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Information on EC 4.2.2.11 - guluronate-specific alginate lyase
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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
- degradation
- lyases
-
klebsiella
- unsaturated
-
endolytic
- polysaccharide
- pneumoniae
- sphingomonas
-
mannuronate
- flavobacterium
- tetrasaccharide
- algae
-
terrestrial
- biomass
-
depolymerization
- aerogenes
-
4.2.2.3
- synthesis
- food industry
- biofuel production
- agriculture
- 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
alginate lyase
Aly1
AlyA
AlyA1PL7
AlyA5
AlyD
AlyE
AlyV5
polyMG-specific alginate lyase
V12B01_09446
V12B01_24274
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and alpha-L-guluronate at their reducing end
Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and alpha-L-guluronate at their reducing end
-
-
-
-
Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and alpha-L-guluronate at their reducing end
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
Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and alpha-L-guluronate at their reducing end
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
Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and alpha-L-guluronate at their reducing end
substrate binding, structural change and exolytic mechanism of alginate depolymerization by Alg17c, overview
Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and alpha-L-guluronate at their reducing end
substrate binding, structural change and exolytic mechanism of alginate depolymerization by Alg17c, overview
-
Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and alpha-L-guluronate at their reducing end
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
-
Eliminative cleavage of alginate to give oligosaccharides with 4-deoxy-alpha-L-erythro-hex-4-enuronosyl groups at their non-reducing ends and alpha-L-guluronate at their reducing end
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
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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
-
?
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
-
?
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)
-
-
?
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
-
?
alginate
?
-
high yields of penta-, hex-, and heptasaccharides in the hydrolysis products
?
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
enzyme shows specificity for polyguluronate and polymannuronate units in alginate molecules
-
?
alginate
?
-
enzyme shows specificity for polyguluronate and polymannuronate units in alginate molecules
-
?
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
?
-
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)
?
alginate
?
-
the enzyme endolytically depolymerizes alginate by beta-elimination into oligo-alginates with degrees of polymerization of 2-5
-
?
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
-
?
alginate
?
-
enzyme degrades alginate into a mixture of products with molecular masses below 1000 Da
?
alginate
algino-oligosaccharides
Shewanella sp. YH1
-
about 50% of the activity with poly(alpha-(1,4)-L-guluronate)
-
?
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
-
?
alpha-L-guluronosyl linkage in alginate
?
-
significant activity is found not only on guluronate-guluronate linkages but also on guluronate-mannuronate linkages
-
?
alpha-L-guluronosyl linkage in alginate
?
-
endolyase
-
?
alpha-L-guluronosyl linkage in alginate
?
-
significant activity is found not only on guluronate-guluronate linkages but also on guluronate-mannuronate linkages
-
?
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
-
?
alpha-L-guluronosyl linkage in alginate
?
-
significant activity is found not only on guluronate-guluronate linkages but also on guluronate-mannuronate linkages
-
?
alpha-L-guluronosyl linkage in alginate
?
-
-
enzyme shows activities toward both polyG, i.e. poly-alpha-(1->4)-L-guluronic acid, and polyM, i.e. poly-beta-D-mannuronic acid
?
alpha-L-guluronosyl linkage in alginate
?
-
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
-
?
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
-
?
alpha-L-guluronosyl linkage in alginate
?
-
-
products are six different di-and trisaccharides. The enzymatic hydrolysis occurs between two random guluronic acid or/and mannuronic acid residues, and produces one G residue or M residue on the reducing end and an unsaturated residue on the non-reducing end for all products
?
alpha-L-guluronosyl linkage in alginate
?
-
-
products are six different di-and trisaccharides. The enzymatic hydrolysis occurs between two random guluronic acid or/and mannuronic acid residues, and produces one G residue or M residue on the reducing end and an unsaturated residue on the non-reducing end for all products
?
alpha-L-guluronosyl linkage in alginate
?
-
endolyase
-
?
alpha-L-guluronosyl linkage in alginate
?
-
final degradation products are alginate monosaccharides
?
alpha-L-guluronosyl linkage in alginate
?
-
final degradation products are alginate monosaccharides
?
alpha-L-guluronosyl linkage in alginate
?
preferably degrades G blocks
-
?
alpha-L-guluronosyl linkage in alginate
?
preferably degrades the M block to the G block in alginate
-
?
alpha-L-guluronosyl linkage in alginate
?
preferably degrades the M block to the G block in alginate
-
?
alpha-L-guluronosyl linkage in alginate
?
preferably degrades G blocks
-
?
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
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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