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Information on EC 4.2.2.11 - guluronate-specific alginate lyase
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EC Tree
4.2.2.11 guluronate-specific alginate lyaseIUBMB Comments
The enzyme catalyses the degradation of alginate by a beta-elimination reaction. It cleaves the (1->4) bond between alpha-L-guluronate and either alpha-L-guluronate or beta-D-mannuronate, generating oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and alpha-L-guluronate at the reducing end. Depending on the composition of the substrate, the enzyme produces oligosaccharides ranging from two to six residues, with preference for shorter products. cf. EC 4.2.2.3, mannuronate-specific alginate lyase.
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Word Map
- 4.2.2.11
- lyases
- degradation
-
klebsiella
- unsaturated
- polysaccharide
-
endolytic
- pneumoniae
-
depolymerization
- synthesis
- aerogenes
- flavobacterium
-
4.2.2.3
- tetrasaccharide
- algae
-
terrestrial
-
mannuronate
- sphingomonas
- biomass
- biofuel production
- agriculture
- industry
- food industry
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
algmytc, guluronate-specific alginate lyase, guluronate lyase, alya1pl7, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A9mC
A9mL
A9mT
Alg17C
Alg2A
alginase II
-
-
-
-
alginate lyase
Aly1
AlyA
AlyA1PL7
AlyA5
AlyD
AlyE
AlyV5
guluronate lyase
-
-
-
-
L-guluronan lyase
-
-
-
-
L-guluronate lyase
-
-
-
-
lyase, polyguluronate
-
-
-
-
poly(1,4-alpha-L-guluronide)lyase
-
-
-
-
poly(alpha-L-guluronate) lyase
-
-
-
-
poly-alpha-L-guluronate lyase
-
-
-
-
polyguluronate-specific alginate lyase
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-
-
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polyMG-specific alginate lyase
V12B01_09446
V12B01_24274
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[alpha-1,4-L-guluronate]n = alpha-L-guluronate + 4-deoxy-alpha-L-erythro-hex-4-enuronosyl-[alpha-1,4-L-guluronate]n-2
[alpha-1,4-L-guluronate]n = alpha-L-guluronate + 4-deoxy-alpha-L-erythro-hex-4-enuronosyl-[alpha-1,4-L-guluronate]n-2
-
-
-
-
[alpha-1,4-L-guluronate]n = alpha-L-guluronate + 4-deoxy-alpha-L-erythro-hex-4-enuronosyl-[alpha-1,4-L-guluronate]n-2
AlyA1PL7 alginate lyase acts via the beta-elimination mechanism, producing the 4,5-unsaturated 4-deoxy-L-erythro-hex-4-enepyranosyluronate (DELTA) on the nonreducing end, catalytic mechanism of G-specific alginate lyases, overview
[alpha-1,4-L-guluronate]n = alpha-L-guluronate + 4-deoxy-alpha-L-erythro-hex-4-enuronosyl-[alpha-1,4-L-guluronate]n-2
AlyA1PL7 alginate lyase acts via the beta-elimination mechanism, producing the 4,5-unsaturated 4-deoxy-L-erythro-hex-4-enepyranosyluronate (DELTA) on the nonreducing end, catalytic mechanism of guluronate-specific alginate lyases, overview
[alpha-1,4-L-guluronate]n = alpha-L-guluronate + 4-deoxy-alpha-L-erythro-hex-4-enuronosyl-[alpha-1,4-L-guluronate]n-2
substrate binding, structural change and exolytic mechanism of alginate depolymerization by Alg17c, overview
[alpha-1,4-L-guluronate]n = alpha-L-guluronate + 4-deoxy-alpha-L-erythro-hex-4-enuronosyl-[alpha-1,4-L-guluronate]n-2
substrate binding, structural change and exolytic mechanism of alginate depolymerization by Alg17c, overview
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[alpha-1,4-L-guluronate]n = alpha-L-guluronate + 4-deoxy-alpha-L-erythro-hex-4-enuronosyl-[alpha-1,4-L-guluronate]n-2
AlyA1PL7 alginate lyase acts via the beta-elimination mechanism, producing the 4,5-unsaturated 4-deoxy-L-erythro-hex-4-enepyranosyluronate (DELTA) on the nonreducing end, catalytic mechanism of guluronate-specific alginate lyases, overview
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[alpha-1,4-L-guluronate]n = alpha-L-guluronate + 4-deoxy-alpha-L-erythro-hex-4-enuronosyl-[alpha-1,4-L-guluronate]n-2
AlyA1PL7 alginate lyase acts via the beta-elimination mechanism, producing the 4,5-unsaturated 4-deoxy-L-erythro-hex-4-enepyranosyluronate (DELTA) on the nonreducing end, catalytic mechanism of G-specific alginate lyases, overview
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
elimination of an alcohol from a polysaccharide
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-
-
-
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SYSTEMATIC NAME
IUBMB Comments
alginate alpha-L-guluronate-uronate lyase
The enzyme catalyses the degradation of alginate by a beta-elimination reaction. It cleaves the (1->4) bond between alpha-L-guluronate and either alpha-L-guluronate or beta-D-mannuronate, generating oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and alpha-L-guluronate at the reducing end. Depending on the composition of the substrate, the enzyme produces oligosaccharides ranging from two to six residues, with preference for shorter products. cf. EC 4.2.2.3, mannuronate-specific alginate lyase.
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CAS REGISTRY NUMBER
COMMENTARY
64177-88-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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-L-1,4-guluronate)
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)
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-mannuronic acid)
?
preferred over poly(alpha-(1->4)-L-guluronic acid)
-
-
?
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
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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)
-
-
-
?
poly-alpha-L-guluronic acid
4-deoxy-erythro-hex-4-ene pyranosyluronate + ?
degradation of alginate
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-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
saturated hexa((1-4)-alpha-L-guluronan)
saturated di((1-4)-alpha-L-guluronan) + unsaturated tetra((1-4)-alpha-L-guluronan)
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-
-
?
saturated penta((1-4)-alpha-L-guluronan)
saturated di((1-4)-alpha-L-guluronan) + unsaturated tri((1-4)-alpha-L-guluronan)
unsaturated hexa((1-4)-alpha-L-guluronan)
unsaturated triguluronic acid + unsaturated tetraguluronic acid
alginate
?
-
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
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-
?
alginate
?
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high yields of penta-, hex-, and heptasaccharides in the hydrolysis products
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?
alginate
?
AB489222
the bifunctional alginate lyase shows substrate specificity for poly(alpha-L-guluronate) and poly(beta-D-mannuronate) units in alginate molecules, cf. EC 4.2.2.3
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-
?
alginate
?
AB489222
enzyme shows specificity for polyguluronate and polymannuronate units in alginate molecules
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-
?
alginate
?
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enzyme shows specificity for polyguluronate and polymannuronate units in alginate molecules
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-
?
alginate
?
AB489222
the bifunctional alginate lyase shows substrate specificity for poly(alpha-L-guluronate) and poly(beta-D-mannuronate) units in alginate molecules, cf. EC 4.2.2.3
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-
?
alginate
?
-
enzyme cleaves the glycosidic linkages between two mannuronates (mannuronate-beta(1-4)-mannuronate) or mannuronate and guluronate (mannuronate-beta(1-4)-guluronate)
-
?
alginate
?
-
enzyme cleaves the glycosidic linkages between two mannuronates (mannuronate-beta(1-4)-mannuronate) or mannuronate and guluronate (mannuronate-beta(1-4)-guluronate)
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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
?
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
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-
?
alginate
?
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enzyme degrades alginate into a mixture of products with molecular masses below 1000 Da
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?
alginate
unsaturated algino-oligosaccharides
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-
-
?
alginate
unsaturated algino-oligosaccharides
best substrate
-
-
?
alginate
unsaturated algino-oligosaccharides
Shewanella sp. YH1
-
about 50% of the activity with poly(alpha-(1,4)-L-guluronate)
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-
?
alpha-L-guluronosyl linkage in alginate
?
-
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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-
?
alpha-L-guluronosyl linkage in alginate
?
-
significant activity is found not only on guluronate-guluronate linkages but also on guluronate-mannuronate linkages
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-
?
alpha-L-guluronosyl linkage in alginate
?
-
endolyase
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-
?
alpha-L-guluronosyl linkage in alginate
?
-
significant activity is found not only on guluronate-guluronate linkages but also on guluronate-mannuronate linkages
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-
?
alpha-L-guluronosyl linkage in alginate
?
-
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
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-
?
alpha-L-guluronosyl linkage in alginate
?
-
significant activity is found not only on guluronate-guluronate linkages but also on guluronate-mannuronate linkages
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?
alpha-L-guluronosyl linkage in alginate
?
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enzyme shows activities toward both polyG, i.e. poly-alpha-(1->4)-L-guluronic acid, and polyM, i.e. poly-beta-D-mannuronic acid
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?
alpha-L-guluronosyl linkage in alginate
?
-
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
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-
?
alpha-L-guluronosyl linkage in alginate
?
-
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
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-
?
alpha-L-guluronosyl linkage in alginate
?
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-
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
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?
alpha-L-guluronosyl linkage in alginate
?
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-
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
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?
alpha-L-guluronosyl linkage in alginate
?
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endolyase
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?
alpha-L-guluronosyl linkage in alginate
?
-
final degradation products are alginate monosaccharides
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?
alpha-L-guluronosyl linkage in alginate
?
-
final degradation products are alginate monosaccharides
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?
alpha-L-guluronosyl linkage in alginate
?
preferably degrades G blocks
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?
alpha-L-guluronosyl linkage in alginate
?
preferably degrades the M block to the G block in alginate
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?
alpha-L-guluronosyl linkage in alginate
?
preferably degrades the M block to the G block in alginate
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?
alpha-L-guluronosyl linkage in alginate
?
preferably degrades G blocks
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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)
Cobetia sp. NAP1
-
-
-
-
?
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)
Flammeovirga sp. NJ-04
reaction of EC 4.2.2.11
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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)
-
-
-
?
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)
-
-
-
-
?
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 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)
Shewanella sp. YH1
-
-
-
-
?
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)
-
-
-
?
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)
Vibrio sp. NJ-04
-
-
-
?
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)
-
-
-
?
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-guluronic acid)
?
preferred over poly-(beta1,4-D-mannuronan)
-
-
?
poly(alpha-(1->4)-L-guluronic acid)
?
90% of the activity with alginate
-
-
?
poly(alpha-(1->4)-L-guluronic acid)
?
-
108% of the activity with alginate
main products are disaccharide, trisaccharide and tetrasaccharide
-
?
poly(alpha-L-guluronate)
?
unmodified substrate poly-G blocks and substrate that with its reducing end being reduced using sodium borohydride prior to the digestion
-
-
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
Cobetia sp. NAP1
-
reaction of EC 4.2.2.3
-
-
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
Flammeovirga sp. NJ-04
-
-
-
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
reaction of EC 4.2.2.3
-
-
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
reaction of EC 4.2.2.3
-
-
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
-
reaction of EC 4.2.2.3, 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)
reaction of EC 4.2.2.3, 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)
Shewanella sp. YH1
-
reaction of EC 4.2.2.3, about 20% of the activity with poly(alpha-(1,4)-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)
reaction of EC 4.2.2.3
-
-
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
Vibrio sp. NJ-04
reaction of EC 4.2.2.3
-
-
?
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)
reaction of EC 4.2.2.3
-
-
?
poly(beta-(1,4)-D-mannuronate)
4-deoxy-alpha-L-erythro-hex-4-enopyranuronosyl-(1,4)-beta-oligo(beta-(1,4)-D-mannuronate)
reaction of EC 4.2.2.3
-
-
?
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)
Cobetia sp. NAP1
-
-
-
-
?
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)
Shewanella sp. YH1
-
about 30% of the activity with poly(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-D-mannuronic acid/alpha-(1->4)-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-D-mannuronic acid/alpha-(1->4)-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-mannuronan)
?
-
Km value decreases with increasing substrate length, and kcat/Km increases. Oligomers containing fewer than 9-10 residues are not substrates
-
-
?
poly-(beta-(1->4)-D-mannuronan)
?
-
30% of the activity with alginate
main products are trisaccharide, tetrasaccharide and pentasaccharide
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
Bacillus sp. (in: Bacteria) ATB-1015
-
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
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
-
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
-
?
poly-beta1,4-D-mannuronan
?
-
seems to have slight activity on poly-mannuronan
-
-
?
poly-beta1,4-D-mannuronan
?
Bacillus sp. (in: Bacteria) ATB-1015
-
seems to have slight activity on poly-mannuronan
-
-
?
saturated hexa((1-4)-alpha-L-guluronan)
unsaturated tetramer and a saturated dimer
-
-
-
-
?
saturated hexa((1-4)-alpha-L-guluronan)
unsaturated tetramer and a saturated dimer
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
-
-
?
saturated hexa((1-4)-alpha-L-guluronan)
unsaturated tetramer and a saturated dimer
-
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
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
-
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
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)
?
-
degraded slower than unsaturated oligoguluronans with the same degree of polymerization, completely different cleavage pattern
-
-
?
saturated penta((1-4)-alpha-L-guluronan)
?
-
degraded slower than unsaturated oligoguluronans with the same degree of polymerization, completely different cleavage pattern
-
-
?
saturated penta((1-4)-alpha-L-guluronan)
saturated di((1-4)-alpha-L-guluronan) + unsaturated tri((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)
?
-
only reactive in a high concentration of enzyme, and for a prolonged reaction time
-
-
?
sodium alginate
?
Alg2A prefers poly-(alpha-L-guluronate) as a substrate over poly-(beta-D-mannuronate), substrate specificity, overview
-
-
?
sodium alginate
?
AlyA1PL7 is an endolytic guluronate lyase that preferentially cleaves guluronate stretches
-
-
?
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 4.2.2.3
-
-
?
sodium alginate
?
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
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
?
LC mass and NMR spectrometris product analysis
-
-
?
sodium alginate
?
AlyA1PL7 is an endolytic guluronate lyase that preferentially cleaves guluronate stretches
-
-
?
sodium alginate
?
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
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
-
?
unsaturated hexa((1-4)-alpha-L-guluronan)
unsaturated triguluronic acid + unsaturated tetraguluronic acid
-
the enzyme degrades unsaturated hexaguluronans faster than saturated hexaguluronans, its subsite number appears to be seven
unsaturated trimers are the mayor product
?
unsaturated hexa((1-4)-alpha-L-guluronan)
unsaturated triguluronic acid + unsaturated tetraguluronic acid
-
the enzyme degrades unsaturated hexaguluronans faster than saturated hexaguluronans, its subsite number appears to be seven
unsaturated trimers are the mayor product
?
unsaturated pentaguluronan
?
-
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
-
-
?
unsaturated pentaguluronan
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
nine amino acid block conserved in the N-terminus
-
-
?
additional information
?
-
nine amino acid block conserved in the N-terminus
-
-
?
additional information
?
-
-
nine amino acid conserved block at the C-termini, unrelated to substrate recognition but to maintenance of the stable three-dimensional conformation
-
-
?
additional information
?
-
nine amino acid conserved block at the C-termini, unrelated to substrate recognition but to maintenance of the stable three-dimensional conformation
-
-
?
additional information
?
-
-
the first twenty amino acids are completely identical in Klebsiella pneumoniae and in Enterobacter cloacae, N-terminus
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
Flammeovirga sp. NJ-04
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
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
the enzyme shows low activity with poly(beta-D-mannuronate), reaction of EC 4.2.2.3
-
-
?
additional information
?
-
enzyme prefers polyM blocks over polyG blocks
-
-
?
additional information
?
-
-
no substrats: pectin, xanthan, guar gum, arabic gum, sesbania gum, guar gum and carrageenan
-
-
?
additional information
?
-
AB489222
no substrats: pectin, xanthan, guar gum, arabic gum, sesbania gum, guar gum and carrageenan
-
-
?
additional information
?
-
-
no substrats: pectin, xanthan, guar gum, arabic gum, sesbania gum, guar gum and carrageenan
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
nine amino acid block conserved in the N-terminus
-
-
?
additional information
?
-
-
the first twenty amino acids are completely identical in Klebsiella pneumoniae and in Enterobacter cloacae, N-terminus
-
-
?
additional information
?
-
-
L-tryptophan, L-histidine and L-lysine residues play an important role in enzymatic activity
-
-
?
additional information
?
-
nine amino acid conserved block at the C-termini, unrelated to substrate recognition but to maintenance of the stable three-dimensional conformation
-
-
?
additional information
?
-
-
operates in a processive manner. It is able to catalyze cleavage adjacent to either mannuronate or guluronate residues in alginate
-
-
?
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(alpha-L-guluronate) and poly(beta-D-mannuronate), cf. EC 4.2.2.3
-
-
?
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
?
-
Saccharophagus degradans 2-40 / ATCC 43961
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 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 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
?
-
-
enzyme acts only on poly-guluronate
-
-
?
additional information
?
-
enzyme prefers polyG blocks over polyM blocks
-
-
?
additional information
?
-
KJ-2 poly-mannuronate-guluronate-specific alginate lyase preferably degrades the glycosidic bond in beta-D-mannuronoyl-alpha-L-guluronate linkage than that in alpha-L-guluronoyl-beta-D-mannuronate linkage
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
KJ-2 poly-mannuronate-guluronate-specific alginate lyase preferably degrades the glycosidic bond in beta-D-mannuronoyl-alpha-L-guluronate linkage than that in alpha-L-guluronoyl-beta-D-mannuronate linkage
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
the relative activities for alginate, M, G, and GM blocks are 100%, 75%, 21%, and 15%, respectively
-
-
?
additional information
?
-
the relative activities for alginate, M, G, and GM blocks are 100%, 75%, 21%, and 15%, respectively
-
-
?
additional information
?
-
the relative activities for alginate, M, G, and GM blocks are 100%, 75%, 21%, and 15%, respectively
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
the relative activities for alginate, M, G, and GM blocks are 100%, 75%, 21%, and 15%, respectively
-
-
?
additional information
?
-
the relative activities for alginate, M, G, and GM blocks are 100%, 75%, 21%, and 15%, respectively
-
-
?
additional information
?
-
the relative activities for alginate, M, G, and GM blocks are 100%, 75%, 21%, and 15%, respectively
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
AlgB mainly releases oligosaccharides with a degree of polymersiation of 2-5 from the different kinds of substrates in an endolytic manner
-
-
?
additional information
?
-
isoforms AlyD and AlyE principally cleave the alpha-1,4 bonds involving alpha-L-guluronate subunits
-
-
?
additional information
?
-
isoforms AlyD and AlyE principally cleave the alpha-1,4 bonds involving alpha-L-guluronate subunits
-
-
?
additional information
?
-
isoforms AlyD and AlyE principally cleave the alpha-1,4 bonds involving alpha-L-guluronate subunits
-
-
?
additional information
?
-
isoforms AlyD and AlyE principally cleave the alpha-1,4 bonds involving alpha-L-guluronate subunits
-
-
?
additional information
?
-
alginate pentasaccharides that can be cleaved by AlyA1PL7 are GGGGG, GGMGG, GGGMG, and GGMMG
-
-
?
additional information
?
-
alginate pentasaccharides that can be cleaved by AlyA1PL7 are GGGGG, GGMGG, GGGMG, and GGMMG
-
-
?
additional information
?
-
-
alginate pentasaccharides that can be cleaved by AlyA1PL7 are GGGGG, GGMGG, GGGMG, and GGMMG
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
alginate pentasaccharides that can be cleaved by AlyA1PL7 are GGGGG, GGMGG, GGGMG, and GGMMG
-
-
?
additional information
?
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
poly-alpha-L-guluronic acid
4-deoxy-erythro-hex-4-ene pyranosyluronate + ?
degradation of alginate
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
alginate
?
AB489222
the bifunctional alginate lyase shows substrate specificity for poly(alpha-L-guluronate) and poly(beta-D-mannuronate) units in alginate molecules, cf. EC 4.2.2.3
-
-
?
alginate
?
AB489222
the bifunctional alginate lyase shows substrate specificity for poly(alpha-L-guluronate) and poly(beta-D-mannuronate) units in alginate molecules, cf. EC 4.2.2.3
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
Bacillus sp. (in: Bacteria) ATB-1015
-
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
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
-
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
-
?
poly-alpha-L-guluronic acid
unsaturated 1,4-di-, 1,4-tri- and 1,4-tetrasaccharides of L-guluronate
-
-
-
-
?
sodium alginate
?
AlyA1PL7 is an endolytic guluronate lyase that preferentially cleaves guluronate stretches
-
-
?
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 4.2.2.3
-
-
?
sodium alginate
?
AlyA1PL7 is an endolytic guluronate lyase that preferentially cleaves guluronate stretches
-
-
?
additional information
?
-
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
-
-
?
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
?
-
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
-
-
?
additional information
?
-
KJ-2 poly-mannuronate-guluronate-specific alginate lyase preferably degrades the glycosidic bond in beta-D-mannuronoyl-alpha-L-guluronate linkage than that in alpha-L-guluronoyl-beta-D-mannuronate linkage
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
Ca2+
CaCl2
Co2+
Cu2+
K+
Mg2+
MgCl2
Mn2+
MnCl2
Na+
NaCl
Ni2+
Zn2+
additional information
Ca2+
1 mM, 174% of initial activity, 10 mM, 135% of initial activity
Ca2+
-
essential cofactor, not only affects enzyme kinetics but also the final degree of conversion
Ca2+
-
involved in the formation of the active intermediate between the acidic uronates and amino acid side chains of the enzyme
Ca2+
at least 2 mM Ca2+ in the reaction mixture is essential for the activity
Ca2+
requires a divalent cation for activity, interaction between the enzyme and divalent cations takes place during substrate fixation and not before
Mg2+
1 mM, 168% of initial activity, 10 mM, 119% of initial activity
Mg2+
-
0.05-0.1 M: activation, higher concentrations cause lower activity or precipitation of alginate
Mg2+
-
50 mM, isoform A 116%, isoform B 121%, isoform C 114% of initial activity
Na+
100 mM, 126% of initial activity, 500 mM, 203% of initial activity
Na+
-
concentrations higher than 3% w/w produce complete loss of activity, the activity is partially restored with 1 mM calcium
Na+
optimum concentration 0.3 M, about 2fold increase in activity compared to absence of NaCl
Na+
up to 10fold increase in activity, optimum concentration 400 mM
Na+
up to 3fold increase in activity, optimum concentration 400 mM
Zn2+
relevance of this zinc ion in catalytic activity, metal-binding protein ligands are His533, Gln551, and Lys573. The metal ion establishes the orientation of His415 and Arg438, which would otherwise be mobile, to set these residues for interactions with substrate
additional information
a metal ion is required. No or poor effects by SDS at 0.001-0.01%, and DTT, Na+ and K+ at 1-5 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ba(OH)2
-
slightly inhibitory, percentage of inhibition is dependent on substrate
NiSO4
-
slightly inhibitory, percentage of inhibition is dependent on substrate
Triton X-100
slightly activating at 0.001%, slightly inhibitory at 0.01%
Ba2+
-
50 mM, isoform A 89%, isoform B 44%, isoform C 42% of initial activity
Co2+
-
50 mM, isoform A 67%, isoform B 66%, isoform C 29% of initial activity
EDTA
-
complete inhibition at 1 mM concentration, almost completely recovered activity by the addition of 2 mM CaCl2 or partially recovered by the addition of CoCl2 or MnCl2, suggesting that the enzyme conformation is bivalent-cation dependent
EDTA
-
1 mM concentration causes 83% inhibition, the enzyme regains about 90% of the original activity when incubated with 10 mM metal compounds such as MnCl2, MgCl2, NiCl2 or CaCl2, the enzyme is most likely to require the metal ions for the expression of activity
EDTA
-
1 mM, approximately 95% inhibition, enzymatic activity is restored totally by treatment with calcium chloride or partially restored with aluminium chloride or manganese (II) chloride
Guanidinium chloride
-
concentrations above 3 M cause significant loss of activity
Guanidinium chloride
-
8 M urea causes apparent retention of approximately 50% of enzyme activity
Mg2+
-
0.1 M: activation, higher concentrations cause lower activity or precipitation of alginate
SDS
-
10 mM SDS causes complete loss of activity whereas the ordered beta-structure is created
Urea
-
enzyme preincubated in the presence of 6 M urea, dialyzed and assayed normally retains 90% activity, but if the enzyme is preincubated and assayed in the presence of 6 M urea no activity is measured
Urea
-
8 M urea causes apparent retention of approximately 50% of enzyme activity
Zn2+
-
50 mM, isoform A 10%, isoform B 14%, isoform C 12% of initial activity
ZnCl2
-
slightly inhibitory, percentage of inhibition is dependent on substrate
additional information
-
10 mM SDS, protein denaturants or 1 mM urea do not affect enzyme activity
-
additional information
-
iodoacetate, dithiothreitol, 2-mercaptoethanol, sodium dodecyl sulfate or p-chloromercuribenzoate have no inhibitory effects
-
additional information
-
dithiothreitol or 2-mercaptoethanol in concentrations between 0.1 and 6 mM have no influence on intracellular alginate lyase
-
additional information
-
activity is lost at standard sea water salinity, restored in the presence of 1 mM calcium, activity is lost even at low salt concentrations if calcium is removed by a calcium chelator
-
additional information
activity of AlgMytC is stable in the presence of various detergents
-
additional information
Shewanella sp. YH1
-
enzymatic activity is about two times higher in phosphate buffer than in Tris buffer
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alginates with low guluronic content
-
cultures in the presence of alginates with low guluronic content give reduced biomass but favor enzyme production
Triton X-100
slightly activating at 0.001%, slightly inhibitory at 0.01%
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.077
saturated deca((1-4)-alpha-L-guluronan)
-
pH 7.0, 50 mM phosphate buffer
-
4.25
saturated tetra((1-4)-alpha-L-guluronan)
-
pH 8.5, 30 °C, 100 mM glycine in 0.1 N NaCl and 0.1 N NaOH
-
1.39
alginate
truncated protein lacking both the CBM16 and CBM32 domains, pH 7.0, 23°C
1.46
alginate
truncated protein lacking the CBM16 domain, pH 7.0, 23°C
0.099
saturated hepta((1-4)-alpha-L-guluronan)
-
pH 7.0, 50 mM phosphate buffer
-
0.192
saturated hepta((1-4)-alpha-L-guluronan)
-
pH 8.5, 30 °C, 100 mM glycine in 0.1 N NaCl and 0.1 N NaOH
-
0.11
saturated hexa((1-4)-alpha-L-guluronan)
-
pH 7.0, 50 mM phosphate buffer
-
0.226
saturated hexa((1-4)-alpha-L-guluronan)
-
pH 8.5, 30 °C, 100 mM glycine in 0.1 N NaCl and 0.1 N NaOH
-
0.232
saturated penta((1-4)-alpha-L-guluronan)
-
pH 8.5, 30 °C, 100 mM glycine in 0.1 N NaCl and 0.1 N NaOH
-
0.3
saturated penta((1-4)-alpha-L-guluronan)
-
pH 7.0, 50 mM phosphate buffer
-
1.753
sodium alginate
with L-guluronate content of 66.7%, pH 7.5, 30°C, recombinant enzyme
3.087
sodium alginate
with L-guluronate content of 52.6%, pH 7.5, 30°C, recombinant enzyme
6.18
sodium alginate
with L-guluronate content of 33.3%, pH 7.5, 30°C, recombinant enzyme
additional information
alginate
-
Km value 0.26 mg/ml, pH 7.0, 30°C
additional information
alginate
AB489222
Km value 0.26 mg/ml, pH 7.0, 30°C
additional information
additional information
-
kinetics, overview
-
additional information
additional information
Michaelis-Menten kinetics, overview
-
additional information
additional information
-
KM value for sodium alginate is 21.5 mg/ml
-
additional information
additional information
-
KM-value for alpha-L-guluronosyl linkage in alginate, 1.086 mg/ml, for poly(alpha-L-guluronic acid), 0.465 mg/ml at pH 8.5, 50°C
-
additional information
additional information
dimeric AlyA5 shows two-phase kinetics with alginate, overview
-
additional information
additional information
dimeric AlyA5 shows two-phase kinetics with alginate, overview
-
additional information
additional information
-
dimeric AlyA5 shows two-phase kinetics with alginate, overview
-
additional information
poly(alpha-(1,4)-L-guluronate)
Km value 1.04 mg/ml, pH 8.0, 30°C
additional information
poly(beta-(1,4)-D-mannuronate)
Km value 6.9 mg/ml, pH 8.0, 30°C
additional information
poly(beta-(1,4)-D-mannuronate/alpha-(1,4)-L-guluronate)
Km value 0.50 mg/ml, pH 8.0, 30°C
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
9.24
alginate
truncated protein lacking both the CBM16 and CBM32 domains, pH 7.0, 23°C
10.4
alginate
truncated protein lacking the CBM16 domain, pH 7.0, 23°C
12.66
sodium alginate
with L-guluronate content of 66.7%, pH 7.5, 30°C, recombinant enzyme
17.89
sodium alginate
with L-guluronate content of 52.6%, pH 7.5, 30°C, recombinant enzyme
19.51
sodium alginate
with L-guluronate content of 33.3%, pH 7.5, 30°C, recombinant enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6.64
alginate
truncated protein lacking both the CBM16 and CBM32 domains, pH 7.0, 23°C
7.12
alginate
truncated protein lacking the CBM16 domain, pH 7.0, 23°C
3.16
sodium alginate
with L-guluronate content of 33.3%, pH 7.5, 30°C, recombinant enzyme
5.79
sodium alginate
with L-guluronate content of 52.6%, pH 7.5, 30°C, recombinant enzyme
7.22
sodium alginate
with L-guluronate content of 66.7%, pH 7.5, 30°C, recombinant enzyme
additional information
alginate
kcat/Km value 26 ml/mg/s, pH 8.5, 30°C
additional information
alginate
-
kcat/Km value 67.4 mg/ml, pH 7.0, 45°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
21.48
substrate poly(beta-(1,4)-D-mannuronate), pH 8.0, 35°C
2152
264
substrate alginate, truncated protein consisting of the catalytic module, pH 6.0, 40°C
27.03
substrate poly(beta-(1,4)-D-mannuronate), pH 8.0, 35°C
41.4
-
purified recombinant His-tagged enzyme, pH 7.0, 50°C, substrate alginate
46
-
purified recombinant His-tagged enzyme, substrate poly(alpha-L-guluronate), pH 7.0, 50°C
7658
substrate poly(beta-(1,4)-D-mannuronate), pH 7.5, 55°C
8409
8643
substrate poly(alpha-(1,4)-L-guluronate), pH 7.5, 55°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
7.5
7.8
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6
highest activity at pH 6.0, which sharply decreases when the pH is higher or lower than pH 6.0
6 - 9
7 - 10
90% of maximal activity at pH 8.5 and pH 10.0, 30% at pH 7.5, inactive below, profile overview
additional information
additional information
pH profile, narrow activity range, overview
additional information
pH profile, narrow activity range, overview
additional information
-
pH profile, narrow activity range, overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
35
37
40
45
50
55
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 70
25 - 40
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.9
7.3 - 7.4
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain M-1,intracellular and extracellular enzyme
-
-
brenda
type 25, intracellular and extracellular enzymes
-
-
brenda
bifunctional enzyme, activities against poly(beta-D-mannuronate), EC 4.2.2.3, and poly(alpha-L-guluronate), EC 4.2.2.11
-
-
brenda
bifunctional alginate lyase, catalyzes both reactions of EC 4.2.2.3 and EC 4.2.2.11
UniProt
brenda
bifunctional alginate lyase, catalyzes the reactions of EC 4.2.2.3 and EC 4.2.2.11
UniProt
brenda
extracellular isozyme; several isozymes with homo- or heterogenous substrate specificities
SwissProt
brenda
sequence contains a putative signal sequence of 23 amino acids
UniProt
brenda
sequence contains a putative 26-amino-acid signal peptide
UniProt
brenda
sequence contains a putative signal sequence of 23 amino acids
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
most of the alginate lyase activity is intracellular
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
evolution
Alg2A belongs to the polysaccharide lyase family 7, but has a different endolytic reaction mode from other alginate lyases from polysaccharide lyase family 7 owing to high yields of penta-, hex-, and hepta-saccharides in the hydrolysis products of Alg2A, overview
evolution
AlyA1PL7 is an endolytic guluronate lyase and belongs to the PL7 family, subfamily 1, the genome of Zobellia galactanivorans contains seven putative alginate lyase genes, five of which are localized within two clusters comprising additional carbohydrate-related genes, phylogenetic analysis. Despite a common jelly roll-fold, these striking differences of the mode of action are explained by a distinct active site topology, an open cleft in AlyA1PL7, whereas AlyA5 displays a pocket topology due to the presence of additional loops partially obstructing the catalytic groove. In contrast to PL7 alginate lyases from terrestrial bacteria, both enzymes proceed according to a calcium-dependent mechanism
evolution
AlyA5 belongs to the PL7 family, subfamily 5, the genome of Zobellia galactanivorans contains seven putative alginate lyase genes, five of which are localized within two clusters comprising additional carbohydrate-related genes, phylogenetic analysis. Despite a common jelly roll-fold, these striking differences of the mode of action are explained by a distinct active site topology, an open cleft in AlyA1PL7, whereas AlyA5 displays a pocket topology due to the presence of additional loops partially obstructing the catalytic groove. In contrast to PL7 alginate lyases from terrestrial bacteria, both enzymes proceed according to a calcium-dependent mechanism
evolution
the enzyme belongs to the polysaccharide lyase PL7 family. Structure and beta-elimination mechanism for glycolytic bond cleavage by Alg17c are similar to those observed for family 15 polysaccharide lyases and other lyases, evolutionary relationships and structure-based hierarchy in the classification, overview
evolution
-
the enzyme belongs to the to the polysaccharide lyase-7 family
evolution
the enzyme contains the conserved amino acid sequences RTELREM, QIH, and YFKAGVYNQ of the polysaccharide lyase family 7
evolution
-
the enzyme belongs to the polysaccharide lyase PL7 family. Structure and beta-elimination mechanism for glycolytic bond cleavage by Alg17c are similar to those observed for family 15 polysaccharide lyases and other lyases, evolutionary relationships and structure-based hierarchy in the classification, overview
-
evolution
-
AlyA1PL7 is an endolytic guluronate lyase and belongs to the PL7 family, subfamily 1, the genome of Zobellia galactanivorans contains seven putative alginate lyase genes, five of which are localized within two clusters comprising additional carbohydrate-related genes, phylogenetic analysis. Despite a common jelly roll-fold, these striking differences of the mode of action are explained by a distinct active site topology, an open cleft in AlyA1PL7, whereas AlyA5 displays a pocket topology due to the presence of additional loops partially obstructing the catalytic groove. In contrast to PL7 alginate lyases from terrestrial bacteria, both enzymes proceed according to a calcium-dependent mechanism
-
evolution
-
AlyA5 belongs to the PL7 family, subfamily 5, the genome of Zobellia galactanivorans contains seven putative alginate lyase genes, five of which are localized within two clusters comprising additional carbohydrate-related genes, phylogenetic analysis. Despite a common jelly roll-fold, these striking differences of the mode of action are explained by a distinct active site topology, an open cleft in AlyA1PL7, whereas AlyA5 displays a pocket topology due to the presence of additional loops partially obstructing the catalytic groove. In contrast to PL7 alginate lyases from terrestrial bacteria, both enzymes proceed according to a calcium-dependent mechanism
-
physiological function
knockout mutant shows growth rates similar to wild-type in MB medium, but grows very slowly in the ASW liquid medium supplemented with 0.3% alginate
physiological function
alginate lyase consists of three domains, i.e. a carbohydrate-binding domain, a family 32 CBM domain, and an alginate lyase domain belonging to polysaccharide lyase family 7 (PL7). The CBM32 domain does not contribute to enhancing AlyQ's activity under the assayed conditions but can bind to cleaved but not intact alginate. The CBM32 and catalytic domains do not interact with one another. The CBM32 domain contains a conserved Arg that may bind to the carboxyl group of alginate. The catalytic domain shares a conserved substrate-binding groove, and the presence of two negatively charged Asp residues may dictate substrate specificity especially at subsite +1
physiological function
Bacillus sp. TAG8 is able to utilize alginate as a sole carbon source
physiological function
deletion of the noncatalytic region of Aly1 causes weak changes of biochemical characteristics but increases the degradation proportions of small size-defined saturated M-enriched oligosaccharide substrates and unsaturated tetrasaccharide fractions without any size changes of degradable oligosaccharides
physiological function
-
knockout mutant shows growth rates similar to wild-type in MB medium, but grows very slowly in the ASW liquid medium supplemented with 0.3% alginate
-
additional information
secondary structure comparison of AlyA5 and AlyA1PL7
additional information
secondary structure comparison of AlyA5 and AlyA1PL7
additional information
-
secondary structure comparison of AlyA5 and AlyA1PL7
additional information
-
secondary structure comparison of AlyA5 and AlyA1PL7
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A0A8F2JCX6_PSEVC
393
0
42338
TrEMBL
-
A0A6B9XMS7_PSEVC
362
0
40036
TrEMBL
-
A0A8F2F481_PSEVC
740
0
82589
TrEMBL
-
A9CEJ9_AGRFC
Agrobacterium fabrum (strain C58 / ATCC 33970)
776
0
87871
TrEMBL
-
G0KZG8_ZOBGA
Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij)
390
0
44037
TrEMBL
-
G0L2Y1_ZOBGA
Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij)
352
0
39252
TrEMBL
-
L8B3Z6_9GAMM
343
0
37573
TrEMBL
other Location (Reliability: 2)
EALGL_SACD2
Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024)
736
0
81582
Swiss-Prot
Mitochondrion (Reliability: 2)
Q9Z6D6_9GAMM
398
0
43159
TrEMBL
Mitochondrion (Reliability: 2)
G0LAE1_ZOBGA
Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij)
446
0
48105
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
23000
25000
28000
31000
32000
36000
37573
x * 37573, sequence calculation, x * 43000, recombinant His-tagged enzyme, SDS-PAGE
38000
38300
monomeric recombinant His-tagged enzyme, gel filtration
41000
42000
x * 42000, recombinant His-tagged enzyme, SDS-PAGE
42400
x * 45500, recombinant enzyme with signal peptide, x * 42400, recombinant enzyme without signal peptide, calulated
43000
45500
x * 45500, recombinant enzyme with signal peptide, x * 42400, recombinant enzyme without signal peptide, calulated
60250
-
x * 60250, isoform A, x * 36000, isoform B, x * 23000, isoform C, SDS-PAGE
69500
dimeric recombinant His-tagged enzyme, gel filtration
77500
x * 77500, SDS-PAGE of recombinant protein used to maltose binding protein
78000
x * 79900, including signal peptide, x * 78000, without signal peptide, calculated. x * 80000, SDS-PAGE
79100
x * 81600, about, sequence calculation, x * 79100, recombinant enzyme, SDS-PAGE
79900
x * 79900, including signal peptide, x * 78000, without signal peptide, calculated. x * 80000, SDS-PAGE
80000
x * 79900, including signal peptide, x * 78000, without signal peptide, calculated. x * 80000, SDS-PAGE
81600
x * 81600, about, sequence calculation, x * 79100, recombinant enzyme, SDS-PAGE
23000
-
x * 60250, isoform A, x * 36000, isoform B, x * 23000, isoform C, SDS-PAGE
36000
-
x * 60250, isoform A, x * 36000, isoform B, x * 23000, isoform C, SDS-PAGE
43000
x * 37573, sequence calculation, x * 43000, recombinant His-tagged enzyme, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
monomer
monomer or dimer
additional information
?
Cobetia sp. NAP1
-
x * 35000, SDS-PAGE, x * 35400, MALDI-TOF, x * 35700, calculated from sequence, mature protein
?
x * 25320, calculated from sequence, including His-tag
?
-
x * 60250, isoform A, x * 36000, isoform B, x * 23000, isoform C, SDS-PAGE
?
-
x * 60250, isoform A, x * 36000, isoform B, x * 23000, isoform C, SDS-PAGE
-
?
x * 45500, recombinant enzyme with signal peptide, x * 42400, recombinant enzyme without signal peptide, calulated
?
-
x * 45500, recombinant enzyme with signal peptide, x * 42400, recombinant enzyme without signal peptide, calulated
-
?
x * 81600, about, sequence calculation, x * 79100, recombinant enzyme, SDS-PAGE
?
Saccharophagus degradans 2-40 / ATCC 43961
-
x * 81600, about, sequence calculation, x * 79100, recombinant enzyme, SDS-PAGE
-
?
x * 37573, sequence calculation, x * 43000, recombinant His-tagged enzyme, SDS-PAGE
?
x * 79900, including signal peptide, x * 78000, without signal peptide, calculated. x * 80000, SDS-PAGE
?
-
x * 79900, including signal peptide, x * 78000, without signal peptide, calculated. x * 80000, SDS-PAGE
-
?
x * 77500, SDS-PAGE of recombinant protein used to maltose binding protein
?
x * 54120, calculated from sequence, x * 55050, SDS-PAGE, mature enzyme
?
x * 33900, calculated from sequence, x * 34000, SDS-PAGe recombinant protein with His-tag
?
2 * 265000-29000, recombinant His-tagged enzyme, SDS-PAGE
homodimer
structure analysis, SDS-PAGE and analytical gel filtration, overview
homodimer
-
structure analysis, SDS-PAGE and analytical gel filtration, overview
-
monomer
1 * 38300, calculated from sequence, 1 * 38000, SDS-PAGE
monomer
1 * 38600, calculated from sequence, 1 * 38000, SDS-PAGE
monomer or dimer
x * 42000, recombinant His-tagged enzyme, SDS-PAGE
monomer or dimer
-
x * 42000, recombinant His-tagged enzyme, SDS-PAGE
-
additional information
transcription of the alyA gene leads to a 43-kDa protein, which is the derivative of the nascent alyA gene product lacking the N-terminal 22 amino-acid signal peptide, and to 33- and 30.5-kDa proteins, which are the C-terminal portions of the nascent alyA gene products that start from the amino-acid residue positions 148 and 162, respectively
additional information
-
transcription of the alyA gene leads to a 43-kDa protein, which is the derivative of the nascent alyA gene product lacking the N-terminal 22 amino-acid signal peptide, and to 33- and 30.5-kDa proteins, which are the C-terminal portions of the nascent alyA gene products that start from the amino-acid residue positions 148 and 162, respectively
-
additional information
-
purification leads to a mixture of three monomeric alginate lyases with molecular masses of 60.25, 36, and 23 kDa
additional information
-
purification leads to a mixture of three monomeric alginate lyases with molecular masses of 60.25, 36, and 23 kDa
-
additional information
overall structure of AlyA1PL7 is a PL7 beta-sandwich jelly roll-fold, formed by two anti-parallel beta-sheets stacked against each other. The outer convex sheet is composed of five beta-strands, and the inner concave sheet is composed of seven beta-strands, forming a groove that harbors the catalytic active site
additional information
overall structure of AlyA1PL7 is a PL7 beta-sandwich jelly roll-fold, formed by two anti-parallel beta-sheets stacked against each other. The outer convex sheet is composed of five beta-strands, and the inner concave sheet is composed of seven beta-strands, forming a groove that harbors the catalytic active site
additional information
-
overall structure of AlyA1PL7 is a PL7 beta-sandwich jelly roll-fold, formed by two anti-parallel beta-sheets stacked against each other. The outer convex sheet is composed of five beta-strands, and the inner concave sheet is composed of seven beta-strands, forming a groove that harbors the catalytic active site
additional information
-
overall structure of AlyA1PL7 is a PL7 beta-sandwich jelly roll-fold, formed by two anti-parallel beta-sheets stacked against each other. The outer convex sheet is composed of five beta-strands, and the inner concave sheet is composed of seven beta-strands, forming a groove that harbors the catalytic active site
-
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
recombinant enzyme with signal peptide and without signal peptide with the His-tag consist of 393 and 372 amino acids, respectively
proteolytic modification
-
recombinant enzyme with signal peptide and without signal peptide with the His-tag consist of 393 and 372 amino acids, respectively
-
proteolytic modification
sequence contains a putative 26-amino-acid signal peptide
proteolytic modification
sequence contains a putative signal sequence of 23 amino acids
proteolytic modification
-
sequence contains a putative signal sequence of 23 amino acids
-
proteolytic modification
-
sequence contains a putative 26-amino-acid signal peptide
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of native protein and its inactive mutant H531A in complex with alginate trisaccharide, at 2.10 and 2.99 A resolutions with final R-factors of 18.3 and 19.9%, respectively. The enzyme is comprised of an alpha/alpha-barrel plus anti-parallel beta-sheet as a basic scaffold. His311 and Tyr365 are the catalytic base and acid, respectively. A short alpha-helix in the central alpha/alpha-barrel domain and a conformational change at the interface between the central and C-terminal domains are essential for the exolytic mode of action
20°C, drop solution comprising 1.4 M NaCl, 0.1 M potassium sodium phosphate and 0.1 M 2-morpholinoethanesulfonate-sodium hydroxide pH 6.5, vapor-diffusion method, monoclinic cristals
-
homology modeling of structure. Residues Asn198, His199, Arg246, and Tyr253 are conserved for the catalytic active site
purified recombinant soluble His-tagged wild-type and selenomethionine-labeled enzyme, and two mutant enzymes H202L and Y258A, and Y258A DELTAMMG variant, free or in complex with an alginate trisaccharide, hanging drop vapour diffusion method, mixing of 15 mg/ml protein in in 20 mM HEPES, pH 7.5, 100 mM KCl, with 0.1 M Tris, pH 8.0, 5% 2-methyl-2,4-pentanediol, 10% PEG 6000, 3 days, 16°C, X-ray diffraction structure determination and analysis at 1.85 A, 1.7 A, 2.45 A, and 1.9 A resolution, respectively
hanging-drop vapour-diffusion, A1-II structure at 2.2 A resolution, A1-II' structure at 1.0 A resolution
-
purified recombinant catalytic domain of AlyA1PL7, hanging drop vapor diffusion method, 0.002 ml of 11.3 mg/ml protein solution with 0.1 mg/ml oligoguluronate, are mixed with 0.001 ml of reservoir solution containing 0.2 M KSCN and 28% PEG-MME 2000, and equilibration against 0.5 ml reservoir solution, 21°C, screening and method optimization, X-ray diffraction structure determination and analysis at 1.43 A resolution
purified recombinant full-length dimeric AlyA5, hanging drop vapor diffusion method, 0.002 ml of 7.7 mg/ml protein solution with 0.1 mg/ml oligoglucuronate, are mixed with 0.001 ml of reservoir solution containing PEG 3350 and 0.2 M sodium/potassium tartrate, and equilibration against 02 ml reservoir solution, 21°C, screening and method optimization, X-ray diffraction structure determination and analysis at 1.75 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
T185N
NCR-truncated protein, mutant has lost its M-producing capability but retained the ability to yield G units by almost completely degrading 2-aminobenzamide-labeled G4 chains. Mutant T185N can degrade 2-aminobenzamide-labeled G5 and 2-aminobenzamide-labeled M5 fractions at greater proportions than wild-type
A78S
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 820 U/mg, against poly(alpha-L-guluronic acid) 938 U/mg. Ratio of activities 1.1
A78S/T89I
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 228 U/mg, against poly(alpha-L-guluronic acid) 34.3 U/mg. Ratio of activities 0.2
A78S/T89I/A217E
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 187 U/mg, against poly(alpha-L-guluronic acid) 29.8 U/mg. Ratio of activities 0.2
G26E
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 692 U/mg, against poly(alpha-L-guluronic acid) 787 U/mg. Ratio of activities 1.1
G26E/P39H
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 246 U/mg, against poly(alpha-L-guluronic acid) 19.5 U/mg. Ratio of activities 0.1. In the absence of Ca2+, no detectable activity against G-M linkages
G304V
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 828 U/mg, against poly(alpha-L-guluronic acid) 878 U/mg. Ratio of activities 1.1
I51M
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 731 U/mg, against poly(alpha-L-guluronic acid) 786 U/mg. Ratio of activities 1.1
I51M/T89I
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 227 U/mg, against poly(alpha-L-guluronic acid) 18.8 U/mg. Ratio of activities 0.1
I51M/T89I/G304V
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 153 U/mg, against poly(alpha-L-guluronic acid) 13.3 U/mg. Ratio of activities 0.1
P39H
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 356 U/mg, against poly(alpha-L-guluronic acid) 37 U/mg. Ratio of activities 0.1
P39T
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 216 U/mg, against poly(alpha-L-guluronic acid) 71 U/mg. Ratio of activities 0.3
S35R
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 443 U/mg, against poly(alpha-L-guluronic acid) 448 U/mg. Ratio of activities 1.0
S35R/P39T
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 32.6 U/mg, against poly(alpha-L-guluronic acid) 6.9 U/mg. Ratio of activities 0.2
S35R/P39T/A224V
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 43 U/mg, against poly(alpha-L-guluronic acid) 3.4 U/mg. Ratio of activities 0.1
S37I
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 53.8 U/mg, against poly(alpha-L-guluronic acid) 4.3 U/mg. Ratio of activities 0.1
S86L
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 31 U/mg, against poly(alpha-L-guluronic acid) 9.1 U/mg. Ratio of activities 0.3
T85A
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) 24.8 is U/mg, against poly(alpha-L-guluronic acid) 4.4 U/mg. Ratio of activities 0.32
T89I
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 218 U/mg, against poly(alpha-L-guluronic acid) 31 U/mg. Ratio of activities 0.1
V6I
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is858 U/mg, against poly(alpha-L-guluronic acid) 851 U/mg. Ratio of activities 1.0
V6I/T85A
-
activity against poly(beta-D-mannuronic acid/alpha-L-guluronic acid) is 23.6 U/mg, against poly(alpha-L-guluronic acid) 2.2 U/mg. Ratio of activities 0.1
H202L
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H415A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Q149A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R260A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R438A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
additional information
additional information
a truncated protein consisting of the catalytic module degrades alginate into unsaturated oligosaccharides with maximal activity at 30°C, 10°C lower than the temperature for wild-type. Thermostability ranges from 0 to 30°C and highest activity is at pH 7.0
additional information
-
engineering of different lyases, each of which cleaves only one of the four possible linkages in alginates: G-G, G-M, M-G, and M-M. The substitutions conferring altered specificity to the mutant enzymes are located in conserved regions in the polysaccharide lyase family 7 alginate lyases. Structure-function analyses suggests that the improved G-G specificity might be caused by increased affinity for nonproductive binding of the alternating G-M structure
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 10
5
-
relatively stable in alkaline pH and unstable in a range outside acidic pH 5.0
34064
5 - 8
5.5 - 8.5
6 - 9
8 - 9
the purified recombinant His-tagged enzyme exhibits stable and high activity at pH between 8.0 and 9.0
729058
8.5 - 10
purified recombinant enzyme, 25°C, 24 h, over 90% activity remaining
730184
4 - 10
purified recombinant His-tagged enzyme, 45°C, the enzyme retains over 60% activity after 24 h incubation at pH 5.0-10.0, but loses about 80% activity at pH 4.0 after 24 h
730135
4 - 10
purified recombinant enzyme, 25°C, 24 h, over 70% activity remaining
730184
5.5 - 8.5
AB489222
purified enzyme, 12 h, over 60% activity within this pH range remains pH 5.5 to 8.5, mostly stable at pH 7.5, half inactivation at pH 9.5
729531
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 40
100
-
incubation for 15 min causes complete loss of activity, activity diminishes with increasing incubation temperatures below 100 °C, addition of hen egg-white lysozyme decreased its thermal activity dramatically
25 - 35
purified recombinant enzyme, pH 9.0, completely stable at 25°C for 24 h and at 35°C for 1 h, but loss of 60% activity after 24 h at 35°C
30 - 50
-
enzyme is rapidly inactivated upon incubation at 30-50°C for 15 min
35
40
45
50
60
90
35
-
30 min, isoform B 59% residual activity, isoform C 55% residual activity
40
purified recombinant His-tagged enzyme, 20 min, stable up to, significant loss of activity above
45
purified recombinant His-tagged enzyme, pH 8.5, 1 h, stable up to
50
purified recombinant His-tagged enzyme, pH 8.5, 1 h, inactivation
60
-
50% of the activity remains after treatment at this temperature for 30 min
60
-
no activity is measured after treatment at this temperature, activity decreases with increasing temperature
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
activity of AlgMytC is stable in the presence of various detergents
more labile to heat treatment in Tris-HCl buffer, pH 7.0 than in phosphate buffer with similar pH
-
stable to freeze-drying, retains activity for several months in this form
-
unstable to heating, shows low activity when mantained in 50 mM Tris-HCl buffer
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, cation exchange chromatography and gel filtration
-
ammonium sulfate precipitation, gel filtration and anion-exchange chromatography
-
cation exchange chromatography, chromatofocusing and gel filtration
-
native enzyme 1.75fold by ammonium sulfate fractionation and anion exchange chromatography
AB489222
partial, ammonium sulfate precipitation and ion-exchange chromatography
-
purification by centrifugation, ammonium sulfate fractionation, anion-exchange chromatography and size exclusion chromatography
-
purification leads to a mixture of three monomeric alginate lyases with molecular masses of 60.25, 36, and 23 kDa
-
recombinant His-tagged enzyme 5.74fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme by nickel affinity chromatography from Escherichia coli strain BL21(DE3)
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration to homogeneity
recombinant His-tagged enzyme lacking the signal peptide from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration
-
recombinant protein
recombinant protein, purified by Ni-NTA Sepharose affinity chromatography
recombinant soluble and renatured His-tagged enzyme from Escherichia coli strain BL21(DE3)
recombinant soluble His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) Rosetta culture supernatant by nickel affinity chromatography and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
DNA and amino acid sequence determination and analysis, phylogenetic analysis
AB489222
expression in Escherichia coli
gene alg2A, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene alg7D, overexpression of soluble His-tagged enzyme lacking the signal peptide in Escherichia coli strain BL21(DE3)
-
gene algMytC, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of N-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3) partly in inclusion bodies
phylogenetic analysis, recombinant expression of His-tagged AlyA1PL7 in Escherichia coli strain BL21(DE3)
phylogenetic analysis, recombinant expression of His-tagged AlyA5 in Escherichia coli strain BL21(DE3)
subcloning of His-tagged wild-type and mutant enzymes in Escherichia coli strain DH5-alpha, expression in Escherichia coli strain BL21(DE3) Rosetta, the enzymes are secreted from periplasmic space
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is induced by an increase in sodium alginate concentration and also by the addition of 0.2-0.3 M NaCl
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
6M urea collapses the circular dicroic spectral bands of the native enzyme caused by aromatic amino acids side chains and causes dissapearance of the enzyme activity, removal of the denaturant by dialysis restored the native-like spectrum and the activity, but some parts of the enzyme conformation are defective in the renaturation conditions
-
enzyme is not thermotolerant, but can refold to its active form following an almost complete denaturation at approximately 60°C
Shewanella sp. YH1
-
solubilization of enzyme from inclusion bodies by 8 M urea in Tris-HCl, pH 8.0
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
-
oligosaccharides produced by alginase may act as osmoprotective agents during the plant germination process. The relative root length of Brassica campestris L. increases with the addition of oligosaccharides with reduced degrees of polymerization. The oligosaccharides with lower degree of polymerization-values are effective in reducing the effect of salt stress on the activity of the superoxide dismutase and guaiacol peroxidase, and oligosaccharides with moderate degree of polymerization-values can reduce the increase in lipid peroxidation activities induced by salt stress
biofuel production
degradation
food industry
industry
alginate lyase is a promising biocatalyst because of its application in saccharification of alginate for the production of renewable biofuels
synthesis
additional information
-
use of recombinant abalone alginate lyase and beta-1,4-endoglucanase for protoplast isolation from Laminaria japonica. In Laminaria japonica blades pretreated with proteinase K and incubated in artificial seawater containing alginate lyase and beta-1,4-endoglucanase, the protoplast number is increased up to 5000000 protoplasts/g fresh weight. These cells are mostly derived from the epidermal layer rather than the cortical layer. Results suggest that at least three enzymes, alginate lyase, cellulase, and protease, are essential for effective protoplast isolation from Laminaria japonica
biofuel production
Alg17C can be used as the key enzyme to produce alginate monomers in the process of utilizing alginate for biofuels and chemicals production
biofuel production
Saccharophagus degradans 2-40 / ATCC 43961
-
Alg17C can be used as the key enzyme to produce alginate monomers in the process of utilizing alginate for biofuels and chemicals production
-
degradation
-
enzymatic treatment for 24 hours is sufficient to release all potential glucose from the glucan rich brown seaweed Laminaria digitata
degradation
enzymatic treatment for 24 hours is sufficient to release all potential glucose from the glucan rich brown seaweed Laminaria digitata
degradation
enzymatic treatment for 24 hours is sufficient to release all potential glucose from the glucan rich brown seaweed Laminaria digitata
degradation
enzymatical saccharification of acid pretreated and untreated brown macroalgae, first at pH 7.5, 25°C for 12 h with a blend of recombinant alginate and oligoalginate lyases, then at pH 5.2 using a commercial cellulase cocktail. The use of recombinant alginate lyases and oligoalginate lyases in combination with cellulases increases the release of glucose from untreated seaweed. For saccharification of pretreated algae, only cellulases are needed to achieve high glucose yields
degradation
enzymatical saccharification of acid pretreated and untreated brown macroalgae, first at pH 7.5, 25°C for 12 h with a blend of recombinant alginate and oligoalginate lyases, then at pH 5.2 using a commercial cellulase cocktail. The use of recombinant alginate lyases and oligoalginate lyases in combination with cellulases increases the release of glucose from untreated seaweed. For saccharification of pretreated algae, only cellulases are needed to achieve high glucose yields
food industry
the KJ-2 polyMG-specific alginate lyase can be used in combination with other alginate lyases for a synergistic saccharification of alginate
food industry
-
the KJ-2 polyMG-specific alginate lyase can be used in combination with other alginate lyases for a synergistic saccharification of alginate
-
synthesis
Alg17C can be used as the key enzyme to produce alginate monomers in the process of utilizing alginate for biofuels and chemicals production
synthesis
alginate lyase is a promising biocatalyst because of its application in saccharification of alginate for the production of biochemicals. Alg2A can be a good tool for the large-scale preparation of alginate oligosaccharides with high degree of polymerization
synthesis
Saccharophagus degradans 2-40 / ATCC 43961
-
Alg17C can be used as the key enzyme to produce alginate monomers in the process of utilizing alginate for biofuels and chemicals production
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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: Bacteria), Bacillus sp. (in: Bacteria) 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
Bacillus sp. (in: Bacteria), Flavobacterium sp.
-
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-?-L-guluronide) Lyase from Enterobacter cloacae M-1.
Biosci. Biotechnol. Biochem.
62
164-166
1998
Enterobacter cloacae, Sphingobacterium multivorum, Enterobacter cloacae M-1intracellular, 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
Enterobacter cloacae, Bacillus sp. (in: Bacteria), Corynebacterium sp., Corynebacterium sp. (Q9RB42), Sphingobacterium multivorum, Klebsiella pneumoniae, Pseudomonas sp., Pseudomonas aeruginosa, Sargassum sp., Vibrio harveyi, Vibrio sp., Pseudoalteromonas elyakovii (Q9Z6D6), Vibrio harveyi AL-128
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. (C4TJD2), Vibrio sp. (C4TJD3), Vibrio sp. (C4TJD4), Vibrio sp. A9m (C4TJD2), Vibrio sp. A9m (C4TJD3), Vibrio sp. A9m (C4TJD4)
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), Sphingomonas sp. MJ-3 (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), Pseudomonas sp. KS-408 (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 CGMCC5336 (AB489222), Isoptericola halotolerans CGMCC 5336
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 elyakovii (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
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
Sphingobacterium multivorum, Flavobacterium sp. S20 (G9CHX6), 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
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