3.2.1.6: endo-1,3(4)-beta-glucanase
This is an abbreviated version!
For detailed information about endo-1,3(4)-beta-glucanase, go to the full flat file.
Word Map on EC 3.2.1.6
-
3.2.1.6
-
cellulase
-
xylanase
-
cellulolytic
-
carboxymethyl
-
straw
-
trichoderma
-
carboxymethylcellulase
-
beta-glucosidase
-
fpase
-
beta-glucans
-
thermocellum
-
lignocellulosic
-
xylan
-
saccharification
-
avicel
-
lichenan
-
reesei
-
hemicellulose
-
avicelase
-
endoglucanases
-
bagasse
-
cellulosic
-
bran
-
cellobiohydrolase
-
cellulose-binding
-
cellulomonas
-
cellulose-degrading
-
exoglucanase
-
fibrobacter
-
lignocellulolytic
-
cellobiase
-
cellulosome
-
succinogenes
-
cellooligosaccharides
-
cellotriose
-
mixed-linkage
-
xylanolytic
-
microcrystalline
-
cellotetraose
-
agriculture
-
fibrolytic
-
acid-swollen
-
cellopentaose
-
synthesis
-
food industry
-
drug development
-
degradation
-
nutrition
-
analysis
-
lignocellulose-degrading
-
macerans
-
laminaribiose
-
neocallimastix
-
dockerin
-
biotechnology
-
sawdust
-
endo-1,4-beta-xylanase
-
endo-1,4-beta-d-glucanase
- 3.2.1.6
- cellulase
- xylanase
-
cellulolytic
-
carboxymethyl
- straw
- trichoderma
- carboxymethylcellulase
- beta-glucosidase
-
fpase
- beta-glucans
- thermocellum
-
lignocellulosic
- xylan
-
saccharification
- avicel
- lichenan
- reesei
- hemicellulose
- avicelase
- endoglucanases
- bagasse
-
cellulosic
- bran
- cellobiohydrolase
-
cellulose-binding
- cellulomonas
-
cellulose-degrading
- exoglucanase
- fibrobacter
-
lignocellulolytic
- cellobiase
- cellulosome
- succinogenes
- cellooligosaccharides
- cellotriose
-
mixed-linkage
-
xylanolytic
-
microcrystalline
- cellotetraose
- agriculture
-
fibrolytic
-
acid-swollen
- cellopentaose
- synthesis
- food industry
- drug development
- degradation
- nutrition
- analysis
-
lignocellulose-degrading
- macerans
- laminaribiose
- neocallimastix
-
dockerin
- biotechnology
- sawdust
- endo-1,4-beta-xylanase
- endo-1,4-beta-d-glucanase
Reaction
Synonyms
1,3-(4)-beta-glucanase (endoglucanase), 1,3-1,4-beta-glucanase EII (barley), 1,3-beta-D-glucanase, AFUA_1G05290, AFUA_2G14360, AFUA_4G13360, AFUA_5G02280, Agl9A, AkLam36, barley-beta-D-glucanase, beta-1,3-1,4 glucanase, beta-1,3-1,4-glucanase, beta-1,3-glucanase, beta-1,3:1,4 glucanase, beta-D-(1-3)-glucanase, beta-glucanase, bglBC1, CBM-CD, CC1G_01665, Cel8A, CelL, chitosanase, CMCase, CtLic26A, enda-beta-(1-3),(1-4)-glucanase, endo beta-1,3-glucanase IV, endo-1,3(4)-beta-D-glucanase, endo-1,3(4)-beta-glucanase, endo-1,3-1,4-beta-D-glucanase, endo-1,3-beta-D-glucanase, endo-1,3-beta-glucanase, endo-1,4-beta-glucanase, endo-beta-(1-3)-D-glucanase, endo-beta-1,3(4)-glucanase, endo-beta-1,3-1,4-D-glucanase, endo-beta-1,3-1,4-glucanase, endo-beta-1,3-glucanase, endo-beta-1,4-glucanase, eng1, ENG16A, Eng2, Eng3, Eng4, Eng5, Engl1, Fsbeta-glucanase, GluA, H(A16-M), HdLam33, LAM, Lam16A, LamA, lamarinase, laminaranase, laminarinase, laminarinase 16A, laminarinase II, laminarinase Lam16A, LamR, LIC 1, Lic16A, Lic8H, Lichenase, More, nonlytic endo-beta-1,3-glucanase I, SsGlc, TcGlu2, TeEgl5A, Xyn10B
ECTree
3.2.1.6 endo-1,3(4)-beta-glucanaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.2.1.6 - endo-1,3(4)-beta-glucanase
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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
1,3-1,4-beta-D-glucan + H2O
?
-
LamR cleaves the 1,4-beta-linkages of 3-O-substituted beta-glucose in beta-glucans such as lichenin and 1,3-1,4-beta-glucan from the cell walls of barley endosperm, analysis of reaction products
-
-
?
alpha-laminariheptaosyl fluoride
?
-
substrate can make a nucleophilic attack upon itself, the major product being a cyclic beta-1,3-heptaglucan. NMR confirms uniquely beta-1,3-linkages and no reducing end. The cyclic laminariheptaose molecule is not completely planar and torsion angles at the glycosidic linkages fluctuate between two energy minima
-
?
beta-1,3-1,4-D-glucotriose + H2O
D-glucose + cellobiose
-
-
-
?
beta-Glc-(1->3)-beta-Glc-(1->4)-beta-Glc-(1->3)-beta-Glc-(1->4)-Glc + H2O
beta-Glc-(1->3)-beta-Glc-(1->4)-beta-Glc + ?
-
-
main product, plus some tetrasaccharide. The enzyme acts on both beta-1,4-linkages of substrate
-
?
carboxymethyl-cellulose + H2O
?
15% of the activity with beta-D-glucan
-
-
?
cellodextrin + H2O
cellobiose + cellotriose + higher oligosaccharides
-
-
-
?
curdlan + H2O
laminaribiose + laminaritriose + ?
-
main products
-
?
Glc-beta(1,4)-Glc-beta(1,3)-Glc-methylumbelliferyl + H2O
methylumbelliferone + Glc-beta(1,4)-Glc-beta(1,3)-Glc
-
-
-
-
?
konjac glucomannan + H2O
?
40% of the activity with barley beta-1,3-1,4-D-glucan
-
-
?
laminarihexaose + H2O
D-glucose + laminaribiose + laminaritriose
-
-
-
?
laminarin + H2O
6-O-glucosyl-laminaritriose + ?
6-O-glucosyl-laminaritriose is produced as one of the major products
-
-
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
laminarin + H2O
D-glucose + laminaripentaose
-
from Laminaria digitata, best substrate for LIC 1, cleaves internal bonds, LIC 1 may have five subsites for glucose at the aglycone site and at least one subsite in the glucone site, LIC 1 should move along the substrate 1 or 5 glucosyl residues after each hydrolytic step, after the hydrolytic step LIC 1 dissociates from or moves along the substrate molecule to the next beta-1,3-linkage distant one or preferentially 4-6 glucosyl residues in the non-reducing end direction
LIC 1 forms almost only glucose and laminaripentaose as soluble products, laminaripentaose is the main product, glucose is 20% from total products and 25% from soluble products
-
?
laminarin + H2O
laminaritriose
from Laminaria digitata
-
-
?
laminaripentaose + H2O
D-glucose + laminaribiose + laminaritriose
-
-
-
?
lichenan + H2O
4-O-glucosyl-laminaribiose + ?
4-O-glucosyl-laminaribiose is produced as one of the major products
-
-
?
lichenan + H2O
beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-4)-D-glucopyranose + ?
-
-
-
-
?
lichenan + H2O
beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->3)-beta-D-glucopyranose + ?
-
from Cetraria islandica. HdLam33 produces no cellotriose, cellobiose, and glucose from lichenan, but produced the trisaccharide cellobiosyl-beta-1,3-glucose
-
-
?
lichenin + H2O
?
-
LamR cleaves the 1,4-beta-linkages of 3-O-substituted beta-glucose in beta-glucans such as lichenin, analysis of reaction products
-
-
?
lichenin + H2O
beta-D-glucopyranosyl-(1->3)-[beta-D-glucopyranosyl-(1->3)-beta-D-glucopyranosyl-(1->4)]-beta-D-glucopyranose + lichenin oligomers
lichenin + H2O
cellotetraose + cellopentaose + glucose
-
from Cetraria islandica, cleaves internal bonds, LIC 1 has high affinity for sequences of cellotetraose linked by beta-1,3-links releasing cellotetraose from lichenin, after the hydrolytic step LIC 1 dissociates from or moves along the substrate molecule to the next beta-1,3-linkage distant one or preferentially 4-6 glucosyl residues in the non-reducing end direction
main products are cellotetraose and cellopentaose, glucose is only 1% of soluble products, LIC 1 produces an additional saccharide as product possibly containing beta-1,3- and beta-1,4-linkages
-
?
oxidized laminarin
laminaritetraose + laminaritriose + laminaribiose + D-glucose
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
-
slight activity
-
?
polysaccharides + H2O
oligosaccharides
-
role in maintenance of channels for communication and translocation through cell walls
-
?
1,3-1,4-beta-D-glucan + H2O
cellooligosaccharide
-
soluble, from barley, endo-acting enzyme, preference for mixed-link 1,3-1,4-beta-D-glucan substrates, highest catalytic efficiency with barley 1,3-1,4-beta-D-glucan
spectrum of oligosaccharide products by EG VI and EG VII including linear beta-1,4-gluco and mixed-link oligosaccharides, relative distribution of the cellooligosaccharides DP 1-5 after 24 h incubation
-
?
1,3-1,4-beta-D-glucan + H2O
cellooligosaccharide
-
soluble, from barley, endo-acting enzyme, preference for mixed-link 1,3-1,4-beta-D-glucan substrates, highest catalytic efficiency with barley 1,3-1,4-beta-D-glucan
spectrum of oligosaccharide products by EG VI and EG VII including linear beta-1,4-gluco and mixed-link oligosaccharides, relative distribution of the cellooligosaccharides DP 1-5 after 24 h incubation
-
?
beta-1,3-1,4-glucan + H2O
?
from Hordeum vulgare, preferred substrate
-
-
?
beta-1,3-1,4-glucan + H2O
?
from Hordeum vulgare, preferred substrate
-
-
?
beta-1,3-1,4-glucan + H2O
?
-
-
high viscosity glucan, 41% of the activity with laminarin, medium and low viscosity, 9% of the activity with laminarin, respectively
-
?
beta-D-glucans + H2O
?
-
role in budding process and cell wall growth
-
-
?
beta-D-glucans + H2O
?
-
in vivo probably facilitation of solubilisation of cell wall glucan
-
-
?
beta-glucan + H2O
?
the enzyme hydrolyses the beta-1,4-glycosidic linkage of barley beta-glucan through an inverting mechanism
-
-
?
beta-glucan + H2O
?
-
degree of hydrolysis reaches 10%, products are oligosaccharides with degree of polymerization 2-10
-
-
?
beta-glucan + H2O
laminaridextrins
-
yeast cell-wall 1,3-beta-glucan
-
-
?
beta-glucan + H2O
laminaridextrins
-
beta-(1-3)-beta-(1-4)mixed-linked, from barley
-
?
beta-glucan + H2O
laminaridextrins
-
beta-(1-3)-beta-(1-4)mixed-linked, from barley
-
?
beta-glucan + H2O
laminaridextrins
-
beta-(1-3)-beta-(1-4)mixed-linked, from barley
-
?
carboxymethyl cellulose + H2O
?
-
49.6% of the activity with laminarin
-
-
?
carboxymethylcellulose + H2O
?
45% of the activity with barley beta-1,3-1,4-D-glucan
-
-
?
carboxymethylcellulose + H2O
?
45% of the activity with barley beta-1,3-1,4-D-glucan
-
-
?
carboxymethylcellulose + H2O
cellobiose + cellotriose + glucose
-
soluble, 1,4-beta-D-glucan, endo-acting enzyme
EG VI releases mainly cellobiose and almost equimolar amounts of cellotriose and glucose, EG VII yields mainly cellobiose and glucose as final reaction products
-
?
carboxymethylcellulose + H2O
cellobiose + cellotriose + glucose
-
soluble, 1,4-beta-D-glucan, endo-acting enzyme
EG VI releases mainly cellobiose and almost equimolar amounts of cellotriose and glucose, EG VII yields mainly cellobiose and glucose as final reaction products
-
?
carboxymethylpachyman + H2O
D-glucose + carboxymethyl-(1-3,1-4)-beta-D-glucan
-
-
-
?
carboxymethylpachyman + H2O
D-glucose + carboxymethyl-(1-3,1-4)-beta-D-glucan
-
-
-
?
carboxymethylpachyman + H2O
D-glucose + carboxymethyl-(1-3,1-4)-beta-D-glucan
-
-
-
?
cellopentaose + H2O
cellobiose + cellotriose
-
-
-
?
curdlan + H2O
?
-
from Alcaligenes faecalis, LamR cleaves the 1,3-beta-linkages of 3-O-substituted glucose units in 1,3-beta-glucans such as laminarin and curdlan
-
-
?
laminaran + H2O
?
-
from Laminaria digitata, 1,3-beta-glucan
-
-
?
laminaribiose + H2O
D-glucose
-
0.03% of the rate of laminarin
-
?
laminarin + H2O
?
-
AkLam36 exhibits exolytic beta-1,3-hydrolytic activity releasing D-glucose preferring beta-1,3-glucans with a few beta-1,6-linked glucose branches such as Laminaria digitata laminarin
-
-
?
laminarin + H2O
?
-
AkLam36 exhibits exolytic beta-1,3-hydrolytic activity with released D-glucose, preferring beta-1,3-glucans with a few beta-1,6-linked glucose branches such as Laminaria digitata laminarin, best substrate is barley beta-D-glucan
-
-
?
laminarin + H2O
?
48% of the activity with curdlan
-
-
?
laminarin + H2O
?
-
from Laminaria digitata, LamR cleaves the 1,3-beta-linkages of 3-O-substituted glucose units in 1,3-beta-glucans such as laminarin and curdlan, analysis of reaction products
-
-
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
-
-
reducing sugars
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
-
-
-
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
-
-
70-90% D-glucose, small amounts of laminaribiose and D-glucose oligomers of 3-4 D-glucose units
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
-
-
laminaridextrins + D-glucose
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
Flavobacterium dormitator
-
-
main product laminaripentaose
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
Flavobacterium dormitator
-
-
D-glucose + laminaribiose, laminaritriose + D-glucose
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
-
-
-
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
-
-
laminaridextrins + D-glucose
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
-
-
reducing sugars
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
-
-
-
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
-
-
laminaridextrins + D-glucose
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
-
-
laminaridextrins + D-glucose
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
-
-
D-glucose + laminaribiose
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
-
-
laminaridextrins + D-glucose
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
-
-
-
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
-
-
reducing sugars
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
-
-
laminaritriose
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
-
-
laminaridextrins + D-glucose
?
laminaritetraose + 2 H2O
laminaribiose + 2 D-glucose
-
from Laminaria digitata. HdLam33 performs a transglycosylation reaction transferring the laminaribiose unit in the non-reducing terminus of laminaritriose , as donor substrate, to a free laminaribiose, as acceptor substrate, giving laminaritetraose and glucose. The resulting laminaritetraose is subsequently hydrolyzed by HdLam33 into 2 mol of glucose and 1 mol of laminaribiose
-
-
?
laminaritetraose + H2O
D-glucose + laminaribiose + laminaritriose
-
-
-
?
laminaritetraose + H2O
D-glucose + laminaribiose + laminaritriose
-
-
-
?
laminaritriose + H2O
D-glucose + laminaribiose
-
-
-
?
lichenan + H2O
?
48% of the activity with barley beta-1,3-1,4-D-glucan
-
-
?
lichenan + H2O
?
48% of the activity with barley beta-1,3-1,4-D-glucan
-
-
?
lichenan + H2O
cellooligosaccharide
-
from Cetraria islandica, endo-acting enzyme, preference for mixed-link 1,3-1,4-beta-D-glucan substrates, rapid hydrolysis
spectrum of oligosaccharide products by EG VI and EG VII
-
?
lichenan + H2O
cellooligosaccharide
-
from Cetraria islandica, endo-acting enzyme, preference for mixed-link 1,3-1,4-beta-D-glucan substrates, rapid hydrolysis
spectrum of oligosaccharide products by EG VI and EG VII
-
?
lichenin + H2O
beta-D-glucopyranosyl-(1->3)-[beta-D-glucopyranosyl-(1->3)-beta-D-glucopyranosyl-(1->4)]-beta-D-glucopyranose + lichenin oligomers
-
-
laminaripentaose + D-glucose
?
lichenin + H2O
beta-D-glucopyranosyl-(1->3)-[beta-D-glucopyranosyl-(1->3)-beta-D-glucopyranosyl-(1->4)]-beta-D-glucopyranose + lichenin oligomers
-
-
laminaripentaose + D-glucose
?
lichenin + H2O
beta-D-glucopyranosyl-(1->3)-[beta-D-glucopyranosyl-(1->3)-beta-D-glucopyranosyl-(1->4)]-beta-D-glucopyranose + lichenin oligomers
Flavobacterium dormitator
-
-
laminaripentaose main product
?
lichenin + H2O
beta-D-glucopyranosyl-(1->3)-[beta-D-glucopyranosyl-(1->3)-beta-D-glucopyranosyl-(1->4)]-beta-D-glucopyranose + lichenin oligomers
Flavobacterium dormitator
-
weak activity of enzyme I
-
?
lichenin + H2O
beta-D-glucopyranosyl-(1->3)-[beta-D-glucopyranosyl-(1->3)-beta-D-glucopyranosyl-(1->4)]-beta-D-glucopyranose + lichenin oligomers
-
-
-
?
lichenin + H2O
beta-D-glucopyranosyl-(1->3)-[beta-D-glucopyranosyl-(1->3)-beta-D-glucopyranosyl-(1->4)]-beta-D-glucopyranose + lichenin oligomers
-
-
-
?
lichenin + H2O
beta-D-glucopyranosyl-(1->3)-[beta-D-glucopyranosyl-(1->3)-beta-D-glucopyranosyl-(1->4)]-beta-D-glucopyranose + lichenin oligomers
-
-
-
?
pachyman + H2O
?
223% of the activity with curdlan
-
-
?
pachyman + H2O
laminarisaccharides
Flavobacterium dormitator
-
weak activity of enzyme I
-
-
?
pachyman + H2O
laminarisaccharides
-
more active on short-chain pachyman
-
?
additional information
?
-
determination of binding constants and binding capacity for substrates tested, in presence and absence of Ca2+
-
-
?
additional information
?
-
-
no direct degradation activity with laminaribiose as a sole substrate, but the enzyme is capable of degrading it via transglycosylation reaction with laminaritriose
-
-
?
additional information
?
-
-
sAkLam36 substrate specificity amd mode of action, overview. The enzyme is inactive toward laminaribiose, starch, carboxymethylcellulose, agar, beta-1,4-mannan, beta-1,4-xylan, and alginic acid, and it is specific to beta-1,3-glucosyl linkages
-
-
?
additional information
?
-
the enzyme acts as a bi-functional enzyme with single catalytic domain
-
-
?
additional information
?
-
enzyme hydrolyzes both beta-1,3-glucan (laminarin) and beta-1,3-1,4-glucan linkages, catalyzes endo-hydrolysis of the beta-1,4 glycosidic linkage adjacent to a 3-O-substituted glucosyl residues in the mixed linked beta-glucans, as well as the beta-1,3 linkage. No substrates: carboxymethylcellulose, avicel
-
-
?
additional information
?
-
activity in decreasing order is barley beta-1,3-1,4-D-glucan, carboxymethylcellulose, lichenan, avicel, konjac glucomannan. No substrates: cellobiose, cellotriose, p-nitrophenyl derivatives of mono- and disaccharides, or beta-1,3-D-glucan, beta-1,4-D-galactomannan, and beta-1,4-D-xylan
-
-
?
additional information
?
-
activity in decreasing order is barley beta-1,3-1,4-D-glucan, carboxymethylcellulose, lichenan, avicel, konjac glucomannan. No substrates: cellobiose, cellotriose, p-nitrophenyl derivatives of mono- and disaccharides, or beta-1,3-D-glucan, beta-1,4-D-galactomannan, and beta-1,4-D-xylan
-
-
?
additional information
?
-
-
laminarinase hydrolyses both beta-1,3-glycosidic bonds and beta-1,4-glycosidic bonds
-
-
?
additional information
?
-
-
laminarinase hydrolyses both beta-1,3-glycosidic bonds and beta-1,4-glycosidic bonds
-
-
?
additional information
?
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enzyme only acts on substrates containing beta-1,3 glycosidic bonds but not on substrates containing only beta-1,4- or beta-1,6-glycosidic bonds
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HdLam33 degrades laminarin and laminarioligosaccharides to laminaribiose and glucose
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no substrates: carboxymethylcellulose, birchwood xylan, avicel and filter paper
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no substrates: carboxymethylcellulose, birchwood xylan, avicel and filter paper
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no substrates: xylan, colloidal chitin, carboxymethyl cellulose, polygalacturonic acid, pectin and laminaribiose
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no substrates: xylan, colloidal chitin, carboxymethyl cellulose, polygalacturonic acid, pectin and laminaribiose
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the ten active-site residues ASn26,Glu63, Arg65, Phe92, Tyr94, Glu105, Asp107, Glu109, Asn182 and Trp184 form a network of hydrogen bonds and hydrophobic stacking interactions with the substrate
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the enzyme has a broad substrate specificity and hydrolyzes barley-beta-D-glucan before chitosan, carboxymethyl-cellulose, and lichenan
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the enzyme hydrolyzes cello-oligosaccharides (G3-G6) to cellotriose and cellobiose but not to D-glucose. Barley beta-glucan and lichenan are hydrolyzed by the enzyme to cellotetraose as the major product
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no activity with carboxymethylcellulose and xylan of all truncated proteins of LamA
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LIC 1 lyses plant and fungal cell walls, making available their contents, LIC 1 may help the cellulases CEL 1 and CEL 2 by hydrolyzing beta-1,3-1,4-glucans, important chiefly in cereal walls
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a group in LIC 1 with pK of 4.9 is necessary for substrate binding
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the enzyme strictly recognizes beta-D-Glcp-(1,3)-D-Glcp at subsites -2 and -1. It permits 6-O-glucosyl substitution at subsite +1 and a beta-1,4-glucosidic linkage at the catalytic site
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the enzyme strictly recognizes beta-D-Glcp-(1,3)-D-Glcp at subsites -2 and -1. It permits 6-O-glucosyl substitution at subsite +1 and a beta-1,4-glucosidic linkage at the catalytic site
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the enzyme shows broad substrate specificity and exhibits high activity on substrates containing beta-1,4-glycosidic bonds and beta-1,3-glycosidic bonds. Although TeEgl5A belongs to endo-1,4-glucanase, it also acts on the 1,3-beta-linkage or mixed-linkage-beta-glucan. The enzyme has a higher specific activity on soluble 1,3-1,4-beta-glucans and 1,4-beta-glucans, such as beta-glucan (100%), laminarin (95%), and lichenin (80%), than on less soluble polysaccharides like carboxymethyl cellulose (15%). No activity on Avicel, cellobiose, and cellotriose. The broader substrate specificity suggests that TeEgl5A belongs to the group of nonspecific endoglucanases
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additional information
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the enzyme shows broad substrate specificity and exhibits high activity on substrates containing beta-1,4-glycosidic bonds and beta-1,3-glycosidic bonds. Although TeEgl5A belongs to endo-1,4-glucanase, it also acts on the 1,3-beta-linkage or mixed-linkage-beta-glucan. The enzyme has a higher specific activity on soluble 1,3-1,4-beta-glucans and 1,4-beta-glucans, such as beta-glucan (100%), laminarin (95%), and lichenin (80%), than on less soluble polysaccharides like carboxymethyl cellulose (15%). No activity on Avicel, cellobiose, and cellotriose. The broader substrate specificity suggests that TeEgl5A belongs to the group of nonspecific endoglucanases
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additional information
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enzyme is active on 1,3-1,4-beta-D-glucans, with no activity against a range of aryl and methylumbelliferyl-beta-glycosides, alpha- and beta-linked polysaccharides, including oat spelts xylan, rhodymenan, and polygalacturonic acid, avicel, laminarin or pachyman
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additional information
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enzyme is active on 1,3-1,4-beta-D-glucans, with no activity against a range of aryl and methylumbelliferyl-beta-glycosides, alpha- and beta-linked polysaccharides, including oat spelts xylan, rhodymenan, and polygalacturonic acid, avicel, laminarin or pachyman
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one active site per enzyme molecule
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additional information
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the enzyme shows broad substrate specificity and exhibits high activity on substrates containing beta-1,4-glycosidic bonds and beta-1,3-glycosidic bonds. Although TeEgl5A belongs to endo-1,4-glucanase, it also acts on the 1,3-beta-linkage or mixed-linkage-beta-glucan. The enzyme has a higher specific activity on soluble 1,3-1,4-beta-glucans and 1,4-beta-glucans, such as beta-glucan (100%), laminarin (95%), and lichenin (80%), than on less soluble polysaccharides like carboxymethyl cellulose (15%). No activity on Avicel, cellobiose, and cellotriose. The broader substrate specificity suggests that TeEgl5A belongs to the group of nonspecific endoglucanases
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additional information
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hydrolysis occurs with retention of the beta-configuration at the anomeric carbon, LamR performs transglycosylation to generate both 1,3-beta-glycosidic and 1,4-beta-glycosidic linkages, a laminaribiosyl unit is the minimum requirement for formation of an enzyme-substrate complex and subsequent hydrolysis/transglycosylation, no substrate: laminaribiose
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the C-terminal region of isoform Eng1 acts as carbohydrate-binding module. In vitro, the purified module has affinity for beta-(1-3)-glucan chains with a minimum degree of polymerization of 30 glucose units
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SsGlc functions in salt stress tolerance in Synechocystis PCC6803
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SsGlc functions in salt stress tolerance in Synechocystis PCC6803
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no activity towards cellulose, curdlan or laminarin
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no activity towards cellulose, curdlan or laminarin
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no substrates: xylan, microcrystalline cellulose, and 4-nitrophenylbeta-D-glucopyranoside
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