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Information on EC 3.2.1.6 - endo-1,3(4)-beta-glucanase
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EC Tree
3.2.1.6 endo-1,3(4)-beta-glucanaseIUBMB Comments
Substrates include laminarin, lichenin and cereal D-glucans; different from EC 3.2.1.52 beta-N-acetylhexosaminidase.
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Word Map
- 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
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
cmcase, lichenase, endo-beta-1,4-glucanase, endo-1,4-beta-glucanase, beta-1,3-1,4-glucanase, cel8a, h(a16-m), lam16a, fsbeta-glucanase, endo-beta-1,3-1,4-glucanase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AFUA_1G05290
AFUA_2G14360
AFUA_4G13360
AFUA_5G02280
beta-1,3-1,4-glucanase
beta-1,3-glucanase
beta-D-(1-3)-glucanase
beta-glucanase
bglBC1
CC1G_01665
Cel8A
CelL
enda-beta-(1-3),(1-4)-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-glucanase
endo-beta-1,3-glucanase
endo-beta-1,4-glucanase
ENG16A
Eng2
Eng3
Eng4
Eng5
GluA
H(A16-M)
-
1,3-1,4-beta-glucanase from Bacillus macerans in which the 16 N-terminal residues have been replaced by the respective residues of the enzyme from Bacillus amyloliquefaciens
Lam16A
lamarinase
laminaranase
laminarinase
LamR
TeEgl5A
Xyn10B
additional information
Xyn10B
-
modular enzyme composed of two family-22 carbohydrate-binding modules, a family-9 carbohydrate-binding module, and two S-layer homologous modules
Xyn10B
-
modular enzyme comprising two family-22 carbohydrate-binding modules (CBMs), a family-10 catalytic module of glycoside hydrolases, a family-9 carbohydrate-binding module, and two S-layer homologous modules consecutively from the N-terminus
additional information
the bacterial beta-1,3-1,4-glucanase belongs to the glycosyl hydrolase family 16, GH16, possessing the conserved EIDIEF motif
additional information
the bacterial beta-1,3-1,4-glucanase belongs to the glycosyl hydrolase family 16, GH16, possessing the conserved EIDIEF motif
-
additional information
-
HdLam33 belongs to the glycoside hydrolase family 16, GH16
additional information
-
the enzyme belongs to the glycosyl hydrolase family 81, GH81
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(Glcbeta(1-3))n + H2O = laminaripentaose + (Glcbeta(1-3))n-5
-
-
-
-
(Glcbeta(1-3))n + H2O = laminaripentaose + (Glcbeta(1-3))n-5
reaction is not in rapid equilibrium
-
(Glcbeta(1-3))n + H2O = laminaripentaose + (Glcbeta(1-3))n-5
substrates include laminarin, lichenin, and cereal D-glucans, different from EC 3.2.1.52 beta-L-N-acetylhexosaminidase
-
(Glcbeta(1-3))n + H2O = laminaripentaose + (Glcbeta(1-3))n-5
substrates include laminarin, lichenin, and cereal D-glucans, different from EC 3.2.1.52 beta-L-N-acetylhexosaminidase
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
3(or 4)-beta-D-glucan 3(4)-glucanohydrolase
Substrates include laminarin, lichenin and cereal D-glucans; different from EC 3.2.1.52 beta-N-acetylhexosaminidase.
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CAS REGISTRY NUMBER
COMMENTARY
62213-14-3
-
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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
?
-
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
-
-
?
additional information
?
-
-
HdLam33 degrades laminarin and laminarioligosaccharides to laminaribiose and glucose
-
-
?
additional information
?
-
no substrates: carboxymethylcellulose, birchwood xylan, avicel and filter paper
-
-
?
additional information
?
-
no substrates: carboxymethylcellulose, birchwood xylan, avicel and filter paper
-
-
?
additional information
?
-
no substrates: xylan, colloidal chitin, carboxymethyl cellulose, polygalacturonic acid, pectin and laminaribiose
-
-
?
additional information
?
-
no substrates: xylan, colloidal chitin, carboxymethyl cellulose, polygalacturonic acid, pectin and laminaribiose
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
the enzyme has a broad substrate specificity and hydrolyzes barley-beta-D-glucan before chitosan, carboxymethyl-cellulose, and lichenan
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
no activity with carboxymethylcellulose and xylan of all truncated proteins of LamA
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
a group in LIC 1 with pK of 4.9 is necessary for substrate binding
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
one active site per enzyme molecule
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
SsGlc functions in salt stress tolerance in Synechocystis PCC6803
-
-
?
additional information
?
-
-
SsGlc functions in salt stress tolerance in Synechocystis PCC6803
-
-
?
additional information
?
-
no activity towards cellulose, curdlan or laminarin
-
-
?
additional information
?
-
-
no activity towards cellulose, curdlan or laminarin
-
-
?
additional information
?
-
-
no substrates: xylan, microcrystalline cellulose, and 4-nitrophenylbeta-D-glucopyranoside
-
-
?
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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
polysaccharides + H2O
oligosaccharides
-
role in maintenance of channels for communication and translocation through cell walls
-
?
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
-
-
?
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
-
-
?
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
?
-
-
HdLam33 degrades laminarin and laminarioligosaccharides to laminaribiose and glucose
-
-
?
additional information
?
-
the enzyme has a broad substrate specificity and hydrolyzes barley-beta-D-glucan before chitosan, carboxymethyl-cellulose, and lichenan
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
SsGlc functions in salt stress tolerance in Synechocystis PCC6803
-
-
?
additional information
?
-
-
SsGlc functions in salt stress tolerance in Synechocystis PCC6803
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Fe2+
Mn2+
additional information
Ca2+
enzyme N-terminal module CBM54 substrate binding promiscuity suggests multiple binding sites, some of them being Ca2+-dependent. The Ca2+-independent sites for avicel, pustulan and chitosan are localized to the spontaneously split-off N-terminal part of 8 kDa of CBM54. Determination of binding constants and binding capacity for substrates tested, in presence and absence of Ca2+
Ca2+
slightly activating, 142% activity at 15 mM, slightly inhibitory at 25 mM with 86% of maximal activity. Calcium ion has a general stabilizing effect on Bacillus beta-1,3-1,4 glucanases. Calcium is bound to the backbone carbonyl oxygens of Pro9, Gly45, Asp207 and carboxylate oxygen of Asp207 and two water molecules
Ca2+
activates, 5 mM Ca2+ increases the lichenase activity by 15%. Ca2+ increases the heat stability of the lichenase activity
Ca2+
identification of calcium ions bound to each monomer, in equivalent sites of each polypeptide chain in the asymmetric unit cell, and displaying the same coordination patterns. Coordination of the calcium ion is 6fold, and involves Gly60 of main chain, Asp248, main chain and side chain, Glu18 of main chain, and two water molecules. Crystallization data
additional information
the enzyme activity is not affected by Mg2+, Ca2+, KI, and sucrose at 10 mM
additional information
-
presence of divalent cations, except Pb2+, Hg2+, and Ag+, enhances the activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KMnO4
-
56% loss of activity by 0.5 mM, complete inactivation by 2 mM
Phenylmercuric nitrate
-
loss of 93% of activity after preincubation of enzyme for with 5 mg/ml for 30 min
Ag+
Flavobacterium dormitator
-
72% inhibition of beta-1,3-glucanase activity after incubation with 1 mM at 5°C, pH 6.0, for 3 h
Ca2+
slightly activating, 142% activity at 15 mM, slightly inhibitory at 25 mM with 86% of maximal activity
epoxyalkyl-beta-glycosides
-
of D-glucose, cellobiose, cellotriose, laminaribiose, laminaritriose, irreversible inactivation of enzyme
-
Hg2+
Flavobacterium dormitator
-
96% inhibition of beta-1,3-glucanase IV activity after incubation with 1 mM at 5°C, pH 6.0, for 3 h, no inhibition in presence of beta-mercaptoethanol
N-bromosuccinimide
-
81% loss of activity by 0.5 mM, complete inactivation by 2 mM
additional information
the enzyme is strongly resistant to pepsin and trypsin. When the enzyme is treated with pepsin and trypsin at 37°C for 1 h, 91.5% and 72.3% of enzyme activity is retained, respectively
-
additional information
-
the enzyme is strongly resistant to pepsin and trypsin. When the enzyme is treated with pepsin and trypsin at 37°C for 1 h, 91.5% and 72.3% of enzyme activity is retained, respectively
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Cysts
The promoter of the Arabidopsis thaliana Cel1 endo-1,4-beta glucanase gene is differentially expressed in plant feeding cells induced by root-knot and cyst nematodes.
Cysts
The tobacco Cel7 gene promoter is auxin-responsive and locally induced in nematode feeding sites of heterologous plants.
Mycoses
Characterization of tomato endo-beta-1,4-glucanase Cel1 protein in fruit during ripening and after fungal infection.
Phytoplasma Disease
Recombinant ?-1,3-1,4-glucanase from Theobroma cacao impairs Moniliophthora perniciosa mycelial growth.
Plague
A single component two-valent LcrV-F1 vaccine protects non-human primates against pneumonic plague.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.011
Glc-beta(1,4)-Glc-beta(1,3)-Glc-methylumbelliferyl
-
mutant enzyme N157A
0.11
Glc-beta(1,4)-Glc-beta(1,3)-Glc-methylumbelliferyl
-
wild-type enzyme
0.139
Glc-beta(1,4)-Glc-beta(1,3)-Glc-methylumbelliferyl
-
mutant enzyme F41A
0.155
Glc-beta(1,4)-Glc-beta(1,3)-Glc-methylumbelliferyl
-
mutant enzyme E70A
0.188
Glc-beta(1,4)-Glc-beta(1,3)-Glc-methylumbelliferyl
-
mutant enzyme E258A
0.26
Glc-beta(1,4)-Glc-beta(1,3)-Glc-methylumbelliferyl
-
mutant enzyme Y115A
1.162
Glc-beta(1,4)-Glc-beta(1,3)-Glc-methylumbelliferyl
-
mutant enzyme K260A
1.763
Glc-beta(1,4)-Glc-beta(1,3)-Glc-methylumbelliferyl
-
mutant enzyme Q18A
additional information
Barley beta-glucan
-
Km value 13.38 mg/ml, pH 5.0, 50°C
additional information
Barley beta-glucan
Km value 0.91 mg/ml, pH 5.5, 55°C
additional information
Barley beta-glucan
Km value 1.38 mg/ml, pH 6.5, 75°C
additional information
Barley beta-glucan
Km value 20.8 mg/ml, pH 6.0, 50°C
additional information
beta-Glucan
-
Km value 2.5 mg/ml, pH 5.0, 50°C
additional information
Laminarin
1.1 mg/ml, truncated protein C of LamA
additional information
Laminarin
1.8 mg/ml, truncated protein CF of LamA
additional information
Laminarin
2.4 mg/ml, truncated protein CB3 of LamA
additional information
Laminarin
2.4 mg/ml, truncated protein SC of LamA
additional information
Laminarin
2.9 mg/ml, truncated protein CBF of LamA
additional information
Laminarin
-
Km value 1.1 mg/ml, pH 5.0, 50°C
additional information
Laminarin
Km value 2.63 mg/ml, pH 6.5, 75°C
additional information
additional information
-
pH 5, 50°C, EG VI: Km for barley 1,3-1,4-beta-D-glucan is 28.6 mg/ml, Km for lichenan is 58.8 mg/ml, Km for carboxymethylcellulose is 76.9 mg/ml, EG VII: Km for barley 1,3-1,4-beta-D-glucan is 9.1 mg/ml, Km for carboxymethylcellulose is 62.5 mg/ml
-
additional information
additional information
-
Km-value for beta-glucan is 0.34 mg/ml for wild-type enzyme, 0.67 mg/ml for mutant enzyme Q18A, 1.3 mg/ml for mutant enzymes F41A and E70A, 0.46 mg/ml for mutant enzyme W72A, 1.4 mg/ml for mutant enzyme W114A, 1 mg/ml for mutant enzyme Y115A, 0.49 mg/ml for mutant enzyme N157A, 0.55 mg/ml for mutant enzyme E258A, 0.65 mg/ml for mutant enzyme K260A
-
additional information
additional information
-
Km-value for beta-glucan is 1.87 mg/ml
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7207
beta-1,3-1,4-glucan
pH 6.4, 40°C, purified recombinant His-tagged enzyme, substrate from Hordeum vulgare
114.8
1,3-1,4-beta-D-glucan
-
pH 5, 50°C, soluble, from barley, EG VII
-
0.000017
Glc-beta(1,4)-Glc-beta(1,3)-Glc-methylumbelliferyl
-
mutant enzyme F41A
0.000083
Glc-beta(1,4)-Glc-beta(1,3)-Glc-methylumbelliferyl
-
mutant enzyme E70A
0.00083
Glc-beta(1,4)-Glc-beta(1,3)-Glc-methylumbelliferyl
-
mutant enzyme Y115A
0.012
Glc-beta(1,4)-Glc-beta(1,3)-Glc-methylumbelliferyl
-
mutant enzyme N157A
0.027
Glc-beta(1,4)-Glc-beta(1,3)-Glc-methylumbelliferyl
-
mutant enzyme E258A
0.035
Glc-beta(1,4)-Glc-beta(1,3)-Glc-methylumbelliferyl
-
mutant enzyme Q18A
0.053
Glc-beta(1,4)-Glc-beta(1,3)-Glc-methylumbelliferyl
-
mutant enzyme K260A
0.383
Glc-beta(1,4)-Glc-beta(1,3)-Glc-methylumbelliferyl
-
wi.d-type enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
Barley beta-glucan
-
kcat/Km value 20.1 ml/mg/s, pH 5.0, 50°C
additional information
Barley beta-glucan
kcat/Km value 2116 ml/mg/s, pH 6.5, 75°C
additional information
beta-Glucan
-
kcat/Km value 19.8 ml/s/mg, pH 5.0, 50°C
additional information
Laminarin
-
kcat/Km value 10.6 ml/s/mg, pH 5.0, 50°C
additional information
Laminarin
kcat/Km value 102 ml/mg/s, pH 6.5, 75°C
additional information
lichenan
-
kcat/Km value 36.2 ml/mg/s, pH 5.0, 50°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.4
172
18
Flavobacterium dormitator
-
purified beta-1,3 glucanase II from periplasmic fraction of Escherichia coli clone cells
6.2
substrate barley beta-1,3-1,4-D-glucan, pH 5.0, 50°C
728.8
purified recombinant His-tagged enzyme, substrate beta-glucan from Hordeum vulgare
additional information
additional information
0.3 U/nmol with substrate curdlan, truncated protein C of LamA
additional information
0.3 U/nmol with substrate pachyman, truncated protein C of LamA
additional information
0.4 U/nmol with substrate barley beta-glucan, truncated protein C of LamA
additional information
0.4 U/nmol with substrate lichenan, truncated protein C of LamA
additional information
0.4 U/nmol with substrate lichenan, truncated protein CF of LamA
additional information
0.4 U/nmol with substrate pachyman, truncated protein CF of LamA
additional information
0.4 U/nmol with substrate zymosan A, truncated protein C of LamA
additional information
0.5 U/nmol with substrate barley beta-glucan, truncated protein CF of LamA
additional information
0.5 U/nmol with substrate zymosan A, truncated protein CF of LamA
additional information
0.6 U/nmol with substrate curdlan, truncated protein CF of LamA
additional information
0.6 U/nmol with substrate pachyman, truncated protein SC of LamA
additional information
0.7 U/nmol with substrate barley beta-glucan, truncated protein SC of LamA
additional information
0.7 U/nmol with substrate curdlan, truncated protein SC of LamA
additional information
0.7 U/nmol with substrate lichenan, truncated protein SC of LamA
additional information
0.7 U/nmol with substrate zymosan A, truncated protein SC of LamA
additional information
0.8 U/nmol with substrate pachyman, truncated protein CB3 of LamA
additional information
0.8 U/nmol with substrate zymosan A, truncated protein CB3 of LamA
additional information
0.9 U/nmol with substrate barley beta-glucan, truncated protein CB3 of LamA
additional information
0.9 U/nmol with substrate lichenan, truncated protein CB3 of LamA
additional information
1.0 U/nmol with substrate curdlan, truncated protein CB3 of LamA
additional information
1.3 U/nmol with substrate lichenan, truncated protein CBF of LamA
additional information
1.3 U/nmol with substrate pachyman, truncated protein CBF of LamA
additional information
1.4 U/nmol with substrate laminarin, truncated protein C of LamA
additional information
1.5 U/nmol with substrate barley beta-glucan, truncated protein CBF of LamA
additional information
1.6 U/nmol with substrate zymosan A, truncated protein CBF of LamA
additional information
1.7 U/nmol with substrate laminarin, truncated protein CF of LamA
additional information
2.0 U/nmol with substrate curdlan, truncated protein CBF of LamA
additional information
2.6 U/nmol with substrate laminarin, truncated protein CB3 of LamA
additional information
3.7 U/nmol with substrate laminarin, truncated protein CBF of LamA
additional information
4.6 U/nmol with substrate laminarin, truncated protein SC of LamA
additional information
no activity with carboxymethylcellulose and xylan of all truncated proteins of LamA
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
5.8
6 - 6.5
Flavobacterium dormitator
-
pH 6.0 with yeast glucan, pH 6.5 with laminarin as substrate
6.5
5.5
toward laminarin hydrolysis for truncated proteins CBF and C
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 8
5 - 8
4.5 - 8
-
pH 4.5: about 60% of maximal activity, pH 8: about 50% of maximal activity
4.5 - 8
pH 4.5: abput 40% of maximal activity, pH 8.0: about 55% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
40
40 - 55
45
50
55
60
80
50
except for barley-beta-D-glucanase activity with an optimum at 40°C
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 70
-
30°C: about 90% of maximal activity, 70°C: about 50% of maximal activity
30 - 80
-
90% of maximal activity at 30°C, 40% of maximal activity at 80°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional CMCase and chitosanase, reactions of EC 3.2.1.4 and EC 3.2.16, respectively
UniProt
brenda
bifunctional CMCase and chitosanase, reactions of EC 3.2.1.4 and EC 3.2.16, respectively
UniProt
brenda
H(A16-M), a 1,3-1,4-beta-glucanase from Bacillus macerans in which the 16 N-terminal residues have been replaced by the respective residues of the enzyme from Bacillus amyloliquefaciens
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
Eng2 is present during the mitotic cycle, and accumulates after meiosis II, expression of eng2+ is required for the efficient release of ascospores, expression of eng2+ is highly upregulated during the sporulation process, and the product is mainly involved in spore morphogenesis
brenda
high expression in dormant conidia
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
Eng2 lacks a signal peptide for entry into the secretory pathway and therefore localizes intracellularly to the cytosol of the diploid cell
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to glycoside hydrolase family 8 (GH8) and contains A154TDGDMDIAYSLLLADKQW172. The enzyme has a lower ratio of lichenase/barley-beta-D-glucanase activities compared to glycoside hydrolase family GH16 enzymes
metabolism
enzyme is highly resistant to trypsin, alpha-chymotrypsin, collagenase and Neutrase 0.8L
physiological function
additional information
physiological function
-
When Schizosaccharomyces pombe diploid cells undergo meiosis, they differentiate into asci containing four haploid ascospores that are highly resistant to environmental stress. beta-Glucanase Eng2 and endo-alpha-1,3-glucanase Agn2 are required for ascus wall endolysis after sporulation in Schizosaccharomyces pombe
physiological function
-
the enzyme causes hydrolysis of the membrane of hyphae from Moniliophthora perniciosa. Recombinant beta-1,3-1,4-glucanase from Theobroma cacao impairs Moniliophthora perniciosa strain ALF553 mycelial growth
physiological function
a mutant lacking the activities of GH81 enzyme Eng1 and the activities of GH16 isoforms Eng2 to Eng5 shows conidial defects, with linear chains of conidia unable to separate while the germination rate is not affected. The mutant shows a about 51% decrease in the endo-beta-(1,3)-glucanase activity in in dormant conidia, about 74% in swollen morphotype and about 32% in germinating conidia
physiological function
-
a mutant lacking the activities of GH81 enzyme Eng1 and the activities of GH16 isoforms Eng2 to Eng5 shows conidial defects, with linear chains of conidia unable to separate while the germination rate is not affected. The mutant shows a about 51% decrease in the endo-beta-(1,3)-glucanase activity in in dormant conidia, about 74% in swollen morphotype and about 32% in germinating conidia
-
additional information
active site residues are Trp103, Asp104, Ile106, Ile108 and Glu109 in the beta-strand. Asp107 and Glu105 (as nucleophile) and Glu109 (as acid catalyst) are essential for enzyme activity. Molecular dynamics simulations and structure-function analysis, three-dimensional model, overview
additional information
Glu95 and Asp156 are catalytically active residues
additional information
modeled enzyme exhibits a (beta/alpha)8-barrel structure typical of GH5 members with an extra one-turn helix. One putative disulfide bridge might form to stabilize the loops
additional information
-
modeled enzyme exhibits a (beta/alpha)8-barrel structure typical of GH5 members with an extra one-turn helix. One putative disulfide bridge might form to stabilize the loops
additional information
-
the enzyme has an active site of 13 amino acids typical of glucanase with beta-1,3 and 1,4 action mode, comparative molecular modelling, overview. The enzyme's active site is composed of 13 amino acids, Trp93, Leu94, Lys95, Asp96, His97, Gly98, Pro99, Asp100, Lys101, Gly102, Phe103, Glu104, Asp105, a space of 2831 A, and presents alpha-helices and loop structures
additional information
-
modeled enzyme exhibits a (beta/alpha)8-barrel structure typical of GH5 members with an extra one-turn helix. One putative disulfide bridge might form to stabilize the loops
-
Show AA Sequence and Transmembrane Helices (3228 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
144600
calculated molecular mass of expressed CBF of LamA
22000
24000
x * 24200, about, sequence calculation, x * 24000, recombinant enzyme, SDS-PAGE
24200
x * 24200, about, sequence calculation, x * 24000, recombinant enzyme, SDS-PAGE
24440
x * 24440, sequence calculation, x * 25500, recombinant His-tagged enzyme, SDS-PAGE
25500
x * 24440, sequence calculation, x * 25500, recombinant His-tagged enzyme, SDS-PAGE
25580
-
x * 25580, sequence calculation, x * 22000, recombinant enzyme, SDS-PAGE
36000
36800
x * 36800, about, sequence calculation, x * 37000, deglycosylated recombinant enzyme, SDS-PAGE
37000
x * 36800, about, sequence calculation, x * 37000, deglycosylated recombinant enzyme, SDS-PAGE
62000
22000
-
x * 25580, sequence calculation, x * 22000, recombinant enzyme, SDS-PAGE
62000
-
SDS-PAGE, a second band of 41000 Da is detected, the larger band may either be a minor impurity or represent a native laminarinase dimer
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
x * 24200, about, sequence calculation, x * 24000, recombinant enzyme, SDS-PAGE
?
x * 24440, sequence calculation, x * 25500, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 24440, sequence calculation, x * 25500, recombinant His-tagged enzyme, SDS-PAGE
-
?
x * 36800, about, sequence calculation, x * 37000, deglycosylated recombinant enzyme, SDS-PAGE
?
-
x * 36800, about, sequence calculation, x * 37000, deglycosylated recombinant enzyme, SDS-PAGE
-
monomer
-
the enzyme is a single chain protein presenting 7 alpha-helices, 10 beta-sheets and 4 salt bridges
additional information
-
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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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
Flavobacterium dormitator
-
beta-1,3-glucanase I is formed by proteolysis of beta-1,3-glucanase II
glycoprotein
the degree of glycosylation is similar in the wild-type and recombinant proteins
glycoprotein
four putative N-glycosylation sites (Asn-Xaa-Thr/Ser-Zaa, where Zaa is not Pro) in the deduced TeEgl5A sequence
glycoprotein
-
four putative N-glycosylation sites (Asn-Xaa-Thr/Ser-Zaa, where Zaa is not Pro) in the deduced TeEgl5A sequence
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
3-D structure, at 1.5 A resolution, of CtLic26A in complex with thiopentasaccharide. Crystals are in space group P2(1)2(1)2(1) with cell dimensions of a = 49.3 A, b = 63.0 A and c = 78.3 A and with a single molecule of CtLic26A in the asymmetric unit
-
homology modeling of structure. Amino acids Glu380, Gln383, Asp384, Tyr395, Ser712, and Arg713 present in the protein are of core importance for binding activities and these residues are having strong hydrogen bond interactions with beta-(1,3)-glucan
-
crystal structure of truncated Fsbeta-glucanase in complex with beta-1,3-1,4-cellotriose, resolution of 2.3 A
-
hanging-drop vapor-diffusion at room temperature, space group P2(1)2(1)2(1), cell parameters: a = 75.77 A, b = 88.76 A, c = 154.79 A. High-resolution crystal structure of the hybrid 1,3-1,4-beta-glucanase H(A16-M)E105Q/E109Q in complex with a beta-glucan tetrasaccharide
-
structure was solved at 1.34 A resolution using native sulfur SAD X-ray crystallography. Crystallized in space group P2(1)2(1)2(1), with unit-cell parameters a = 38, b = 47, c = 152 A
-
X-ray crystallography screening of ligands bound nucleophile mutant E115S, to 1 A resolution. Laminariheptaose binds in an arch with the reducing and nonreducing ends occupying either side of the catalytic cleft of the enzyme. alpha-Laminariheptaosyl fluoride can make a nucleophilic attack upon itself, the major product being a cyclic beta-1,3-heptaglucan. The cyclic laminariheptaose molecule is not completely planar and torsion angles at the glycosidic linkages fluctuate between two energy minima
to 1.95 A resolution, and molecular dynamics simulation studies. LamR is formed mostly by beta-sheets in a complex jelly roll topology that is conserved among members of glycosyl hydrolase family 16. It contains a relatively large number of salt bridges, which are not randomly distributed on the structure. They form clusters interconnecting beta-sheets of the catalytic domain. Structure reveals a glycerol molecule fortuitously bound to the active site of the enzyme molecule
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E258A
-
kcat/Km for beta-glucan is 4.8fold lower than wild-type value
E70A
-
kcat/Km for beta-glucan is 36.5fold lower than wild-type value
F41A
-
kcat/Km for beta-glucan is 219fold lower than wild-type value
K260A
-
kcat/Km for beta-glucan is 31fold lower than wild-type value
N157A
-
kcat/Km for beta-glucan is 1.4fold lower than wild-type value
Q18A
-
kcat/Km for beta-glucan is 6.25fold lower than wild-type value
W114A
-
kcat/Km for beta-glucan is 3.5fold lower than wild-type value
W72A
-
kcat/Km for beta-glucan is 1.3fold higher than wild-type value
Y115A
-
kcat/Km for beta-glucan is 14.6fold lower than wild-type value
N207D
-
increase in Tm-value to 75.3°C, compared to wild-type Tm-value of 71.4°C
A98W
-
turnover-number for lichenan is 1.3fold lower than wild-type value, turnover-number for laminarin is 1.4fold higher than wild-type value
E131Q
-
turnover-number for lichenan is 3.9fold lower than wild-type value, turnover-number for laminarin is 1.2fold lower than wild-type value
E63D
-
turnover-number for lichenan is 10.5fold lower than wild-type value, turnover-number for laminarin is 27.1fold lower than wild-type value
E63Q
-
turnover-number for lichenan is 147fold lower than wild-type value, turnover-number for laminarin is 67.4fold lower than wild-type value
H99D
-
turnover-number for lichenan is 4.3fold lower than wild-type value, turnover-number for laminarin is 1.3fold lower than wild-type value
H99R
-
turnover-number for lichenan is 8.1fold lower than wild-type value, turnover-number for laminarin is 1.5fold lowerthan wild-type value
N26A
-
turnover-number for lichenan is 4.5fold lower than wild-type value, turnover-number for laminarin is 5.8fold lower than wild-type value
R65A
-
turnover-number for lichenan is 1.5fold lower than wild-type value, turnover-number for laminarin is 2.8fold lower than wild-type value
S90A
-
turnover-number for lichenan is 3.7fold lower than wild-type value, turnover-number for laminarin is 4.7fold lower than wild-type value
W184Y
-
turnover-number for lichenan is 7.3fold lower than wild-type value, turnover-number for laminarin is 2.8fold lower than wild-type value
W192A
-
turnover-number for lichenan is 29.4fold lower than wild-type value, turnover-number for laminarin is 12.5fold lower than wild-type value
Y123A
-
turnover-number for lichenan is 29.5fold lower than wild-type value, turnover-number for laminarin is 12.5fold lower than wild-type value
Y123F
-
turnover-number for lichenan is 1.9fold lower than wild-type value, turnover-number for laminarin is 2.5fold higher than wild-type value
Y24A
-
turnover-number for lichenan is 3.7fold lower than wild-type value, turnover-number for laminarin is 3.8fold lower than wild-type value
Y24F
-
turnover-number for lichenan is 2.5fold lower than wild-type value, turnover-number for laminarin is 1.5fold lower than wild-type value
Y24W
-
turnover-number for lichenan is 1.5fold lower than wild-type value, turnover-number for laminarin is 1.9fold higher than wild-type value
D156A
site-directed mutagenesis, the mutant shows a nearly complete loss of enzyme activity
E95A
site-directed mutagenesis, the mutant shows a nearly complete loss of enzyme activity
E115S
X-ray crystallography screening of ligands bound nucleophile mutant E115S. Laminariheptaose binds in an arch with the reducing and nonreducing ends occupying either side of the catalytic cleft of the enzyme. R-laminariheptaosyl fluoride can make a nucleophilic attack upon itself, the major product being a cyclic beta-1,3-heptaglucan
additional information
additional information
cloning and purification of shortende N-terminal family 54 substrate-binding module CBM54C. The binding constants of CBM54C to xylan, chitin, insoluble yeast cell wall beta-glucan, and bacterial crystalline cellulose are of the same order of magnitude as for module CBM54. The shortened module CBM54C does not bind pustulan, avicel, and chitosan, in contrast to CBM54. Calcium ions restore the ability of CBM54C to bind these three carbohydrates. The Ca2+-independent binding-sites for avicel, pustulan and chitosan are localized to the spontaneously split-off N-terminal part of 8 kDa of CBM54
additional information
-
construction of an expression plasmid pMB138 containing a fragment of gene gls fused to GFP and the acmA gene from Lactococcus lactis, encoding an N-acetylmuraminidase, which works as a functional anchor for the beta-glucanase imobilizing it on the cell surface of the transgenic cells. The mutant chimera shows endo-beta-1,3-1,4-glucanase in transformed Lactococcus lactis strain AS1.2829
additional information
-
recombinant expression of beta-1,3-1,4-glucanase from Bacillus subtilis fused to alpha-agglutinin and expressed under the control of the GAL1 promoter in Saccharomyces cerevisiae to construct a food-grade industrial arming yeast displaying beta-1,3-1,4-glucanase on the cell surface and enzyme activity, and to evaluate the thermal stability of the glucanase for practical application
additional information
-
construction of an expression plasmid pMB138 containing a fragment of gene gls fused to GFP and the acmA gene from Lactococcus lactis, encoding an N-acetylmuraminidase, which works as a functional anchor for the beta-glucanase imobilizing it on the cell surface of the transgenic cells. The mutant chimera shows endo-beta-1,3-1,4-glucanase in transformed Lactococcus lactis strain AS1.2829
-
additional information
-
deletion of the carbohydrate-binding domain results in a protein largely defective in complementing the cell separation defect of eng1 deletion mutants. This defect is due to a reduction of the catalytic activity against insoluble substrates and to a defect in targeting of truncated Eng1 to the septum, as the mutant localizes to the lateral cell wall
additional information
-
a point mutation, that destroys the catalytic activity of the protein, results in a phenotype similar to that of the mutant strain with gene eng2+ placed under the control of a repressible promoter. Exogenous addition of purified Eng2 releases the ascospores from asci generated by the eng2+-deficient mutant
additional information
-
construction of truncated proteins: a recombinant catalytic module polypeptide (rCD), a carbohydrate-binding module polypeptide composed of two family-22 carbohydrate-binding modules (rCBM) and a polypeptide composed of the family-22 carbohydrate-binding modules and the catalytic module (rCBM-CD). rCBM-CD is highly active towards beta-1,3-1,4-glucan, rCD is negligibly active towards the same substrate. The Vmax/KM value of rCBM-CD for beta-1,3-1,4-glucan is 7.8 times larger than that for oat-spelt xylan
additional information
-
engineering of truncated enzyme composed of two family-22 carbohydrate-binding modules and the catalytic module (rCBM22-CM), an enzyme composed of the catalytic module and family-9 carbohydrate-binding module (rCM-CBM9), and the catalytic module polypeptide. Although the addition of family-9 carbohydrate-binding module to rCM and rCM22-CM does not significantly change catalytic activity towards xylan and beta-1,3-1,4-glucan, the addition of family-22 carbohydrate-binding module to rCM and rCM-CBM9 drastically enhances catalytic activity towards xylan and especially beta-1,3-1,4-glucan. The addition of family-22 carbohydrate-binding module to rCM and rCM-CBM9 shofts the optimum temperature from 65°C to 75°C, but that of family-9 carbohydrate-binding module to rCM and rCM-22-CM does not affect the optimum temperature
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1 - 10
purified recombinant enzyme, stable at, the enzyme retains more than 90% of maximum activity at pH 4.0-5.0, over 80% of the activity remains after incubation at pH 1.0-10.0, 37°C for 1 h
729084
4 - 10
6 - 9
6 - 9
Flavobacterium dormitator
-
-
136721
6 - 9
Flavobacterium dormitator
-
enzymes I, II and IV: 10 min, 55°C, stable, unstable below pH 6 and above pH 9
136707
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 60
-
at 20°C 8% loss of activity, loss of 80% of activity after heating at 60°C for 3 min
30 - 60
-
stable at 30°C, 25% of original activity lost after incubation at 40°C for 1 h, complete denaturation within 10 min at 60°C
37
-
with barley beta-glucan as substrate, 26% of activity after 30 min, no activity after 180 min
40
50
50 - 60
-
stable for 20 min at 50°C, at 60°C loss of 75% of maximal activity
50 - 70
60
70
75
80
85
90
95 - 100
-
incubation at 100°C: 82% of initial activity at 95°C, 57% at 100°C
additional information
40
purified recombinant His-tagged enzyme, 80% remaining activity after 2 h
50
purified recombinant His-tagged enzyme, 70% remaining activity after 2 h
50 - 70
Flavobacterium dormitator
-
enzyme IV: 80% of activity after heating at 50°C for 10 min
50 - 70
Flavobacterium dormitator
-
enzyme I: full activity on heating at 55°C at pH 6.0 for 10 min, substantial loss of activity by heating at 70°C for 10 min
60
-
free recombinant enzyme, 2 h, 20.1% remaining activity. Recombinant enzyme in transgenic Saccharomyces cerevisiae cells shows increased activity with incubation time and reaches 129.2% of activity compared to controls after 1 h, then the activity gradually decreases
60
purified recombinant His-tagged enzyme, 20% remaining activity after 30 min, below 10% after 60 min
70
-
free recombinant enzyme, 2 h, almost no remaining activity. Recombinant enzyme in transgenic Saccharomyces cerevisiae cells shows increased activity with incubation time and reaches 109.2% of activity compared to controls after 1 h, then the activity gradually decreases
70
purified recombinant His-tagged enzyme, inactivation within 10 min
70
purified recombinant enzyme, 60% of maximal activity after 1 h
80
purified recombinant His-tagged enzyme, inactivation within 5 min
80
purified recombinant enzyme, 50% of maximal activity after 1 h
85
purified recombinant enzyme, 30% of maximal activity after 1 h
90
purified recombinant enzyme, 50% of maximal activity after 10 min
additional information
-
hypothesis for thermal inactivation: the first phase in thermal denaturation could be produced when calcium interactions are disrupted and the main loop becomes free to rearrange. This phase yields a partially active intermediary during the first phase of inactivation and then the intermediary is slowly converted into a totally inactive enzyme in the second phase
additional information
enzyme shows relatively low thermostability, which is stabilized by adding laminarin, xylan, colloidal chitin, pectin, and its related polysaccharides
additional information
Ca2+ increases the heat stability of the lichenase activity retaining 59% activity in the presence of Ca2+ after 15 min of heat treatment at 70°C, compared to 34% in the absence of Ca2+. Ca2+ also increases the heat stability of the beta-glucanase activity (from 18 to 28%). No significant influence of Ca2+ on the heat stability of the chitosanase and CMCase activities are observed
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
about 66% of activity lost after dialysis against distilled water at 2°C for 18 h
-
calcium ion has a general stabilizing effect on Bacillus beta-1,3-1,4 glucanases
resistant against proteolysis by trypsin and chymotrypsin, slow digestion by protease V8, complete digestion by thermolysin
-
stabilization of activity at 37°C for 3 h by bovine serum albumin, no effect for longer periods
-
stable against proteolysis, full activity after papain treatment for 20 h
Flavobacterium dormitator
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ethanol
-
40% of activity after 20 min incubation with 10% v/v ethanol
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 0.1 M McIlvaine buffer, pH 5.8, retains almost all initial activity after 1 week of storage
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
beta-1,3-glucanase II from periplasmic fraction of Escherichia coli clone cells
Flavobacterium dormitator
-
immobilized Ni2+ affinity chromatography, gel filtration chromatography
native enzyme 10.1fold by anion exchange and hydroxyapatite chromatography
native enzyme 126fold by ammonium sulfate fractionation, several steps of cation exchange chromatography, and gel filtration
-
native enzyme 340fold from digestive fluid by ammonium sulfate fractionation, hydrophobic interaction and cation exchange chromatography, and gel filtration to homogeneity
-
precipitation, a combination of anion exchange, hydrophobic interaction and gel filtration chromatography, all chromatography is carried out at 4°C
-
recombinant enzyme
recombinant enzyme from Escherichia coli strain BL21(DE3) to homogeneity
recombinant enzyme from Pichia pastoris strain GS115 culture supernatant by ultrafiltration, gel filtration, anion exchange chromatography, followed by deglycosylation
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography
-
recombinant protein
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, expression of the His-tagged enzyme in Escherichia coli strain Bl21
DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant heterologous enzyme expression of His-tagged enzyme in Escherichia coli strain Rosetta (DE3)
-
expression in Escherichia coli
expression in Escherichia coli, Enterococcus faecalis, Lactococcus lactis
-
expression in Pichia pastoris
expression in Pichia pastoris. The beta-1,3-1,4-glucanase gene is modified and expressed according to its preferred codon usage
expression of five truncated proteins of LamA in Escherichia coli BL21(DE3)
expression of recombinant truncated proteins in Escherichia coli
-
gene bglc8H, DNA and amino acid sequence determination and analysis, phylogenetic tree, cloning in Escherichia coli strain DH5alpha
gene gls, expression of a fragment of gene gls fused to GFP and the acmA gene from Lactococcus lactis, encoding an N-acetylmuraminidase, in Lactococcus lactis strain AS1.2829, the recombinant chimera is functional
-
gene SU40-glu, DNA and amino acid sequence determination and analysis, phylogenetic analysis, overexpression in Escherichia coli strain BL21(DE3)
gene Teegl5A, DNA and amino acid sequence determination and analysis, cloning in Escherichia coli strain Trans-T1, functional expression in Pichia pastoris strain GS115 and secretion to the culture medium
placing of gene eng2+ under the control of a repressible promoter
-
subcloning in Escherichia coli strain Dh5alpha, recombinant expression of beta-1,3-1,4-glucanase from Bacillus subtilis fused to alpha-agglutinin and expressed under the control of the GAL1 promoter in Saccharomyces cerevisiae, plasmid construction, overview
-
the enda-beta-(1-3),(1-4)-glucanase gene bglBC1 is modified by substituting its native promoter with a strong promoter, BJ27X, to increase expression of the gene when cloned into Bacillus subtilis RM125 and Bacillus megaterium ATCC14945
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
analysis
biotechnology
-
construction of a transgenic yeast, Saccharomyces cerevisiae, expressing the enzyme, results in a food-grade yeast that has the potential to improve the brewing properties of beer
degradation
-
oligosaccharides with degree of polymerization 2-10 are formed by hydrolysis of beta-glucan and laminarin. The recombinant enzyme preparations are fast and effective in decreasing the reduced viscosity of wholegrain barley extract than some commercial enzyme preparations
drug development
the various truncated proteins of LamA also show inhibition on the mycelium growth of Rhizopus solani, a pathogen infecting a broad range of many crops, suggesting the application potential of LamA as an antifungal agent in many aspects
food industry
nutrition
synthesis
additional information
agriculture
-
disease protection of plants because of antimycotic activity in combination with chitinases
agriculture
-
Streptomyces sp. 9X166 culture filtrate shows hydrolytic activity toward Phytophthora sp. Solutions with beta-1,3-glucanase activity are able to degrade both freeze-dried and living mycelium
analysis
assay procedure for the measurement of beta-glucanase and lichenase in crude enzyme extracts. Substrate 4,6-O-benzylidene-2-chloro-4-nitrophenyl-beta-3'-cellotriosyl-beta-glucopyranoside is a more generally applicable reagent. Standard curves allow the assay absorbance response to be directly converted to beta-glucanase/lichenase activity on barley beta-glucan. Manual and automated assay formats aloow the analysis of beta-glucanase in malt flour and lichenase enzyme extracts and the assays are repeatable
food industry
-
construction of a transgenic yeast, Saccharomyces cerevisiae, expressing the enzyme, results in a food-grade yeast that has the potential to improve the brewing properties of beer
food industry
application in malting and brewing industry. Under simulated mashing conditions, addition of Agl9A at 20 U/ml or a commercial xylanase at 200 U/ml reduce the filtration rate by 26.71% and 20.21%, respectively, and viscosity by 6.12% and 4.78%, respectively. Combined use of Agl9A at 10 U/ml and the xylanase at 100 U/ml even more effectively reduces the filtration rate by 31.73% and viscosity by 8.79%
food industry
the enzyme reduces viscosity of mash during brewing peocesses
food industry
-
the enzyme reduces viscosity of mash during brewing peocesses
-
nutrition
-
reducing the amount of high-molecular-mass beta-glucans during malting in brewing industry, improvement of digestibility in broiler chicks production
nutrition
-
reducing the amount of high-molecular-mass beta-glucans during malting in brewing industry, improvement of digestibility in broiler chicks production
nutrition
-
endo-beta-D-glucanases EG VI and EG VII are ideal candidates for tailored modification of macromolecular beta-glucan in industrial applications
nutrition
-
endo-beta-D-glucanases EG VI and EG VII are ideal candidates for tailored modification of macromolecular beta-glucan in industrial applications
-
synthesis
-
the major products of water-soluble beta-glucan hydrolyzed by over-produced endo-beta-(1-3),(1-4)-glucanase are trioligosaccharides and tetrasaccharides, which can be developed as useful products such as antihypercholesterolemic, anti-hypertriglyceridemic, and anti-hyperglycemic agents
synthesis
Niallia circulans ATCC 21367
-
the major products of water-soluble beta-glucan hydrolyzed by over-produced endo-beta-(1-3),(1-4)-glucanase are trioligosaccharides and tetrasaccharides, which can be developed as useful products such as antihypercholesterolemic, anti-hypertriglyceridemic, and anti-hyperglycemic agents
-
additional information
the enzyme is a good candidate for extensive application in the detergent, textile, feed, and food industries
additional information
-
the enzyme is a good candidate for extensive application in the detergent, textile, feed, and food industries
additional information
-
the enzyme is a good candidate for extensive application in the detergent, textile, feed, and food industries
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Schwarz, W.; Bronnenmeier, K.; Staudenbauer, W.L.
Molecular cloning of Clostridium thermocellum genes involved in beta-glucan degradation in bacteriophage lambda
Biotechnol. Lett.
7
859-864
1985
Acetivibrio thermocellus
-
brenda
Manners, D.J.; Wilson, G.
Studies on beta-glucanases. Some properties of a bacterial endo-beta-(1-3)-glucanase system
Biochem. J.
135
11-18
1973
Flavobacterium sp.
brenda
Borriss, R.; Schroeder, K.L.
beta-1,3-1,4-Glucanase in spore-forming microorganisms. The efficiency of beta-glucanases in reducing the viscosity of wort
Zentralbl. Bakteriol. Parasitenkd. Infektionskr. Hyg. , Abt. II
136
324-329
1981
Paenibacillus macerans
-
brenda
Sharma, A.; Nakas, J.P.
Preliminary characterization of laminarinase from Trichoderma longibrachiatum
Enzyme Microb. Technol.
9
89-93
1987
Trichoderma longibrachiatum
-
brenda
Totsuka, A.; Usui, T.
Separation and characterization of the endo-beta-(1-3)-D-glucanase from Rhizoctonia solani
Agric. Biol. Chem.
50
543-550
1986
Rhizoctonia solani
-
brenda
Leatham, G.F.
Extracellular enzymes produced by the cultivated mushroom Lentinus edodes during degradation of a lignocellulosic medium
Appl. Environ. Microbiol.
50
859-867
1985
Lentinula edodes
brenda
Wong, Y.S.; MacClachlan, G.A.
1,3-beta-D-Glucanases from Pisum sativum seedlings
Plant Physiol.
65
222-228
1980
Pisum sativum
brenda
Villa, T.G.; Phaff, H.J.
Recovery of invertase and laminarinases from industrial waste broth of baker's yeast
Eur. J. Appl. Microbiol. Biotechnol.
9
9-14
1980
Saccharomyces cerevisiae
-
brenda
Martinez, M.J.; Reyes, F.; Lahoz, R.; Perez-Leblic, M.I.
Lytic enzymes in autolysis of Botrytis cinerea
FEMS Microbiol. Lett.
19
157-160
1983
Botrytis cinerea
-
brenda
Nagasaki, S.; Mori, H.; Yamamoto, S.
Characterization of endo beta-1,3-glucanase IV from Flavobacterium dorminator var. glucanolyticae FA-5
Agric. Biol. Chem.
45
2689-2694
1981
Flavobacterium dormitator
-
brenda
Kawai, M.; Noguchi, M.; Shimura, G.; Suga, Y.; Samejima, H.
Effect of different culture conditions on production of cellulolytic and plant tissue macerating enzymes by Irpex lacteus Fr.
Agric. Biol. Chem.
42
333-337
1978
Irpex lacteus
-
brenda
Salyers, A.A.; Palmer, J.K.; Wilkins, T.D.
Laminarinase (beta-glucanase) activity in Bacteroides from the human colon
Appl. Environ. Microbiol.
33
1118-1124
1977
Bacteroides fragilis, Bacteroides thetaiotaomicron, Parabacteroides distasonis
brenda
Santos, T.; Villanueva, J.R.; Nombela, C.
Production and catabolite repression of Penicillium italicum beta-glucanases
J. Bacteriol.
129
52-58
1977
Penicillium italicum
brenda
Slakeski, N.; Fincher, G.B.
Barley (1-3,1-4)-beta-glucanase isoenzyme E1 gene expression is medaited by auxin and giberellic acid
FEBS Lett.
306
98-102
1992
Hordeum vulgare
brenda
Planas, A.; Juncosa, M.; Cayetano, A.; Querol, E.
Studies on Bacillus licheniformis endo-beta-1,3-1,4-D-glucanase: characterization and kinetic analysis
Appl. Microbiol. Biotechnol.
37
583-589
1992
Bacillus licheniformis
-
brenda
Isakov, V.V.; Sova, V.V.; Denisenko, V.A.; Sakharovsky, V.G.; Elyakova, L.A.; Dzizenko, A.K.
A study of the action of laminarinases from Spisula sacchalinensis by the use of nuclear magnetic resonance
Biochim. Biophys. Acta
268
184-186
1972
Pseudocardium sachalinense
brenda
Tingle, M.A.; Halvorson, H.O.
A comparison of beta-glucanase and beta-glucosidase in Saccharomyces lactis
Biochim. Biophys. Acta
250
165-171
1971
Kluyveromyces lactis
brenda
Sova, V.V.; Elyakova, L.A.; Vaskovsky, V.E.
Purification and some properties of beta-1,3-glucan glucanohydrolase from the crystalline style of bivalvia, Spisula sacchalinensis
Biochim. Biophys. Acta
212
111-115
1970
Pseudocardium sachalinense
brenda
Totani, K.; Harumiya, S.; Nanjo, F.; Usui, T.
Substrate affinity chromatography of beta-1,3-glucanase from Basidiomycetes species
Agric. Biol. Chem.
47
1159-1162
1983
Basidiomycota
-
brenda
Villa, T.G.; Notario, V.; Villanueva, J.R.
Occurrence of an endo-1,3-beta-glucanase in culture fluids of the yeast Candida utilis. Purification and characterization of the enzyme activity
Biochem. J.
177
107-114
1979
Cyberlindnera jadinii
brenda
Manners, D.J.; Marshall, J.J.
Some properties of a beta-1,3-glucanase from rye
Phytochemistry
12
547-553
1973
Secale cereale
-
brenda
Mueller, J.J.; Thomsen, K.K.; Heinemann, U.
Crystal structure of barley 1,3-1,4-beta-glucanase at 2.0-A resolution and comparison with Bacillus 1,3-1,4-beta-glucanase
J. Biol. Chem.
273
3438-3446
1998
Hordeum vulgare
brenda
Nagata, S.; Sawatani, M.; Kuriyama, M.; Misono, H.; Nagasaki, S.
Purification and characterization of nonlytic endo-beta-1,3-glucanase I from Flavobacterium dormitator var. glucanolyticae
Agric. Biol. Chem.
54
2107-2114
1990
Flavobacterium dormitator
-
brenda
Zverlov, V.V.; Volkov, I.Y.; Velikodvorskaya, T.V.; Schwarz, W.H.
Highly thermostable endo-1,3-beta-glucanase (laminarinase) LamA from Thermotoga neapolitana: nucleotide sequence of the gen and characterization of the recombinant gene product
Microbiology
143
1701-1708
1997
Thermotoga neapolitana
brenda
Ekinci, M.S.; McCrae, S.I.; Flint, H.J.
Isolation and overexpression of a gene encoding an extracellular beta-(1,3-1,4)-glucanase from Streptococcus bovis JB1
Appl. Environ. Microbiol.
63
3752-3756
1997
Streptococcus equinus JB1
brenda
Nagata, S.; Isafumi, M.; Ishihara, F.; Misono, H.; Nagasaki, S.
Cloning and expression of endo-beta-1,3-glucanase gene from Flavobacterium dorminator in Escherichia coli and characterization of the gene product
Agric. Biol. Chem.
54
2675-2680
1990
Flavobacterium dormitator
brenda
Bang, M.L.; Villadsen, I.; Sandal, T.
Cloning and characterization of an endo-beta-1,3(4)glucanase and an aspartic protease from Phaffia rhodozyma CBS 6938
Appl. Microbiol. Biotechnol.
51
215-222
1999
Phaffia rhodozyma, Phaffia rhodozyma CBS 6938
brenda
Thrane, C.; Tronsmo, A.; Jensen, D.F.
endo-1,3-beta-Glucanase and cellulase from Trichoderma harzianum: purification and partial characterization, induction of and biological activity against plant pathogenic Pythium spp.
Eur. J. Plant Physiol.
103
331-344
1997
Trichoderma harzianum
brenda
Petersen, B.O.; Krah, M.; Duus, J.O.; Thomsen, K.K.
A transglycosylating 1,3(4)-beta-glucanase from Rhodothermus marinus. NMR analysis of enzyme reactions
Eur. J. Biochem.
267
361-369
2000
Rhodothermus marinus
brenda
Genta, F.A.; Terra, W.R.; Ferreira, C.
Action pattern, specificity, lytic activities, and physiological role of five digestive beta-glucanases isolated from Periplaneta americana
Insect Biochem. Mol. Biol.
33
1085-1097
2003
Periplaneta americana
brenda
McCarthy, T.; Hanniffy, O.; Savage, A.V.; Tuohy, M.G.
Catalytic properties and mode of action of three endo-beta-glucanases from Talaromyces emersonii on soluble beta-1,4- and beta-1,3;1,4-linked glucans
Int. J. Biol. Macromol.
33
141-148
2003
Rasamsonia emersonii, Rasamsonia emersonii CBS 814.70
brenda
Zhao, G.; Ali, E.; Araki, R.; Sakka, M.; Kimura, T.; Sakka, K.
Function of the family-9 and family-22 carbohydrate-binding modules in a modular beta-1,3-1,4-glucanase/xylanase derived from Clostridium stercorarium Xyn10B
Biosci. Biotechnol. Biochem.
69
1562-1567
2005
Thermoclostridium stercorarium
brenda
Kim, K.H.; Kim, Y.O.; Ko, B.S.; Youn, H.J.; Lee, D.S.
Over-expression of the gene (bglBC1) from Bacillus circulans encoding an endo-beta-(1-->3),(1-->4)-glucanase useful for the preparation of oligosaccharides from barley beta-glucan
Biotechnol. Lett.
26
1749-1755
2004
Niallia circulans, Niallia circulans ATCC 21367
brenda
Araki, R.; Ali, M.K.; Sakka, M.; Kimura, T.; Sakka, K.; Ohmiya, K.
Essential role of the family-22 carbohydrate-binding modules for beta-1,3-1,4-glucanase activity of Clostridium stercorarium Xyn10B
FEBS Lett.
561
155-158
2004
Thermoclostridium stercorarium
brenda
Tsai, L.C.; Shyur, L.F.; Cheng, Y.S.; Lee, S.H.
Crystal structure of truncated Fibrobacter succinogenes 1,3-1,4-beta-D-glucanase in complex with beta-1,3-1,4-cellotriose
J. Mol. Biol.
354
642-651
2005
Fibrobacter succinogenes
brenda
Gaiser, O.J.; Piotukh, K.; Ponnuswamy, M.N.; Planas, A.; Borriss, R.; Heinemann, U.
Structural basis for the substrate specificity of a Bacillus 1,3-1,4-beta-glucanase
J. Mol. Biol.
357
1211-1225
2006
Paenibacillus macerans
brenda
Vasur, J.; Kawai, R.; Larsson, A.M.; Igarashi, K.; Sandgren, M.; Samejima, M.; Stahlberg, J.
X-ray crystallographic native sulfur SAD structure determination of laminarinase Lam16A from Phanerochaete chrysosporium
Acta Crystallogr. Sect. D
62
1422-1429
2006
Phanerodontia chrysosporium
brenda
Kawai, R.; Igarashi, K.; Yoshida, M.; Kitaoka, M.; Samejima, M.
Hydrolysis of beta -1,3/1,6-glucan by glycoside hydrolase family 16 endo-1,3(4)-beta-glucanase from the basidiomycete Phanerochaete chrysosporium
Appl. Microbiol. Biotechnol.
71
898-906
2006
Phanerodontia chrysosporium (Q874E3), Phanerodontia chrysosporium
brenda
Teng, D.; Wang, J.H.; Fan, Y.; Yang, Y.L.; Tian, Z.G.; Luo, J.; Yang, G.P.; Zhang, F.
Cloning of beta-1,3-1,4-glucanase gene from Bacillus licheniformis EGW039 (CGMCC 0635) and its expression in Escherichia coli BL21 (DE3)
Appl. Microbiol. Biotechnol.
72
705-712
2006
Bacillus licheniformis, Bacillus licheniformis EGW039 / CGMCC 0635
brenda
Teng, D.; Fan, Y.; Yang, Y.L.; Tian, Z.G.; Luo, J.; Wang, J.H.
Codon optimization of Bacillus licheniformis beta-1,3-1,4-glucanase gene and its expression in Pichia pastoris
Appl. Microbiol. Biotechnol.
74
1074-1083
2007
Bacillus licheniformis (Q8GMY0), Bacillus licheniformis
brenda
Boyce, A.; Walsh, G.
Production, purification and application-relevant characterisation of an endo-1,3(4)-beta-glucanase from Rhizomucor miehei
Appl. Microbiol. Biotechnol.
76
835-841
2007
Rhizomucor miehei
brenda
Tamoi, M.; Kurotaki, H.; Fukamizo, T.
beta-1,4-Glucanase-like protein from the cyanobacterium Synechocystis PCC6803 is a beta-1,3-1,4-glucanase and functions in salt stress tolerance
Biochem. J.
405
139-146
2007
Synechocystis sp. PCC 6803 (Q55365), Synechocystis sp. PCC 6803
brenda
Gargallo, R.; Cedano, J.; Mozo-Villarias, A.; Querol, E.; Oliva, B.
Study of the influence of temperature on the dynamics of the catalytic cleft in 1,3-1,4-beta-glucanase by molecular dynamics simulations
J. Mol. Model.
12
835-845
2006
Bacillus licheniformis
brenda
Money, V.A.; Cartmell, A.; Guerreiro, C.I.; Ducros, V.M.; Fontes, C.M.; Gilbert, H.J.; Davies, G.J.
Probing the beta-1,3:1,4 glucanase, CtLic26A, with a thio-oligosaccharide and enzyme variants
Org. Biomol. Chem.
6
851-853
2008
Acetivibrio thermocellus
brenda
Allardyce, B.J.; Linton, S.M.
Purification and characterisation of endo-beta-1,4-glucanase and laminarinase enzymes from the gecarcinid land crab Gecarcoidea natalis and the aquatic crayfish Cherax destructor
J. Exp. Biol.
211
2275-2287
2008
Cherax destructor, Cherax destructor Clark 1936
brenda
Cheng, Y.M.; Hong, T.Y.; Liu, C.C.; Meng, M.
Cloning and functional characterization of a complex endo-beta-1,3-glucanase from Paenibacillus sp.
Appl. Microbiol. Biotechnol.
81
1051-1061
2009
Paenibacillus sp. CCRC 17245 (Q000P7)
brenda
Martin-Cuadrado, A.B.; Encinar del Dedo, J.; de Medina-Redondo, M.; Fontaine, T.; del Rey, F.; Latge, J.P.; Vazquez de Aldana, C.R.
The Schizosaccharomyces pombe endo-1,3-beta-glucanase Eng1 contains a novel carbohydrate binding module required for septum localization
Mol. Microbiol.
69
188-200
2008
Schizosaccharomyces pombe
brenda
Qiao, J.; Dong, B.; Li, Y.; Zhang, B.; Cao, Y.
Cloning of a beta-1,3-1,4-glucanase gene from Bacillus subtilis MA139 and its functional expression in Escherichia coli
Appl. Biochem. Biotechnol.
152
334-342
2009
Bacillus subtilis (A8CGP1), Bacillus subtilis MA139 (A8CGP1), Bacillus subtilis MA139
brenda
Kumagai, Y.; Ojima, T.
Enzymatic properties and the primary structure of a beta-1,3-glucanase from the digestive fluid of the Pacific abalone Haliotis discus hannai
Comp. Biochem. Physiol. B
154
113-120
2009
Haliotis discus hannai
brenda
Kumagai, Y.; Ojima, T.
Isolation and characterization of two types of beta-1,3-glucanases from the common sea hare Aplysia kurodai
Comp. Biochem. Physiol. B
155
138-144
2010
Aplysia kurodai
brenda
Encinar del Dedo, J.; Duenas, E.; Arnaiz, Y.; del Rey, F.; Vazquez de Aldana, C.R.
beta-glucanase Eng2 is required for ascus wall endolysis after sporulation in the fission yeast Schizosaccharomyces pombe
Eukaryot. Cell
8
1278-1286
2009
Schizosaccharomyces pombe
brenda
Guo, Q.; Zhang, W.; Ma, L.L.; Chen, Q.H.; Chen, J.C.; Zhang, H.B.; Ruan, H.; He, G.Q.
A food-grade industrial arming yeast expressing beta-1,3-1,4-glucanase with enhanced thermal stability
J. Zhejiang Univ. Sci. B
11
41-51
2010
Bacillus subtilis
brenda
Li, X.; Huang, X.; Shao, X.; Li, L.
Functional cell surface display of endo-beta-1,3-1,4-glucanase in Lactococcus lactis using N-acetylmuraminidase as the anchoring motif
Sheng Wu Gong Cheng Xue Bao
25
89-94
2009
Bacillus subtilis, Bacillus subtilis BF7658
brenda
Bai, Y.; Wang, J.; Zhang, Z.; Shi, P.; Luo, H.; Huang, H.; Luo, C.; Yao, B.
A novel family 9 beta-1,3(4)-glucanase from thermoacidophilic Alicyclobacillus sp. A4 with potential applications in the brewing industry
Appl. Microbiol. Biotechnol.
87
251-259
2010
Alicyclobacillus sp. (D7PC10)
brenda
Vasur, J.; Kawai, R.; Jonsson, K.H.; Widmalm, G.; Engstroem, A.; Frank, M.; Andersson, E.; Hansson, H.; Forsberg, Z.; Igarashi, K.; Samejima, M.; Sandgren, M.; Stahlberg, J.
Synthesis of cyclic beta-glucan using laminarinase 16A glycosynthase mutant from the basidiomycete Phanerochaete chrysosporium
J. Am. Chem. Soc.
132
1724-1730
2010
Phanerodontia chrysosporium (Q874E3), Phanerodontia chrysosporium
brenda
Bleicher, L.; Prates, E.T.; Gomes, T.C.; Silveira, R.L.; Nascimento, A.S.; Rojas, A.L.; Golubev, A.; Martinez, L.; Skaf, M.S.; Polikarpov, I.
Molecular basis of the thermostability and thermophilicity of laminarinases: X-ray structure of the hyperthermostable laminarinase from Rhodothermus marinus and molecular dynamics simulations
J. Phys. Chem. B
115
7940-7949
2011
Rhodothermus marinus (O52754)
brenda
Dvortsov, I.; Lunina, N.; Zverlov, V.; Velikodvorskaia, G.
Substrate-binding properties of family 54 module of laminarinase Lic16A of Clostridium thermocellum
Mol. Biol. (Mosk.)
44
671-676
2010
Acetivibrio thermocellus (Q59328)
brenda
Wang, K.; Luo, H.; Bai, Y.; Shi, P.; Huang, H.; Xue, X.; Yao, B.
A thermophilic endo-1,4-beta-glucanase from Talaromyces emersonii CBS394.64 with broad substrate specificity and great application potentials
Appl. Microbiol. Biotechnol.
98
7051-7060
2014
Rasamsonia emersonii (X4YXV3), Rasamsonia emersonii, Rasamsonia emersonii CBS394.64 (X4YXV3)
brenda
Masilamani, R.; Sharma, O.P.; Muthuvel, S.K.; Natarajan, S.
Cloning, expression of beta-1,3-1,4 glucanase from Bacillus subtilis SU40 and the effect of calcium ion on the stability of recombinant enzyme: in vitro and in silico analysis
Bioinformation
9
958-962
2013
Bacillus licheniformis (Q84GK1)
brenda
Na, H.B.; Jung, W.K.; Jeong, Y.S.; Kim, H.J.; Kim, S.K.; Kim, J.; Yun, H.D.; Lee, J.K.; Kim, H.
Characterization of a GH family 8 beta-1,3-1,4-glucanase with distinctive broad substrate specificity from Paenibacillus sp. X4
Biotechnol. Lett.
37
643-655
2015
Paenibacillus sp. (A0A088BCU2)
brenda
Britto, D.S.; Pirovani, C.P.; Andrade, B.S.; Dos Santos, T.P.; Pungartnik, C.; Cascardo, J.C.; Micheli, F.; Gesteira, A.S.
Recombinant beta-1,3-1,4-glucanase from Theobroma cacao impairs Moniliophthora perniciosa mycelial growth
Mol. Biol. Rep.
40
5417-5427
2013
Theobroma cacao
brenda
Kobayashi, T.; Uchimura, K.; Kubota, T.; Nunoura, T.; Deguchi, S.
Biochemical and genetic characterization of beta-1,3 glucanase from a deep subseafloor Laceyella putida
Appl. Microbiol. Biotechnol.
100
203-214
2016
Laceyella putida (A0A0P0UPC6), Laceyella putida JAM FM3001 (A0A0P0UPC6)
brenda
Ahmed, R.; Jain, S.K.; Shukla, P.K.
In-silico characterization of beta-(1,3)-endoglucanase (ENGL1) from Aspergillus fumigatus by homology modeling and docking studies
Bioinformation
9
802-807
2013
Aspergillus fumigatus
brenda
Kuge, T.; Nagoya, H.; Tryfona, T.; Kurokawa, T.; Yoshimi, Y.; Dohmae, N.; Tsubaki, K.; Dupree, P.; Tsumuraya, Y.; Kotake, T.
Action of an endo-beta-1,3(4)-glucanase on cellobiosyl unit structure in barley beta-1,3:1,4-glucan
Biosci. Biotechnol. Biochem.
79
1810-1817
2015
Trichoderma sp.
brenda
Mangan, D.; Liadova, A.; Ivory, R.; McCleary, B.V.
Novel approaches to the automated assay of beta-glucanase and lichenase activity
Carbohydr. Res.
435
162-172
2016
Acetivibrio thermocellus (Q59328)
brenda
Mouyna, I.; Aimanianda, V.; Hartl, L.; Prevost, M.C.; Sismeiro, O.; Dillies, M.A.; Jagla, B.; Legendre, R.; Coppee, J.Y.; Latge, J.P.
GH16 and GH81 family beta-(1,3)-glucanases in Aspergillus fumigatus are essential for conidial cell wall morphogenesis
Cell. Microbiol.
18
1285-1293
2016
Aspergillus fumigatus (Q4WEA1), Aspergillus fumigatus (Q4WJP2), Aspergillus fumigatus (Q4WQM7), Aspergillus fumigatus (Q4X084), Aspergillus fumigatus ATCC MYA-4609 (Q4WEA1), Aspergillus fumigatus ATCC MYA-4609 (Q4WJP2), Aspergillus fumigatus ATCC MYA-4609 (Q4WQM7), Aspergillus fumigatus ATCC MYA-4609 (Q4X084)
brenda
Sakdapetsiri, C.; Fukuta, Y.; Aramsirirujiwet, Y.; Shirasaka, N.; Kitpreechavanich, V.
Antagonistic activity of endo-beta-1,3-glucanase from a novel isolate, Streptomyces sp. 9X166, against black rot in orchids
J. Basic Microbiol.
56
469-479
2016
Streptomyces sp.
brenda
Merzlov, D.A.; Zorov, I.N.; Dotsenko, G.S.; Denisenko, Y.A.; Rozhkova, A.M.; Satrutdinov, A.D.; Rubtsova, E.A.; Kondratieva, E.G.; Sinitsyn, A.P.
Properties of enzyme preparations and homogeneous enzymes - endoglucanases EG2 Penicillium verruculosum and LAM Myceliophthora thermophila
Biochemistry (Moscow)
80
473-482
2015
Thermothelomyces heterothallicus
brenda
Murray, P.G.; Grassick, A.; Laffey, C.D.; Cuffe, M.M.; Higgins, T.; Savage, A.V.; Planas, A.; Tuohy, M.G.
Isolation and characterization of a thermostable endo-beta-glucanase active on 1,3-1,4-beta-D-glucans from the aerobic fungus Talaromyces emersonii CBS 814.70
Enzyme Microb. Technol.
29
90-98
2001
Rasamsonia emersonii, Rasamsonia emersonii CBS 814.70
brenda
Saraihom, S.; Kobayashi, D.; Lotrakul, P.; Prasongsuk, S.; Eveleigh, D.; Punnapayak, H.
First report of a tropical Lysobacter enzymogenes producing bifunctional endoglucanase activity towards carboxymethylcellulose and chitosan
Ann. Microbiol.
66
907-919
2016
Lysobacter enzymogenes (A0A0K2GVV7), Lysobacter enzymogenes 521 (A0A0K2GVV7)
-
brenda
Kim, D.; Lee, M.; Cho, H.; Lee, J.; Lee, M.; Chung, C.; Shin, D.; Rhee, Y.; Son, K.; Park, H.
Genetic and functional characterization of an extracellular modular GH6 endo-beta-1,4-glucanase from an earthworm symbiont, Cellulosimicrobium funkei HY-13
Antonie van Leeuwenhoek
109
1-12
2016
Cellulosimicrobium funkei (A0A0P0IZM9), Cellulosimicrobium funkei HY-13 (A0A0P0IZM9)
brenda
Meng, D.D.; Wang, B.; Ma, X.Q.; Ji, S.Q.; Lu, M.; Li, F.L.
Characterization of a thermostable endo-1,3(4)-beta-glucanase from Caldicellulosiruptor sp. strain F32 and its application for yeast lysis
Appl. Microbiol. Biotechnol.
100
4923-4934
2016
Caldicellulosiruptor sp. F32 (A0A0S2UQ60)
brenda
Wang, J.; Kang, L.; Liu, Z.; Yuan, S.
Gene cloning, heterologous expression and characterization of a Coprinopsis cinerea endo-beta-1,3(4)-glucanase
Fungal Biol.
121
61-68
2017
Coprinopsis cinerea (A8N2G5), Coprinopsis cinerea ATCC MYA-4618 (A8N2G5)
brenda
Li, J.; Xu, X.; Shi, P.; Liu, B.; Zhang, Y.; Zhang, W.
Overexpression and characterization of a novel endo-beta-1,3(4)-glucanase from thermophilic fungus Humicola insolens Y1
Protein Expr. Purif.
138
63-68
2017
Humicola insolens (A0A0U2RV57), Humicola insolens Y1 (A0A0U2RV57)
brenda
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