H.
Isolation of mutant alginate lyases with cleavage specificity for Di-guluronic acid linkages
J. Biol. Chem.
285
35284-35292
2010
Klebsiella pneumoniae
brenda
Park, H.; Kam, N.; Lee, E.; Kim, H.
Cloning and characterization of a novel oligoalginate lyase from a newly isolated bacterium Sphingomonas sp. MJ-3
Mar. Biotechnol.
14
189-202
2012
Sphingomonas sp. (G1EH67)
brenda
Li, J.; Dong, S.; Song, J.; Li, C.; Chen, X.; Xie, B.; Zhang, Y.
Purification and characterization of a bifunctional alginate lyase from Pseudoalteromonas sp. SM0524
Mar. Drugs
9
109-123
2011
Pseudoalteromonas sp.
brenda
Kim, H.T.; Chung, J.H.; Wang, D.; Lee, J.; Woo, H.C.; Choi, I.G.; Kim, K.H.
Depolymerization of alginate into a monomeric sugar acid using Alg17C, an exo-oligoalginate lyase cloned from Saccharophagus degradans 2-40
Appl. Microbiol. Biotechnol.
93
2233-2239
2012
Saccharophagus degradans (Q21FJ0), Saccharophagus degradans 2-40 / ATCC 43961 (Q21FJ0)
brenda
Lee, S.I.; Choi, S.H.; Lee, E.Y.; Kim, H.S.
Molecular cloning, purification, and characterization of a novel polyMG-specific alginate lyase responsible for alginate MG block degradation in Stenotrophomas maltophilia KJ-2
Appl. Microbiol. Biotechnol.
95
1643-1653
2012
Stenotrophomonas maltophilia (I6P4V6), Stenotrophomonas maltophilia KJ-2 (I6P4V6)
brenda
Farrell, E.K.; Tipton, P.A.
Functional characterization of AlgL, an alginate lyase from Pseudomonas aeruginosa
Biochemistry
51
10259-10266
2012
Pseudomonas aeruginosa
brenda
Kim, H.T.; Ko, H.J.; Kim, N.; Kim, D.; Lee, D.; Choi, I.G.; Woo, H.C.; Kim, M.D.; Kim, K.H.
Characterization of a recombinant endo-type alginate lyase (Alg7D) from Saccharophagus degradans
Biotechnol. Lett.
34
1087-1092
2012
Saccharophagus degradans
brenda
Wang, Y.; Guo, E.W.; Yu, W.G.; Han, F.
Purification and characterization of a new alginate lyase from a marine bacterium Vibrio sp.
Biotechnol. Lett.
35
703-708
2013
Vibrio sp., Vibrio sp. QY105
brenda
Kam, N.; Park, Y.J.; Lee, E.Y.; Kim, H.S.
Molecular identification of a polyM-specific alginate lyase from Pseudomonas sp. strain KS-408 for degradation of glycosidic linkages between two mannuronates or mannuronate and guluronate in alginate
Can. J. Microbiol.
57
1032-1041
2011
Pseudomonas sp. (G9J5R3)
brenda
Dou, W.; Wei, D.; Li, H.; Li, H.; Rahman, M.M.; Shi, J.; Xu, Z.; Ma, Y.
Purification and characterisation of a bifunctional alginate lyase from novel Isoptericola halotolerans CGMCC 5336
Carbohydr. Polym.
98
1476-1482
2013
Isoptericola halotolerans, Isoptericola halotolerans (AB489222), Isoptericola halotolerans CGMCC 5336, Isoptericola halotolerans CGMCC5336 (AB489222)
brenda
SilChenko, A.; Kusaikin, M.; Zakharenko, A.; Zvyagintseva, T.
Isolation from the marine mollusk Lambis sp. and catalytic properties of an alginate lyase with rare substrate specificity
Chem. Nat. Compd.
49
215-218
2013
Lambis sp. AAB-2014
-
brenda
Thomas, F.; Lundqvist, L.C.; Jam, M.; Jeudy, A.; Barbeyron, T.; Sandstroem, C.; Michel, G.; Czjzek, M.
Comparative characterization of two marine alginate lyases from Zobellia galactanivorans reveals distinct modes of action and exquisite adaptation to their natural substrate
J. Biol. Chem.
288
23021-23037
2013
Zobellia galactanivorans (G0KZG8), Zobellia galactanivorans (G0L2Y1), Zobellia galactanivorans, Zobellia galactanivorans DSM 12802 (G0KZG8)
brenda
Park, D.; Jagtap, S.; Nair, S.K.
Structure of a PL17 family alginate lyase demonstrates functional similarities among exotype depolymerases
J. Biol. Chem.
289
8645-8655
2014
Saccharophagus degradans (Q21FJ0)
brenda
Sim, S.J.; Baik, K.S.; Park, S.C.; Choe, H.N.; Seong, C.N.; Shin, T.S.; Woo, H.C.; Cho, J.Y.; Kim, D.
Characterization of alginate lyase gene using a metagenomic library constructed from the gut microflora of abalone
J. Ind. Microbiol. Biotechnol.
39
585-593
2012
uncultured bacterium (G3LI08)
brenda
Huang, L.; Zhou, J.; Li, X.; Peng, Q.; Lu, H.; Du, Y.
Characterization of a new alginate lyase from newly isolated Flavobacterium sp. S20
J. Ind. Microbiol. Biotechnol.
40
113-122
2013
Flavobacterium sp. (G9CHX6)
brenda
Sakatoku, A.; Tanaka, D.; Nakamura, S.
Purification and characterization of an alkaliphilic alginate lyase AlgMytC from Saccharophagus sp. Myt-1
J. Microbiol. Biotechnol.
23
872-877
2013
Saccharophagus sp. Myt-1 (L8B3Z6)
brenda
Ravanal, M.; Sharma, S.; Gimpel, J.; Reveco-Urzua, F.; Overland, M.; Horn, S.; Lienqueo, M.
The role of alginate lyases in the enzymatic saccharification of brown macroalgae, Macrocystis pyrifera and Saccharina latissima
Algal Res.
26
287-293
2017
Microbulbifer sp. 6532A (E7FLJ9), Pseudoalteromonas distincta (Q9Z6D6)
-
brenda
Badur, A.H.; Jagtap, S.S.; Yalamanchili, G.; Lee, J.K.; Zhao, H.; Rao, C.V.
Alginate lyases from alginate-degrading Vibrio splendidus 12B01 are endolytic
Appl. Environ. Microbiol.
81
1865-1873
2015
Vibrio splendidus (A3UR44), Vibrio splendidus (A3UT33), Vibrio splendidus 12B01 (A3UR44), Vibrio splendidus 12B01 (A3UT33)
brenda
Han, W.; Gu, J.; Cheng, Y.; Liu, H.; Li, Y.; Li, F.
Novel alginate lyase (Aly5) from a polysaccharide-degrading marine bacterium, Flammeovirga sp. strain MY04 effects of module truncation on biochemical characteristics, alginate degradation patterns, and oligosaccharide-yielding properties
Appl. Environ. Microbiol.
82
364-374
2016
Flammeovirga sp. MY04 (A0A0M4N5N7)
brenda
Cheng, Y.; Wang, D.; Gu, J.; Li, J.; Liu, H.; Li, F.; Han, W.
Biochemical characteristics and variable alginate-degrading modes of a novel bifunctional endolytic alginate lyase
Appl. Environ. Microbiol.
83
e01608
2017
Flammeovirga sp. MY04 (A0A1B1FUW4)
brenda
Yagi, H.; Fujise, A.; Itabashi, N.; Ohshiro, T.
Purification and characterization of a novel alginate lyase from the marine bacterium Cobetia sp. NAP1 isolated from brown algae
Biosci. Biotechnol. Biochem.
80
2338-2346
2016
Cobetia sp. NAP1
brenda
Zhu, B.; Ni, F.; Sun, Y.; Yao, Z.
Expression and characterization of a new heat-stable endo-type alginate lyase from deep-sea bacterium Flammeovirga sp. NJ-04
Extremophiles
21
1027-1036
2017
Flammeovirga sp. NJ-04 (A0A1Z2QRE2)
brenda
Peng, C.; Wang, Q.; Lu, D.; Han, W.; Li, F.
A novel bifunctional endolytic alginate lyase with variable alginate-degrading modes and versatile monosaccharide-producing properties
Front. Microbiol.
9
167
2018
Flammeovirga sp. MY04 (A0A1B1FUS6)
brenda
Yu, Z.; Zhu, B.; Wang, W.; Tan, H.; Yin, H.
Characterization of a new oligoalginate lyase from marine bacterium Vibrio sp.
Int. J. Biol. Macromol.
112
937-942
2018
Vibrio sp. W13 (A0A0F7KQI4)
brenda
Zhu, B.; Ni, F.; Ning, L.; Sun, Y.; Yao, Z.
Cloning and characterization of a new pH-stable alginate lyase with high salt tolerance from marine Vibrio sp. NJ-04
Int. J. Biol. Macromol.
115
1063-1070
2018
Vibrio sp. NJ-04 (A0A1Z2QRD5)
brenda
Zhu, B.; Tan, H.; Qin, Y.; Xu, Q.; Du, Y.; Yin, H.
Characterization of a new endo-type alginate lyase from Vibrio sp. W13
Int. J. Biol. Macromol.
75
330-337
2015
Vibrio sp. W13 (A0A0A1DYR7)
brenda
Tavafi, H.; Abdi-Ali, A.; Ghadam, P.; Gharavi, S.
Screening of alginate lyase-producing bacteria and optimization of media compositions for extracellular alginate lyase production
Iran. Biomed. J.
21
48-56
2017
Bacillus sp. TAG8 (A0A0H3WC39)
brenda
Yagi, H.; Fujise, A.; Itabashi, N.; Ohshiro, T.
Characterization of a novel endo-type alginate lyase derived from Shewanella sp. YH1
J. Biochem.
163
341-350
2018
Shewanella sp. YH1
brenda
Zhu, B.; Ning, L.; Jiang, Y.; Ge, L.
Biochemical characterization and degradation pattern of a novel endo-type bifunctional alginate lyase AlyA from marine bacterium Isoptericola halotolerans
Mar. Drugs
16
258
2018
Isoptericola halotolerans (A0A346FH09), Isoptericola halotolerans NJ-05 (A0A346FH09)
brenda
Zhu, Y.; Wu, L.; Chen, Y.; Ni, H.; Xiao, A.; Cai, H.
Characterization of an extracellular biofunctional alginate lyase from marine Microbulbifer sp. ALW1 and antioxidant activity of enzymatic hydrolysates
Microbiol. Res.
182
49-58
2016
Microbulbifer sp. ALW1
brenda
Pei, X.; Chang, Y.; Shen, J.
Cloning, expression and characterization of an endo-acting bifunctional alginate lyase of marine bacterium Wenyingzhuangia fucanilytica
Protein Expr. Purif.
154
44-51
2019
Wenyingzhuangia fucanilytica (A0A1B1Y7V0)
brenda
Manns, D.; Nyffenegger, C.; Saake, B.; Meyer, A.
Impact of different alginate lyases on combined cellulase-lyase saccharification of brown seaweed
RSC Adv.
6
45392-45401
2016
Flavobacterium sp. S20 (G9CHX6), Sphingobacterium multivorum, Sphingomonas sp. A1 (Q75WP3)
-
brenda
Sim, P.; Furusawa, G.; Teh, A.
Functional and structural studies of a multidomain alginate lyase from Persicobacter sp. CCB-QB2
Sci. Rep.
7
13656
2017
Persicobacter sp. CCB-QB2 (A0A3B6UEP6)
brenda
Wang, X.H.; Sun, X.H.; Chen, X.L.; Li, P.Y.; Qin, Q.L.; Zhang, Y.Q.; Xu, F.
Synergy of the two alginate lyase domains of a novel alginate lyase from Vibrio sp. NC2 in alginate degradation
Appl. Environ. Microbiol.
88
e0155922
2022
Vibrio sp. NC2
brenda
Yang, M.; Li, N.; Yang, S.; Yu, Y.; Han, Z.; Li, L.; Mou, H.
Study on expression and action mode of recombinant alginate lyases based on conserved domains reconstruction
Appl. Microbiol. Biotechnol.
103
807-817
2019
Microbulbifer sp. Q7
brenda
Lyu, Q.; Zhang, K.; Shi, Y.; Li, W.; Diao, X.; Liu, W.
Structural insights into a novel Ca2+-independent PL-6 alginate lyase from Vibrio OU02 identify the possible subsites responsible for product distribution
Biochim. Biophys. Acta Gen. Subj.
1863
1167-1176
2019
Vibrio splendidus (A0A2S7V3I3), Vibrio splendidus OU02 (A0A2S7V3I3)
brenda
Zhu, B.; Ni, F.; Sun, Y.; Ning, L.; Yao, Z.
Elucidation of degrading pattern and substrate recognition of a novel bifunctional alginate lyase from Flammeovirga sp. NJ-04 and its use for preparation alginate oligosaccharides
Biotechnol. Biofuels
12
13
2019
Flammeovirga sp. NJ-04 (A0A291NNN1)
brenda
Chen, Y.; Dou, W.; Li, H.; Shi, J.; Xu, Z.
The alginate lyase from Isoptericola halotolerans CGMCC 5336 as a new tool for the production of alginate oligosaccharides with guluronic acid as reducing end
Carbohydr. Res.
470
36-41
2018
Isoptericola halotolerans, Isoptericola halotolerans CGMCC 5336
brenda
Zheng, K.; Zhu, Y.; An, Z.; Lin, J.; Shan, S.; Zhang, H.
Cloning, Expression and characterization of an alginate lyase in Bacillus subtilis WB600
Fermentation
9
144
2023
Vibrio alginolyticus
-
brenda
Zhu, B.; Sun, Y.; Ni, F.; Ning, L.; Yao, Z.
Characterization of a new endo-type alginate lyase from Vibrio sp. NJU-03
Int. J. Biol. Macromol.
108
1140-1147
2018
Vibrio sp. NJU-03 (A0A1Z2QRI2)
brenda
Tang, L.; Bao, M.; Wang, Y.; Fu, Z.; Han, F.; Yu, W.
Effects of module truncation of a new alginate lyase VxAly7C from marine Vibrio xiamenensis QY104 on biochemical characteristics and product distribution
Int. J. Mol. Sci.
23
4795
2021
Vibrio xiamenensis, Vibrio xiamenensis QY104
brenda
He, M.; Guo, M.; Zhang, X.; Chen, K.; Yan, J.; Irbis, C.
Purification and characterization of alginate lyase from Sphingomonas sp. ZH0
J. Biosci. Bioeng.
126
310-316
2018
Sphingomonas sp. ZH0 (L0GEW5), Sphingomonas sp. ZH0 (X2C723)
brenda
Xie, M.; Li, J.; He, P.; Lin, X.
Expression and characterization of a bifunctional alginate lyase named Al163 from the Antarctic bacterium Pseudoalteromonas sp. NJ-21
J. Oceanol. Limnol.
36
1304-1314
2018
Pseudoalteromonas sp. NJ-21
-
brenda
Yan, F.; Chen, J.; Cai, T.; Zhong, J.; Zhang, S.
Cloning, expression, and characterization of a novel endo-type alginate lyase from Microbulbifer sp. BY17
J. Sci. Food Agric.
102
4522-4531
2022
Microbulbifer sp. BY17 (A0A1Y0SY54)
brenda
Wang, Y.; Chen, X.; Bi, X.; Ren, Y.; Han, Q.; Zhou, Y.; Han, Y.; Yao, R.; Li, S.
Characterization of an alkaline alginate lyase with pH-stable and thermo-tolerance property
Mar. Drugs
17
308
2019
Vibrio sp. SY01
brenda
Yan, J.; Chen, P.; Zeng, Y.; Men, Y.; Mu, S.; Zhu, Y.; Chen, Y.; Sun, Y.
The characterization and modification of a novel bifunctional and robust alginate lyase derived from Marinimicrobium sp. H1
Mar. Drugs
17
545
2019
Marinimicrobium sp. H1 (A0A650FAR8)
brenda
Wang, Z.P.; Cao, M.; Li, B.; Ji, X.F.; Zhang, X.Y.; Zhang, Y.Q.; Wang, H.Y.
Cloning, secretory expression and characterization of a unique ph-stable and cold-adapted alginate lyase
Mar. Drugs
18
189
2020
Vibrio sp. W2
brenda
Zhou, H.X.; Xu, S.S.; Yin, X.J.; Wang, F.L.; Li, Y.
Characterization of a new bifunctional and cold-adapted polysaccharide lyase (PL) family 7 alginate lyase from Flavobacterium sp
Mar. Drugs
18
388
2020
Flavobacterium sp. (A0A7G4RN99)
brenda
Ma, Y.; Li, J.; Zhang, X.Y.; Ni, H.D.; Wang, F.B.; Wang, H.Y.; Wang, Z.P.
Characterization of a new intracellular alginate lyase with metal ions-tolerant and pH-stable properties
Mar. Drugs
18
416
2020
Vibrio sp. W2 (A0A7U3T8H1)
brenda
Zhang, Y.H.; Shao, Y.; Jiao, C.; Yang, Q.M.; Weng, H.F.; Xiao, A.F.
Characterization and application of an alginate lyase, Aly1281 from marine bacterium Pseudoalteromonas carrageenovora ASY5
Mar. Drugs
18
95
2020
Pseudoalteromonas carrageenovora, Pseudoalteromonas carrageenovora ASY5
brenda
Nguyen, T.N.T.; Chataway, T.; Araujo, R.; Puri, M.; Franco, C.M.M.
Purification and characterization of a novel alginate lyase from a marine Streptomyces species isolated from seaweed
Mar. Drugs
19
590
2021
Streptomyces luridiscabiei
brenda