3.2.1.39: glucan endo-1,3-beta-D-glucosidase
This is an abbreviated version!
For detailed information about glucan endo-1,3-beta-D-glucosidase, go to the full flat file.
Word Map on EC 3.2.1.39
-
3.2.1.39
-
chitinase
-
glucans
-
barley
-
beta-glucans
-
pathogenesis-related
-
polysaccharide
-
cellulase
-
beta-1,3-glucans
-
xylanase
-
trichoderma
-
elicitors
-
chitin
-
phytophthora
-
biocontrol
-
callose
-
lichenan
-
solani
-
mannoproteins
-
rhizoctonia
-
transglycosylation
-
defense-related
-
thaumatin-like
-
zymolyase
-
digesta
-
mycoparasitism
-
harzianum
-
laminaribiose
-
mixed-linkage
-
circulans
-
capsici
-
hemicellulase
-
fibrobacter
-
gentiobiose
-
curdlan
-
digitata
-
carbohydrases
-
laminaria
-
pectinase
-
neurexins
-
pharmacology
-
medicine
-
synthesis
-
food industry
-
biotechnology
-
agriculture
-
analysis
- 3.2.1.39
- chitinase
- glucans
- barley
- beta-glucans
-
pathogenesis-related
- polysaccharide
- cellulase
- beta-1,3-glucans
- xylanase
- trichoderma
- elicitors
- chitin
- phytophthora
-
biocontrol
- callose
- lichenan
- solani
-
mannoproteins
- rhizoctonia
-
transglycosylation
-
defense-related
-
thaumatin-like
-
zymolyase
-
digesta
-
mycoparasitism
- harzianum
- laminaribiose
-
mixed-linkage
- circulans
- capsici
-
hemicellulase
-
fibrobacter
- gentiobiose
- curdlan
- digitata
-
carbohydrases
-
laminaria
- pectinase
-
neurexins
- pharmacology
- medicine
- synthesis
- food industry
- biotechnology
- agriculture
- analysis
Reaction
Synonyms
(1-3)-beta-D-glucan endohydrolase, (1-3)-beta-D-glucanase, (1-3)-beta-glucanase GI, (1->3)-beta-glucan endohydrolase, (1->3)-beta-glucan endohydrolase BGN13.1, (1->3)-beta-glucan endohydrolase GI, (1->3)-beta-glucan endohydrolase GII, (1->3)-beta-glucan endohydrolase GIII, (1->3)-beta-glucan endohydrolase GIV, (1->3)-beta-glucan endohydrolase GV, (1->3)-beta-glucan endohydrolase GVI, (1->3)-beta-glucanase, (1->3)-beta-glucanase A1, (1->3)-beta-glucanase BGN13.1, (1->3)-beta-glucanase isoenzyme GI, (1->3)-beta-glucanase isoenzyme GII, (1->3)-beta-glucanase isoenzyme GIII, (1->3)-beta-glucanase isoenzyme GIV, (1->3)-beta-glucanase isoenzyme GV, (1->3)-beta-glucanase isoenzyme GVI, (13)-beta-glucan 3-glucanohydrolase, (13)-beta-glucan endohydrolase, 1,3-beta-D-glucanase, 1,3-beta-glucan 3-glucanohydrolase, 1,3-beta-glucan hydrolase, 1,3-beta-glucanase, 1,3-beta-glucanase I, Acidic beta-1,3-glucanase, acidic endo-beta-1,3-glucanase, AkLam36, Anther-specific protein A6, Ban-Gluc, Basic beta-1,3-endoglucanase BGN13.1, Basic beta-1,3-glucanase, beta-(1-3)-glucanase, beta-1,3 glucanase, beta-1,3-D-glucanase, beta-1,3-endoglucanase, Beta-1,3-endoglucanase GI, Beta-1,3-endoglucanase GII, Beta-1,3-endoglucanase GIII, Beta-1,3-endoglucanase GIV, Beta-1,3-endoglucanase GV, Beta-1,3-endoglucanase GVI, Beta-1,3-endoglucanase, basic, beta-1,3-glucan hydrolase, beta-1,3-glucanase, beta-1,3-glucanase I, beta-1,3-glucanase II, beta-glucanase, Bgl, Bgl2, Bgl64A, BglF, BglII, BglS27, Bglu50A, Bgt17AE158A, CaENG, callase, CC1G_04051, CcGluE, Cel17A, DEHA2G18766g, DEHA2G18766p, EGase1, EGase2, EGase3, endo-(1,3)-beta-D-glucanase, endo-(1-3)-beta-glucanase, endo-(13)-beta-D-glucanase, endo-1,3-beta-D-glucanase, endo-1,3-beta-glucanase, endo-1,3-beta-glucosidase, endo-1,3-glucanase, endo-1,3;4-beta-glucanase, endo-beta-1,3(4)-glucanase, endo-beta-1,3-D-glucanase, endo-beta-1,3-glucanase, endo-beta-1->3-glucanase, endo-type beta-1,3-glucanase, Endo23, Eng, eng1, ENG16A, Eng2, Eng2 protein, EngA, Engl1, exo-beta-1,3-glucanase, Fra e 9.01 allergen, Gbl2a, Gbl2b, Gbl2c, Gbl2d, Gbl2e, Gbl2f, Gbl3, Gfa, GH family 81 beta-1,3-glucanase, GLU, Glu1, GluA, GLUB20-2, glucan endo-1,3-beta-glucosidase, Glucanase GLA, Glucanase GLB, glucanase LIV, glucanase Lo, GLUD2, HdLam33, kitalase, LAM, Lam81A, LamA, laminaranase, laminarinase, Lic16A, lytic beta-(1-3)-glucanase I, lytic beta-(1-3)-glucanase II, Mo enzyme, More, oligo-1,3-glucosidase, OsGlu1, OsGlu2, PCEng2p, PfLamA, PpGns1, PR-2B, PR-35, PR-36, PR-37, Rv0315, SLam, SpsLamIV, TLam, TmLam, VIT_05s0077g01150, VIT_205s0077g01150, VIT_206s0061g00120, VIT_208s0007g06060, YlCrh1Sp, YlCrh2Sp, zerzaust, ZET, ZgLamA
ECTree
3.2.1.39 glucan endo-1,3-beta-D-glucosidaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.2.1.39 - glucan endo-1,3-beta-D-glucosidase
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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
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
laminariheptaose
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
-
gentiobiose, low activity
-
?
alkali soluble 1,3-beta-glucan + H2O
reducing sugar + ?
-
produced by solubilised 1,3-beta-glucan synthase complex of A. fumigatus
-
?
alkaline-treated paramylon + H2O
?
-
78.6% of the activity with laminarin
-
-
?
azurine-crosslinked beta-1,3:1,4-glucan + H2O
?
-
AZCL-barley-beta-glucan, 100fold less active than on AZCL-pachyman
-
?
beta-1,3-1,4-glucan + H2O
?
substrate from Hordeum vulgare, substrate of EC 3.2.1.6, endo-1,3(4)-beta-glucanase
-
-
?
carboxymethyl cellulose + H2O
?
-
49.56% activity compared to laminarin
-
-
?
carboxymethyl-cellulose + H2O
?
-
carboxymethyl-cellulose is only hydrolyzed by YlCrh1Sp
-
-
?
carboxymethylated pachyman + H2O
oligoglucosides
-
86% of activity compared to laminarin from Laminaria digitata
-
-
?
cellobiose + H2O
2 D-glucose
-
0.61% activity compared to laminarin
-
-
?
Glc-beta-(1->4)-Glc-beta-(1->3)-Glc-beta-(1->4)-Glc + H2O
D-glucose + Glc-beta-(1->4)-Glc-beta-(1->3)-Glc
laminarihexose + H2O
laminaritriose + laminaritetraose
active with the wild-type enzyme, but also the active site mutant E259A, that shows residual activity in the substrate complex crystal and cleaves the substrate in two different ways, generating trisaccharides and tetrasaccharides, mass spectrometry
laminaritriose shows higher binding affinity and fully occupies the -1, -2 and -3 sites of the active-site cleft, even at a low molar excess of the substrate. At elevated substrate concentration laminaritetrose also occupies the active site, spanning the opposite sites +1, +2, +3 and +4 of the cleft
-
?
laminarin + H2O
D-glucose + laminaribiose
-
more specific for compounds having beta-1,3-glucosidic linkages
-
-
?
laminarin + H2O
laminaritriose
preferred substrate
main product
-
?
laminarin from Eisenia bicyclis + H2O
oligoglucosides
-
9% of activity compared to laminarin from Laminaria digitata
-
-
?
laminarin from Laminaria digitata + H2O
oligoglucosides
-
-
mixture with different chain length
-
?
laminarioligosaccharide + H2O
D-glucose + laminaribiose + laminaritriose
CaLam digests laminarin and laminarioligosaccharides except laminaribiose as an endo-beta-1,3-glucanase, releasing glucose, laminaribiose and laminaritriose as the major products
-
-
?
laminaripentaose + H2O
D-glucose + laminaritriose + laminaribiose
-
more specific for compounds having beta-1,3-glucosidic linkages
-
-
?
laminaritetraose + H2O
D-glucose + ?
-
more specific for compounds having beta-1,3-glucosidic linkages
-
-
?
laminaritriose + H2O
D-glucose + ?
-
more specific for compounds having beta-1,3-glucosidic linkages
-
-
?
lichenin from Cetraria islandica + H2O
oligoglucosides
-
6% of activity compared to laminarin from Laminaria digitata
-
-
?
mycolaminarin + H2O
reducing sugar
-
highest activity
no glucose release, approximately four glycosidic linkages hydrolyzed per molecule mycolaminarin, predominant product are tetrasaccharides
?
pendulan + H2O
reducing sugar + ?
-
acts in random fashion, reaction product with high molecular weight, major role in decreasing the molecular weight of pendulan during fermentation
-
?
polysaccharide + H2O
ethanol-soluble sugar + ?
-
crude fraction from unripe bananas, not active in polysaccharide fraction from ripe bananas, possible involvement in ripening and/or softening process
-
?
reduced laminarioligosaccharides + H2O
laminaribiose + laminaritriose + laminaritetraose + laminaripentaose
-
velocity of catalytic reaction increases with the number of 1,3-beta-glucosidic bonds, preferentially cleaves between the glucose residues at positions 2 and 3 from the reducing end
-
?
yeast beta-D-glucan + H2O
laminaritriose + laminari-oligosaccharides
-
-
-
?
zymosan + H2O
?
beta-(1->3)-glucose, substrate from Saccharomyces cerevisiae, 9.11% activity compared to curdlan
-
-
?
(1-3)-beta-D-glucan + H2O
laminaritriose + laminaritetraose
-
if derived from marine organisms, other(1-3)-beta-D-glucans are not substrate
main products
-
?
(1-3)-beta-D-glucan + H2O
laminaritriose + laminaritetraose
-
if derived from marine organisms, other(1-3)-beta-D-glucans are not substrate
main products
-
?
(1-3:1-4)-beta-D-glucan + H2O
?
-
release of cellobiose as main product
-
?
(1-3:1-4)-beta-D-glucan + H2O
?
-
from cereals, limited action, due to action at few consecutive beta-1,3-linked glucose residues
-
?
2 laminaripentaose + H2O
octasaccharide + ?
transglycosylation activity, product is a linear beta-1,3-octasaccharide containing an intrachain beta-1,6 linkage
-
-
?
2 laminaripentaose + H2O
octasaccharide + ?
transglycosylation activity, product is a linear beta-1,3-octasaccharide containing an intrachain beta-1,6 linkage
-
-
?
3-O-beta-D-Glc-D-Glc-D-Glc + H2O
?
Flavobacterium dormitator
-
releases laminaribiose and glucose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc + H2O
?
-
releases laminaribiose and glucose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc + H2O
?
-
smallest substrate, products are smaller oligosaccharides and glucose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
end-products are laminaritriose, laminaribiose and glucose, exhibits weak glucosyltransferase activity
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
release of laminaritriose and glucose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
laminaritetraose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
laminaritetraose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
end-product laminaribiose, no glucose release
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
products are smaller oligosaccharides and glucose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
laminaripentaose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
laminaripentaose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
end-products laminaritriose and laminaribiose, no glucose release
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
laminaripentaose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
laminaripentaose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
laminaripentaose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
laminarihexaose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
main product laminaritriose, small amounts laminaritriose and laminaribiose, no glucose release
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
-
laminarihexaose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
Flavobacterium dormitator
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
low activity
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
-
laminaribiose
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
2% of activity compared to laminaran from Laminaria cichorioides
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
7% of activity compared to laminaran from Laminaria cichorioides
-
-
?
barley beta-glucan + H2O
?
16.20% activity compared to curdlan
-
-
?
barley beta-glucan + H2O
?
16.20% activity compared to curdlan
-
-
?
barley beta-glucan + H2O
?
main linkage type beta-1,3-1,4(Glc), about 10% of the specific activity compared to laminarin
-
-
?
beta-1,3-glucan + H2O
?
-
sources: Pediococcus parvalus and yeast
-
-
?
beta-1,3-glucan + H2O
?
-
sources: Pediococcus parvalus and yeast
-
-
?
beta-1,3-glucan + H2O
?
-
25% of the activity with curdlan
-
-
?
beta-glucan + H2O
?
-
beta-glucanases I and II differ in substrate affinity according to the degree of its polymerization, complete degradation of yeast glucan is determined by synergistic activities of more than one beta-glucanase
-
?
beta-glucan + H2O
?
-
beta-glucanases I and II differ in substrate affinity according to the degree of its polymerization, complete degradation of yeast glucan is determined by synergistic activities of more than one beta-glucanase
-
?
beta-glucan + H2O
?
Fungi imperfecti
-
beta-1,3-glucanase of the random type, producing more higher oligosaccharides
-
?
beta-glucan + H2O
?
-
from cell wall polysaccharide extracts of fruits or from barley, activites and substrate specificities of enzymes from different cultivars, overview
-
-
?
beta-glucan + H2O
?
-
rapid reduction up to 60% on the turbidity of substrate suspension, slow and very little release of glucose and reducing sugars
-
?
beta-glucan + H2O
?
Barley beta-glucan, 1,3-1,4-beta-glucose monomers, high activity
-
-
?
beta-glucan + H2O
?
-
macro- and micro-assay method development and evaluation, overview
-
-
?
beta-glucan + H2O
?
-
macro- and micro-assay method development and evaluation, overview
-
-
?
carboxymethyl curdlan + H2O
?
13.7% of the activity with laminarin
-
-
?
carboxymethyl pachyman + H2O
?
-
135% of the activity with laminarin
-
-
?
carboxymethyl pachyman + H2O
?
-
135% of the activity with laminarin
-
-
?
carboxymethyl pachyman + H2O
?
9.1% of the activity with laminarin
-
-
?
carboxymethyl-pachyman + H2O
?
1.7% activity compared to laminarin
-
-
?
carboxymethylated pachyman + H2O
D-glucose + ?
Eulota maakii
-
7% of activity compared to laminaran from Laminaria cichorioides
-
-
?
carboxymethylated pachyman + H2O
D-glucose + ?
-
14% of activity compared to laminaran from Laminaria cichorioides
-
-
?
carboxymethylated pachyman + H2O
D-glucose + ?
-
24% of activity compared to laminaran from Laminaria cichorioides
-
-
?
cell wall glucan + H2O
reducing sugar + ?
-
from Fusarium oxysporum f. sp. apii, possible inducible antimicrobial defense system in plants
-
?
cell wall glucan + H2O
reducing sugar + ?
-
putative role during cell wall morphogenesis
-
?
cell wall glucan + H2O
reducing sugar + ?
-
from fungi
-
?
cell wall glucan + H2O
reducing sugar + ?
Flavobacterium dormitator
-
living yeast cells
-
?
cell wall glucan + H2O
reducing sugar + ?
-
from Phytophthora megasperma, carbohydrate release to elicit glyceollin accumulation in cotyledons
-
?
cell wall glucan + H2O
reducing sugar + ?
-
cell wall autolysis
-
?
cell wall glucan + H2O
reducing sugar + ?
-
involved in modification and limited degradation of the cell wall during cell life cycle
-
?
cell wall glucan + H2O
reducing sugar + ?
-
cell wall autolysis
-
?
cell wall glucan + H2O
reducing sugar + ?
-
from different fungi, containing beta-1,3-, beta-1,4 and/or beta-1,6-linkages
-
?
cell wall glucan + H2O
reducing sugar + ?
-
from yeast and different fungi, slight activity, involvement in mycoparasitism
-
?
curdlan + H2O
?
100% activity. When curdlan is used as the substrate, hydrolysis products mainly range from glucose to tetrasaccharide
-
-
?
curdlan + H2O
?
Pseudomonas aeruginosa CAU 342A
100% activity. When curdlan is used as the substrate, hydrolysis products mainly range from glucose to tetrasaccharide
-
-
?
curdlan + H2O
glucobiose + glucotriose
beta-(1->3)-(glucose), substrate from Agrobacterium sp., recombinant CcGluE hydrolyses curdlan powder effectively. The hydrolytic products of curdlan are glucan oligosaccharides with degrees of polymerisation of 2-13, and the main products are glucobiose and glucotriose, overview
-
-
?
curdlan + H2O
glucobiose + glucotriose
degradation
-
-
?
curdlan + H2O
laminaribiose + laminaritriose
100% activity
-
-
?
curdlan + H2O
laminarioligosaccharides + laminaribiose
-
the enzyme hydrolyzes selectively curdlan containing only beta-1,3 linkages
hydrolysis of curdlan powder results in the accumulation of laminaribiose
-
?
curdlan + H2O
laminarioligosaccharides + laminaribiose
-
the enzyme hydrolyzes selectively curdlan containing only beta-1,3 linkages
hydrolysis of curdlan powder results in the accumulation of laminaribiose
-
?
curdlan + H2O
laminaritriose + laminaribiose
-
water-insoluble curdlan, best substrate
main products, plus minor amounts of D-glucose and laminaritetraose
-
?
curdlan + H2O
laminaritriose + laminaribiose
-
water-insoluble curdlan, best substrate
main products, plus minor amounts of D-glucose and laminaritetraose
-
?
Glc-beta-(1->4)-Glc-beta-(1->3)-Glc-beta-(1->4)-Glc + H2O
D-glucose + Glc-beta-(1->4)-Glc-beta-(1->3)-Glc
-
containing one beta-1,4-linkage separated by one beta-1,3-linkage, i.e. G4G3G, which is not further degraded
-
?
Glc-beta-(1->4)-Glc-beta-(1->3)-Glc-beta-(1->4)-Glc + H2O
D-glucose + Glc-beta-(1->4)-Glc-beta-(1->3)-Glc
-
containing one beta-1,4-linkage separated by one beta-1,3-linkage, i.e. G4G3G, which is not further degraded
-
?
laminaran from Laminaria cichorioides + H2O
D-glucose + ?
Eulota maakii
-
-
glucose content in products about 90%
-
?
laminaran from Laminaria cichorioides + H2O
D-glucose + ?
-
-
glucose content in products about 40%
-
?
laminaran from Laminaria cichorioides + H2O
D-glucose + ?
-
-
glucose content in products about 33%, retention of the glycoside bond configuration
-
?
Laminaria digitata laminarin + H2O
laminarioligosaccharides
-
contains a small amount of beta-1,6 linkages compared with curdlan
-
-
?
Laminaria digitata laminarin + H2O
laminarioligosaccharides
-
contains a small amount of beta-1,6 linkages compared with curdlan
-
-
?
laminaribiose + H2O
?
wild-type enzyme performs glucosidase activity on laminarioligosaccharides, while the mutant performs transglycosylation
-
-
?
laminaribiose + H2O
?
wild-type enzyme performs glucosidase activity on laminarioligosaccharides, while the mutant performs transglycosylation
-
-
?
laminarin + H2O
?
13% of activity compared to barley beta-glucan
-
-
?
laminarin + H2O
?
13% of activity compared to barley beta-glucan
-
-
?
laminarin + H2O
?
-
best substrate, the enzyme shows an endo-type cleavage mode and hydrolyzes laminarin into glucoses, disaccharides, trioligosaccharides, and tetraoligosaccharides
-
-
?
laminarin + H2O
?
beta-(1->3)-glucose, 44.47% activity compared to curdlan
-
-
?
laminarin + H2O
?
beta-(1->3)-glucose, 44.47% activity compared to curdlan
-
-
?
laminarin + H2O
?
47.6% activity compared to curdlan
-
-
?
laminarin + H2O
?
72.2% activity compared to curdlan. When laminarin is used as the substrate, major products are a series of beta-1,3-oligosaccharides with degree of polymerization from 1 to 5
-
-
?
laminarin + H2O
?
Pseudomonas aeruginosa CAU 342A
72.2% activity compared to curdlan. When laminarin is used as the substrate, major products are a series of beta-1,3-oligosaccharides with degree of polymerization from 1 to 5
-
-
?
laminarin + H2O
?
main linkage type beta-1,3-(Glc). The enzyme cleaves laminarin randomly, yielding glucose, laminaribiose, and higher laminari-oligosaccharides
-
-
?
laminarin + H2O
?
the wild-type enzyme displays a bent topology adapted to the binding of helical-shaped laminarin
-
-
?
laminarin + H2O
?
the wild-type enzyme displays a bent topology adapted to the binding of helical-shaped laminarin
-
-
?
laminarin + H2O
D-glucose + ?
-
best substrate, specific for for 1,3-beta-glucans in which 1,6-beta-linkages are present
-
?
laminarin + H2O
D-glucose + ?
-
soluble reduced 1,3-beta-glucan, release of reducing 1,3-beta-oligosaccharides of variable size, presence of a single 1,6-beta branched glucose every three glucose units of a linear 1,3-beta-glucan chain prevents hydrolysis
-
?
laminarin + H2O
D-glucose + ?
-
specifically hydrolyzes (1-3)-beta-glycosidic linkages, predominant products are laminaribiose and laminaritriose, minor amounts of glucose and higher oligosaccharides
-
?
laminarin + H2O
D-glucose + ?
-
major products are glucose, laminaribiose, laminaritriose, laminaritetraose and higher liminarioligosaccharides
-
?
laminarin + H2O
D-glucose + ?
-
highly specific to hydrolyse beta-1,3-glycosidic bonds
-
?
laminarin + H2O
D-glucose + ?
-
soluble laminarin, no glucose release
-
?
laminarin + H2O
D-glucose + ?
Flavobacterium dormitator
-
major products are glucose, laminaribiose, laminaritriose, laminaritetraose and higher liminarioligosaccharides
-
?
laminarin + H2O
D-glucose + ?
-
release of laminarisaccharides with polymerization degree from 1-7
-
?
laminarin + H2O
D-glucose + ?
-
devoid of debranching activity, depolymerizes the unbranched portions of the beta-(1-3), beta-(1-6)-glucan, down to laminaritriose, retaining the anomeric configuration
-
?
laminarin + H2O
D-glucose + ?
-
hydrolysis at highest rates by isoform GI, lower hydrolysis by isoform GII, enzyme requires a long run of contiguous beta-1,3-D-glucosidic linkages, where glucosyl units neither substituted nor branched
-
?
laminarin + H2O
D-glucose + ?
-
functional opportunities to inhibit the advance of pathogenic fungi
-
?
laminarin + H2O
D-glucose + ?
-
major products are glucose, laminaribiose, laminaritriose, laminaritetraose and higher liminarioligosaccharides
-
?
laminarin + H2O
D-glucose + ?
-
highest rates from Laminaria digitata, major products are laminaribiose and laminaritriose for isoforms GII and GIII, GI yields predominantly (1-3)-beta-D-oligoglucosides greater than 4 units
-
?
laminarin + H2O
D-glucose + ?
-
end-products are laminarihexaose to laminaritriose, some glucose and little gentiobiose for lytic beta-(1-3)-glucanase I
-
?
laminarin + H2O
D-glucose + ?
-
release of laminaritetraose, laminaritriose, laminaribiose and glucose
-
?
laminarin + H2O
D-glucose + ?
-
from Laminaria digitata, lower rates are from Laminaria hyperborea and Eisenia bicyclis, best substrates are unbranched (1-3)-beta-D-glucans
-
?
laminarin + H2O
D-glucose + ?
-
end-products are laminaritriose, laminaribiose and glucose
-
?
laminarin + H2O
D-glucose + ?
-
accumulation of the enzyme after inoculation with fungi, involvement in pathogenesis in relation to active plant defense
-
?
laminarin + H2O
D-glucose + ?
-
action of enzyme requires oligomers with glucose units more than 9
-
?
laminarin + H2O
D-glucose + ?
-
different product patterns for glucanases I, IIIB, IV and V
-
?
laminarin + H2O
D-glucose + ?
-
major products are laminaribiose and laminaritriose
-
?
laminarin + H2O
D-glucose + ?
-
product distribution consistent of 20% laminaribiose, 30% laminaritriose and 50% higher oligosaccharides
-
?
laminarin + H2O
D-glucose + ?
-
specifically hydrolyzes (1-3)-beta-glycosidic linkages, predominant products are laminaribiose and laminaritriose, minor amounts of glucose and higher oligosaccharides
-
?
laminarin + H2O
D-glucose + ?
-
specifically hydrolyzes beta-1,3-bonds, final products are glucose, laminaribiose and laminaritetraose
-
?
laminarin + H2O
D-glucose + ?
-
accumulation of the enzyme after inoculation with fungi, involvement in pathogenesis in relation to active plant defense
-
?
laminarin + H2O
D-glucose + ?
-
very active against substrates containing beta-1,3-linkages, mainly disaccharides and oligosaccharides produced, involvement in mycoparasitism
-
?
laminarin + H2O
D-glucose + ?
-
specifically hydrolyzes beta-1,3-bonds, final products are glucose, laminaribiose and laminaritetraose
-
?
laminarin + H2O
D-glucose + ?
-
only active against glucans containing beta-1,3-linkages
-
?
laminarin + H2O
D-glucose + ?
-
highly specific to hydrolyse beta-1,3-glycosidic bonds
-
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose
CaLam digests laminarin and laminarioligosaccharides except laminaribiose as an endo-beta-1,3-glucanase, releasing glucose, laminaribiose and laminaritriose as the major products
-
-
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose
-
major products, enzyme most frequently attacks the bond between the 3rd and 4th residue from the non-reducing end
-
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose
-
major products, enzyme most frequently attacks the bond between the 3rd and 4th residue from the non-reducing end
-
?
laminarin + H2O
D-glucose + laminarioligosaccharides
-
-
-
-
?
laminarin + H2O
D-glucose + laminarioligosaccharides
endolytic depolymerization of glucans composed of beta-1,3-linked main chains
-
-
?
laminarin + H2O
D-glucose + laminarioligosaccharides
-
-
if the degree of cleavage of laminarin under exhaustive hydrolysis reaches 74%, the major products are glucose and di-, tri-, and tetrasaccharides
-
?
laminarin + H2O
laminaribiose + laminaritriose
-
5% of the activity with curdlan
-
-
?
laminarin + H2O
laminaribiose + laminaritriose
-
5% of the activity with curdlan
-
-
?
laminarin + H2O
laminaribiose + laminaritriose + laminaritetraose
-
-
main reaction products
-
?
laminarin + H2O
laminaribiose + laminaritriose + laminaritetraose
-
-
main reaction products
-
?
laminarin + H2O
laminaribiose + laminaritriose + laminaritetraose
-
-
main reaction products
-
?
laminarin + H2O
laminaritriose + ?
-
the mutant enzyme W203F fused to 1,3-beta-D-glucanase catalytic domain shows a 3.6fold increase in specific activity against laminarin as compared with the 1,3-beta-D-glucanase catalytic domain alone with laminaritriose as the major product
major product
-
?
laminarin + H2O
laminaritriose + ?
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
-
the mutant enzyme W203F fused to 1,3-beta-D-glucanase catalytic domain shows a 3.6fold increase in specific activity against laminarin as compared with the 1,3-beta-D-glucanase catalytic domain alone with laminaritriose as the major product
major product
-
?
laminarin + H2O
laminaritrisaccharides + laminaritetrasaccharides
laminarin from Saccharina cichorioides with molecular weight of 3.5 kDa
-
-
?
laminarin + H2O
laminaritrisaccharides + laminaritetrasaccharides
laminarin from Saccharina cichorioides with molecular weight of 3.5 kDa
-
-
?
laminarioligosaccharide + H2O
laminaribiose + beta-D-glucose
-
e.g. laminaritetraose
-
-
?
laminarioligosaccharide + H2O
laminaribiose + beta-D-glucose
-
-
-
?
laminarioligosaccharide + H2O
laminaribiose + beta-D-glucose
substrate specificities and products, overview
-
-
?
laminaripentaose + H2O
laminaritetraose + ?
efficient hydrolytic activity
-
-
?
laminaripentaose + H2O
laminaritetraose + ?
efficient hydrolytic activity
-
-
?
laminaritetraose + H2O
laminaritriose + ?
efficient hydrolytic activity
-
-
?
laminaritetraose + H2O
laminaritriose + ?
efficient hydrolytic activity
-
-
?
laminaritriose + H2O
?
wild-type enzyme performs glucosidase activity on laminarioligosaccharides, while the mutant performs transglycosylation
-
-
?
laminaritriose + H2O
?
wild-type enzyme performs glucosidase activity on laminarioligosaccharides, while the mutant performs transglycosylation
-
-
?
laminaritriose + H2O
D-glucose + laminaribiose
-
-
-
?
laminaritriose + H2O
D-glucose + laminaribiose
the smallest oligosaccharide that can be degraded by the enzyme
-
-
?
laminaritriose + H2O
D-glucose + laminaribiose
the smallest oligosaccharide that can be degraded by the enzyme
-
-
?
lichenan + H2O
?
90% of activity compared to barley beta-glucan
-
-
?
lichenan + H2O
?
90% of activity compared to barley beta-glucan
-
-
?
lichenan + H2O
?
main linkage type beta-1,3-1,4(Glc), about 10% of the specific activity compared to laminarin
-
-
?
lichenan + H2O
D-glucose + ?
Eulota maakii
-
16% of activity compared to laminaran from Laminaria cichorioides
-
-
?
lichenan + H2O
D-glucose + ?
-
20% of activity compared to laminaran from Laminaria cichorioides
-
-
?
lichenan + H2O
D-glucose + ?
-
22% of activity compared to laminaran from Laminaria cichorioides
-
-
?
O-carboxymethyl-(1,3:1,6)-beta-D-glucan + H2O
?
-
from yeast, low activity
-
?
O-carboxymethyl-(1,3:1,6)-beta-D-glucan + H2O
?
-
from yeast, low activity
-
?
O-carboxymethyl-pachyman + H2O
?
-
release of laminarisaccharides ranging in polymerization degree from 1-7
-
?
O-carboxymethyl-pachyman + H2O
?
-
faster hydrolysis by isoform GII than by isoform GI, isoform GII may play a role in response to fungal infection
-
?
O-carboxymethyl-pachyman + H2O
?
-
rate of hydrolysis decreases as degree of substitutions increases, requirement for three unsubstituted beta-1,3-glycosyl residues
-
?
O-carboxymethyl-pachyman + H2O
?
-
unbranched (1-3)-beta-glucan from Poria cocos
-
?
pachyman + H2O
?
-
release of laminarisaccharides in polymerization degree form 1-7
-
?
pachyman + H2O
?
most favored substrate, 223% activity compared to curdlan
-
-
?
pachyman + H2O
?
most favored substrate, 223% activity compared to curdlan
-
-
?
pachyman + H2O
?
-
insoluble pachyman, more affinity than on soluble, short-chain pachyman, forms L-1 and L-2 release predominantly pentaose, form L-4 yields a mixture from biose to heptaose
-
?
pachyman + H2O
D-glucose + ?
-
10% of activity compared to laminaran from Laminaria cichorioides
-
-
?
pachyman + H2O
D-glucose + ?
-
13% of activity compared to laminaran from Laminaria cichorioides
-
-
?
paramylon + H2O
?
-
23.4% of the activity with laminarin
the enzyme effectively produces soluble beta-1,3-glucans from alkaline-treated Euglena freeze-dried powder containing paramylon
-
?
paramylon + H2O
?
-
action of endo-beta-1,3-glucanase on the microwave-pretreated paramylon produces soluble beta-1,3-glucans with degrees of polymerisation (DP) ranging from 2-59
-
-
?
periodate-oxidized laminaran + H2O
D-glucose + ?
Eulota maakii
-
0.5% of activity compared to laminaran from Laminaria cichorioides
-
-
?
periodate-oxidized laminaran + H2O
D-glucose + ?
-
90% of activity compared to laminaran from Laminaria cichorioides
-
-
?
periodate-oxidized laminaran + H2O
D-glucose + ?
-
85% of activity compared to laminaran from Laminaria cichorioides
-
-
?
periodate-oxidized laminarin + H2O
?
98% activity compared to laminarin
-
-
?
periodate-oxidized laminarin + H2O
?
98% activity compared to laminarin
-
-
?
periodate-oxidized laminarin + H2O
?
-
100% of the activity with laminarin
-
-
?
reduced laminarin + H2O
laminaritriose + laminaritetraose + laminari-oligosaccharides
high hydrolytic activity
-
-
?
reduced laminarin + H2O
laminaritriose + laminaritetraose + laminari-oligosaccharides
high hydrolytic activity
-
-
?
schizophyllan + H2O
?
-
from Schizophyllum commune, low activity
-
?
additional information
?
-
-
no activity towards chitosan, lichenan, carboxymethylcellulose, amylose, and p-nitrophenyl beta-D-glucopyranoside
-
-
?
additional information
?
-
-
the enzyme exerts relatively high specific activity toward the glucans comprising beta-1,3-glycosidic bond, such as laminarin, pachyman, and barley beta-glucan, with relative activity of 100%, 78.86%, and 40.18%, respectively. Low activity with zymosan A, carboxymethylcellulose-Na, and agarose
-
-
?
additional information
?
-
-
AkLam36 specific for beta-1,3-glucosyl linkages. AkLam36 is an endolytic enzyme degrading laminarin and laminarioligosaccharides to laminaritriose, laminaribiose, and D-glucose. AkLam36 shows higher activity toward beta-1,3-glucans with a few beta-1,6-linked glucose branches such as Laminaria digitata laminarin than highly branched beta-1,3-glucans such as Eisenia bicyclis laminarin
-
-
?
additional information
?
-
-
enzyme preferentially acts on soluble beta-1,3-glucans. Additional transferase activity for oligosaccharides of a low degree of polymerization
-
-
?
additional information
?
-
-
enzyme is involved in the autolytic cell wall degradation resulting from carbon starvation of the fungus and liberates reducing sugars from cell debris
-
-
?
additional information
?
-
-
enzyme hydrolyzes soluble and insoluble (1-3)-beta-D-glucan chains
-
-
?
additional information
?
-
-
no substrate: pustulan, p-nitrophenyl-beta-D-glucopyranoside
-
-
?
additional information
?
-
-
no substrate: laminaribiose or laminaritriose, carboxymethyl cellulose, chitin, and pustulan
-
-
?
additional information
?
-
cGluE shows high endo-beta-(1->3) glucanase activity and low beta-1,4 and beta-1,6 glucanase activities with broad substrate specificity for glucan, including curdlan, laminarin and beta-(1->3)/(1->6)-glucan, and the highest catalytic activity for curdlan. The enzyme exerts beta-(1->3)-glucan-degrading activity
-
-
?
additional information
?
-
-
cGluE shows high endo-beta-(1->3) glucanase activity and low beta-1,4 and beta-1,6 glucanase activities with broad substrate specificity for glucan, including curdlan, laminarin and beta-(1->3)/(1->6)-glucan, and the highest catalytic activity for curdlan. The enzyme exerts beta-(1->3)-glucan-degrading activity
-
-
?
additional information
?
-
cGluE shows high endo-beta-(1->3) glucanase activity and low beta-1,4 and beta-1,6 glucanase activities with broad substrate specificity for glucan, including curdlan, laminarin and beta-(1->3)/(1->6)-glucan, e.g. chitosan from crab shell and water-soluble starch from Ipomoea batatas, and the highest catalytic activity for curdlan. Degradation mode analysis indicates that CcGluE is more likely to hydrolyse glucopentaose and reveals that CcGluE is an endoglucanase. Curdlan is insoluble because of its special structure, which greatly limits the efficiency of the enzyme degradation of curdlan, but a homogenising pre-treatment method with curdlan, improves the degradation efficiency of CcGluE for curdlan powder by 7.1fold, overview. No activity with inulin, microcrystalline cellulose, carboxymethylcellulose, gel-chitin, and alpha-chitin
-
-
?
additional information
?
-
-
cGluE shows high endo-beta-(1->3) glucanase activity and low beta-1,4 and beta-1,6 glucanase activities with broad substrate specificity for glucan, including curdlan, laminarin and beta-(1->3)/(1->6)-glucan, e.g. chitosan from crab shell and water-soluble starch from Ipomoea batatas, and the highest catalytic activity for curdlan. Degradation mode analysis indicates that CcGluE is more likely to hydrolyse glucopentaose and reveals that CcGluE is an endoglucanase. Curdlan is insoluble because of its special structure, which greatly limits the efficiency of the enzyme degradation of curdlan, but a homogenising pre-treatment method with curdlan, improves the degradation efficiency of CcGluE for curdlan powder by 7.1fold, overview. No activity with inulin, microcrystalline cellulose, carboxymethylcellulose, gel-chitin, and alpha-chitin
-
-
?
additional information
?
-
-
no substrate: laminaribiose or laminaritriose, carboxymethyl cellulose, chitin, and pustulan
-
-
?
additional information
?
-
cGluE shows high endo-beta-(1->3) glucanase activity and low beta-1,4 and beta-1,6 glucanase activities with broad substrate specificity for glucan, including curdlan, laminarin and beta-(1->3)/(1->6)-glucan, and the highest catalytic activity for curdlan. The enzyme exerts beta-(1->3)-glucan-degrading activity
-
-
?
additional information
?
-
cGluE shows high endo-beta-(1->3) glucanase activity and low beta-1,4 and beta-1,6 glucanase activities with broad substrate specificity for glucan, including curdlan, laminarin and beta-(1->3)/(1->6)-glucan, e.g. chitosan from crab shell and water-soluble starch from Ipomoea batatas, and the highest catalytic activity for curdlan. Degradation mode analysis indicates that CcGluE is more likely to hydrolyse glucopentaose and reveals that CcGluE is an endoglucanase. Curdlan is insoluble because of its special structure, which greatly limits the efficiency of the enzyme degradation of curdlan, but a homogenising pre-treatment method with curdlan, improves the degradation efficiency of CcGluE for curdlan powder by 7.1fold, overview. No activity with inulin, microcrystalline cellulose, carboxymethylcellulose, gel-chitin, and alpha-chitin
-
-
?
additional information
?
-
no substrates: laminaribiose, pustulan, carboxymethyl cellulose
-
-
?
additional information
?
-
the enzyme does not act on substrates containing only beta-1,4-glycosidic bondas (like carboxymethyl cellulose) or beta-1,6-glycosidic bonds (like pustulan)
-
-
?
additional information
?
-
-
the enzyme does not act on substrates containing only beta-1,4-glycosidic bondas (like carboxymethyl cellulose) or beta-1,6-glycosidic bonds (like pustulan)
-
-
?
additional information
?
-
-
the enzyme does not act on substrates containing only beta-1,4-glycosidic bondas (like carboxymethyl cellulose) or beta-1,6-glycosidic bonds (like pustulan)
-
-
?
additional information
?
-
no substrates: laminaribiose, pustulan, carboxymethyl cellulose
-
-
?
additional information
?
-
-
enzyme cleaves cell wall debris of yeast Pichia fermentans, Zygosaccharomyces bailii, Saccharomycodes ludwigii, Dekkera bruxellensis. No substrate: xylan, pustulan, carboxymethyl cellulose, dextran
-
-
?
additional information
?
-
-
enzyme cleaves cell wall debris of yeast Pichia fermentans, Zygosaccharomyces bailii, Saccharomycodes ludwigii, Dekkera bruxellensis. No substrate: xylan, pustulan, carboxymethyl cellulose, dextran
-
-
?
additional information
?
-
-
the enzyme is inducible with a complex plant beta-glucan laminarin from which it releases simple saccharides when supplied to leaves as a substrate
-
-
?
additional information
?
-
-
the enzyme is inducible with a complex plant beta-glucan laminarin from which it releases simple saccharides when supplied to leaves as a substrate
-
-
?
additional information
?
-
-
enzyme additionally catalyzes a transglycosylation reaction by which reaction products with a higher molecular weight than the supplied substrates are initially generated. Ultimately the substrates are degraded into glucose, laminaribiose and laminaritriose
-
-
?
additional information
?
-
Eulota maakii
-
no substrate: pachyman, p-nitrophenyl-beta-D-glucopyranoside
-
-
?
additional information
?
-
-
enzyme catalyzes transfer of the glyconic part of a substrate molecule on methyl-beta-D-xylopyranoside, glycerol and methyl-alpha-D-glucopyranoside. Low activity on yeast glucan, no substrates: pachyman and aubasidan, pustulan, pullulan, amylopectin, and carboxymethylcellulose
-
-
?
additional information
?
-
enzyme catalyzes transfer of the glyconic part of a substrate molecule on methyl-beta-D-xylopyranoside, glycerol and methyl-alpha-D-glucopyranoside. Low activity on yeast glucan, no substrates: pachyman and aubasidan, pustulan, pullulan, amylopectin, and carboxymethylcellulose
-
-
?
additional information
?
-
-
the enzyme catalyzes transfer of glyconic part of substrate molecule on methyl-beta-D-xylopyranoside, glycerol and methyl-alpha-D-glucopyranoside
-
-
?
additional information
?
-
the enzyme catalyzes transfer of glyconic part of substrate molecule on methyl-beta-D-xylopyranoside, glycerol and methyl-alpha-D-glucopyranoside
-
-
?
additional information
?
-
-
the enzyme has no ability to degrade pachiman, aubasidan, pustulan, pullulan, amylopectin, and carboxymethyl-cellulose
-
-
?
additional information
?
-
the enzyme has no ability to degrade pachiman, aubasidan, pustulan, pullulan, amylopectin, and carboxymethyl-cellulose
-
-
?
additional information
?
-
-
the enzyme catalyzes transfer of glyconic part of substrate molecule on methyl-beta-D-xylopyranoside, glycerol and methyl-alpha-D-glucopyranoside
-
-
?
additional information
?
-
the enzyme catalyzes transfer of glyconic part of substrate molecule on methyl-beta-D-xylopyranoside, glycerol and methyl-alpha-D-glucopyranoside
-
-
?
additional information
?
-
-
the enzyme has no ability to degrade pachiman, aubasidan, pustulan, pullulan, amylopectin, and carboxymethyl-cellulose
-
-
?
additional information
?
-
the enzyme has no ability to degrade pachiman, aubasidan, pustulan, pullulan, amylopectin, and carboxymethyl-cellulose
-
-
?
additional information
?
-
-
enzyme catalyzes transfer of the glyconic part of a substrate molecule on methyl-beta-D-xylopyranoside, glycerol and methyl-alpha-D-glucopyranoside. Low activity on yeast glucan, no substrates: pachyman and aubasidan, pustulan, pullulan, amylopectin, and carboxymethylcellulose
-
-
?
additional information
?
-
enzyme catalyzes transfer of the glyconic part of a substrate molecule on methyl-beta-D-xylopyranoside, glycerol and methyl-alpha-D-glucopyranoside. Low activity on yeast glucan, no substrates: pachyman and aubasidan, pustulan, pullulan, amylopectin, and carboxymethylcellulose
-
-
?
additional information
?
-
-
laminarinase mainly hydrolyses beta?1,3-glycosidic bonds, with negligible activity towards beta-1,4-glycosidic bonds
-
-
?
additional information
?
-
-
laminarinase mainly hydrolyses beta?1,3-glycosidic bonds, with negligible activity towards beta-1,4-glycosidic bonds
-
-
?
additional information
?
-
HdLam33 possesses transglycosylation activity splitting glycoside linkage in a retaining manner, overview. It also shows activity of EC 3.2.1.6, endo-1,3(4)-beta-glucanase
-
-
?
additional information
?
-
-
HdLam33 possesses transglycosylation activity splitting glycoside linkage in a retaining manner, overview. It also shows activity of EC 3.2.1.6, endo-1,3(4)-beta-glucanase
-
-
?
additional information
?
-
-
hydrothermal microwave pretreatment of substrate paramylon at 170 °C for 2 min is established to facilitate the enzymatic production of soluble bioactive beta-1,3-glucans from the recalcitrant substrate paramylon, structure comparisons of paramylon granules with and without heat treatment, overview. Virtual absence of enzymatic hydrolysis of paramylon pretreated at the lower incubation temperatures may be explained by steric hindrance of the enzymes
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additional information
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no activity with xylan, colloidal chitin, carboxymethylcellulose, polygalacturonic acid, and pectin
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additional information
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no activity with xylan, colloidal chitin, carboxymethylcellulose, polygalacturonic acid, and pectin
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additional information
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no substrate: beta-1,3-1,4-glucans such as barley glucan or lichenan, or beta-1,6 glucans such as pustulan
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additional information
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Littorina kurila
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narrow substrate specificity, hydrolyzes only the (1-3)-beta-D-glucosidic bonds in the mixed (1-3),(1-6)- and (1-3),(1-4)-beta-D-glucans down to glucose and glucooligosaccharides. Enzyme acts with retention of the anomeric configuration and additionally catalyzes transglycosylation reactions
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additional information
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no substrate: starch, cellulose, chitin, chitosan
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additional information
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OsGlu1 may act in the defense response to pathogen attack
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additional information
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OsGlu1 may act in the defense response to pathogen attack
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additional information
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OsGlu1 may act in the defense response to pathogen attack
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additional information
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the catalytic module has an inhibitory effect on the growth of Candida albicans and Rhizoctonia solani. The presence of the carbohydrate-binding module and the analogue of coagulation factor Fa5/8C enhance the inhibitory effect
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additional information
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the catalytic module specifically hydrolyzes beta-1,3- and beta-1,3-1,4-glucan. The catalytic module has an inhibitory effect on the growth of Candida albicans and Rhizoctonia solani. The presence of the carbohydrate-binding module and the analogue of coagulation factor Fa5/8C enhance the inhibitory effect
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additional information
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poor substrates: yeast glucan, pachyman, amylopectin, carboxymethy cellulose, and pustulan
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additional information
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no substrate: starch, cellulose, chitin, chitosan
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additional information
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endo-1,3-beta-D-glucanases catalyze the hydrolysis of internal beta-(1,3)-O-glycosidic bonds
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additional information
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the enzyme does not display activity towards agarose, pachyman, Zymosan A, barley beta-glucan, and (carboxymethyl)cellulose
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additional information
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Pseudomonas aeruginosa CAU 342A
the enzyme does not display activity towards agarose, pachyman, Zymosan A, barley beta-glucan, and (carboxymethyl)cellulose
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additional information
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besides endo-activity, enzyme has some exo-activity, and catalyzes hydrolysis of mixed-linked oligosaccharides with both beta-1,3 and beta-1,4 specificities
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additional information
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no activity with cellulose, xylan and chitin
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additional information
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no activity with cellulose, xylan and chitin
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additional information
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enzyme does not hydrolyze beta-1,4 linkages present in cellooligosaccharides such as cellobiose, cellotriose, cellotetraose and cellopentaose
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additional information
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the enzyme hardly cleaves the beta-1,3 linkage in laminaribiose
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additional information
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the enzyme hardly cleaves the beta-1,3 linkage in laminaribiose
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additional information
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the enzyme hardly cleaves the beta-1,3 linkage in laminaribiose
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additional information
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the enzyme hardly cleaves the beta-1,3 linkage in laminaribiose
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additional information
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laminaribiose and laminaritriose are no substrates, laminaritetraose is very inefficiently cleaved
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additional information
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role as a regulator for the acid trehalase activity by association in the enzyme aggregate
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additional information
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laminaribiose and laminaritriose are no substrates, laminaritetraose is very inefficiently cleaved
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additional information
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laminaribiose and laminaritriose are no substrates, laminaritetraose is very inefficiently cleaved
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additional information
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plant endo-1,3-beta-glucanases hydrolyze (1,3)-beta-glucans, with very limited activity towards mixed (1,3,1,4)-beta-glucans and branched (1,3,1,6)-beta-glucans
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additional information
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plant endo-1,3-beta-glucanases hydrolyze (1,3)-beta-glucans, with very limited activity towards mixed (1,3,1,4)-beta-glucans and branched (1,3,1,6)-beta-glucans
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additional information
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Enzyme shows low processivity of 0.4. No substrate: yeast beta-1,3-1,6-glucan or other polysaccharides. enzyme is unable to lyse Saccharomyces cerevisiae cells
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additional information
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no substrates : cellulose, xylan, amylose, starch, beta-cyclodextrin
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additional information
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no substrates : cellulose, xylan, amylose, starch, beta-cyclodextrin
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additional information
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BglS27 preferentially catalyzes the hydrolysis of glucans with a beta-1,3-linkage using an endolytic mode of action
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additional information
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no activity with oat spelt xylan and carboxymethyl cellulose
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additional information
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Eisenia bicyclis laminarin, with a higher amount of beta-1,6-linkages, is no substrate for the enzyme. Trisaccharide is inevitably released from the hydrolysis of laminarioligosaccharides with 5 to 7 degrees of polymerization. Although the enzyme cleaves off disaccharide from tetrasaccharide, the reaction rate is lower than those of laminaripentaose to laminariheptaose. The results indicate that the active site of Mo endo-beta-1,3-glucanase can efficiently recognize glucosyl residue chain of greater than laminaripentaose and hydrolyzes the beta-1,3 linkage between the 3rd and 4th glucosyl residue
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additional information
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Eisenia bicyclis laminarin, with a higher amount of beta-1,6-linkages, is no substrate for the enzyme. Trisaccharide is inevitably released from the hydrolysis of laminarioligosaccharides with 5 to 7 degrees of polymerization. Although the enzyme cleaves off disaccharide from tetrasaccharide, the reaction rate is lower than those of laminaripentaose to laminariheptaose. The results indicate that the active site of Mo endo-beta-1,3-glucanase can efficiently recognize glucosyl residue chain of greater than laminaripentaose and hydrolyzes the beta-1,3 linkage between the 3rd and 4th glucosyl residue
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additional information
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the enzyme is an endoglucanase that hydrolyzes beta-1,3-glucans as laminarin and yeast beta-1,3-1,6-glucan, but is inactive toward other polysaccharides, e.g. unbranched beta-1,3-glucans or mixed beta-1,3-1,4-glucan from cereals, or disaccharides
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additional information
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the enzyme is an endoglucanase that hydrolyzes beta-1,3-glucans as laminarin and yeast beta-1,3-1,6-glucan, but is inactive toward other polysaccharides, e.g. unbranched beta-1,3-glucans or mixed beta-1,3-1,4-glucan from cereals, or disaccharides
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additional information
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substrate specificities of wild-type and mutant enzymes, overview
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additional information
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substrate specificities of wild-type and mutant enzymes, overview
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additional information
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specific cleavage of internal beta-1,3-bonds. No substrate: avicel, carboxymethyl cellulose and cellopentaose, xylan, arabinan and manan containing polysaccharides
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additional information
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specific cleavage of internal beta-1,3-bonds. No substrate: avicel, carboxymethyl cellulose and cellopentaose, xylan, arabinan and manan containing polysaccharides
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additional information
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specific cleavage of internal beta-1,3-bonds. No substrate: avicel, carboxymethyl cellulose and cellopentaose, xylan, arabinan and manan containing polysaccharides
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additional information
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specifically cleaves beta-1,3-linkages in polysaccharides
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additional information
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specifically cleaves beta-1,3-linkages in polysaccharides
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additional information
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YlCrh2Sp does not hydrolyze carboxymethyl-cellulose, pustulan, and lichenan
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additional information
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the enzyme specifically cleaves beta-1,4-linkages next to beta-1,3-linkages and is active on linear 1,3-beta-D-glucans with 3-6 monomers and on a glucan tetrasaccharide containing two beta-1,4-linkages separated by one beta-1,3-linkage. The activity towards beta-1,4-linkages is much lower than towards beta-1,3-linkages. Enzyme-substrate complex structure analysis using wild-type and mutant enzymes with glucan oligomers, binding structure and substrate recognition, overview
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additional information
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the enzyme specifically cleaves beta-1,4-linkages next to beta-1,3-linkages and is active on linear 1,3-beta-D-glucans with 3-6 monomers and on a glucan tetrasaccharide containing two beta-1,4-linkages separated by one beta-1,3-linkage. The activity towards beta-1,4-linkages is much lower than towards beta-1,3-linkages. Enzyme-substrate complex structure analysis using wild-type and mutant enzymes with glucan oligomers, binding structure and substrate recognition, overview
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additional information
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the enzyme specifically cleaves beta-1,4-linkages next to beta-1,3-linkages and is active on linear 1,3-beta-D-glucans with 3-6 monomers and on a glucan tetrasaccharide containing two beta-1,4-linkages separated by one beta-1,3-linkage. The activity towards beta-1,4-linkages is much lower than towards beta-1,3-linkages. Enzyme-substrate complex structure analysis using wild-type and mutant enzymes with glucan oligomers, binding structure and substrate recognition, overview
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