Information on EC 3.2.1.6 - endo-1,3(4)-beta-glucanase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
3.2.1.6
-
RECOMMENDED NAME
GeneOntology No.
endo-1,3(4)-beta-glucanase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Endohydrolysis of (1->3)- or (1->4)-linkages in beta-D-glucans when the glucose residue whose reducing group is involved in the linkage to be hydrolysed is itself substituted at C-3
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
62213-14-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
ATCC21367
-
-
Manually annotated by BRENDA team
ATCC21367
-
-
Manually annotated by BRENDA team
Bacillus licheniformis EGW039 / CGMCC 0635
-
-
-
Manually annotated by BRENDA team
gene gls
-
-
Manually annotated by BRENDA team
isolated from pig intestine
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
Flavobacterium dormitator
var. glucanolyticae FA-5
-
-
Manually annotated by BRENDA team
Cytophaga
-
-
Manually annotated by BRENDA team
barley
-
-
Manually annotated by BRENDA team
Polyporus tulipiferae
-
-
Manually annotated by BRENDA team
shiitake mushroom
-
-
Manually annotated by BRENDA team
bifunctional CMCase and chitosanase, reactions of EC 3.2.1.4 and EC 3.2.16, respectively
UniProt
Manually annotated by BRENDA team
bifunctional CMCase and chitosanase, reactions of EC 3.2.1.4 and EC 3.2.16, respectively
UniProt
Manually annotated by BRENDA team
clone HB 2-4, gene bglc8H or lic8H
UniProt
Manually annotated by BRENDA team
adult, female
-
-
Manually annotated by BRENDA team
CBS 6938
-
-
Manually annotated by BRENDA team
CBS 6938
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene Teegl5A
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
DSM 1330
-
-
Manually annotated by BRENDA team
Saccharomyces lactis
-
-
-
Manually annotated by BRENDA team
rye
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,3-1,4-beta-D-glucan + H2O
?
show the reaction diagram
-
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
-
-
?
1,3-1,4-beta-D-glucan + H2O
cellooligosaccharide
show the reaction diagram
1,3-beta-oligosaccharide + H2O
?
show the reaction diagram
-
from DP3 to DP6
-
-
?
alpha-laminariheptaosyl fluoride
?
show the reaction diagram
-
-
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
-
?
amygdalin + H2O
?
show the reaction diagram
Saccharomyces lactis
-
slight activity
-
-
?
avicel + H2O
?
show the reaction diagram
barley beta-1,3-1,4-D-glucan + H2O
cellotriose
show the reaction diagram
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
beta-1,3-1,4-D-glucotriose + H2O
D-glucose + cellobiose
show the reaction diagram
-
-
-
?
beta-1,3-1,4-glucan + H2O
?
show the reaction diagram
beta-D-glucan
?
show the reaction diagram
source yeast cell wall
-
-
?
beta-D-glucan + H2O
?
show the reaction diagram
beta-D-glucans + H2O
?
show the reaction diagram
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 + ?
show the reaction diagram
-
-
main product, plus some tetrasaccharide. The enzyme acts on both beta-1,4-linkages of substrate
-
?
beta-glucan + H2O
?
show the reaction diagram
beta-glucan + H2O
laminaridextrins
show the reaction diagram
birchwood xylan + H2O
?
show the reaction diagram
-
-
-
?
carboxymethyl cellulose + H2O
?
show the reaction diagram
carboxymethyl-cellulose + H2O
?
show the reaction diagram
carboxymethylcellulose + H2O
?
show the reaction diagram
carboxymethylcellulose + H2O
cellobiose + cellotriose + glucose
show the reaction diagram
carboxymethylcellulose + H2O
D-glucose
show the reaction diagram
-
-
-
?
carboxymethylpachyman + H2O
?
show the reaction diagram
-
-
-
?
carboxymethylpachyman + H2O
D-glucose + carboxymethyl-(1-3,1-4)-beta-D-glucan
show the reaction diagram
carob bean gum + H2O
?
show the reaction diagram
-
-
-
?
cellobiose + H2O
D-glucose
show the reaction diagram
-
-
-
?
cellodextrin + H2O
cellobiose + cellotriose + higher oligosaccharides
show the reaction diagram
-
-
-
?
cellohexaose + H2O
?
show the reaction diagram
-
-
-
?
cellopentaose + H2O
?
show the reaction diagram
-
-
-
?
cellopentaose + H2O
cellobiose + cellotriose
show the reaction diagram
cellotetraose + H2O
?
show the reaction diagram
-
-
-
?
cellulose + H2O
?
show the reaction diagram
bacterial crystalline cellulose
-
-
?
cellulose + H2O +
?
show the reaction diagram
-
80% of the activity with laminarin
-
-
?
chitin + H2O
?
show the reaction diagram
-
-
-
?
chitosan + H2O
?
show the reaction diagram
CM-curdlan + H2O
?
show the reaction diagram
-
80.7% of the activity with CM-curdlan
-
-
?
curdlan + H2O
?
show the reaction diagram
curdlan + H2O
laminaribiose + laminaritriose + ?
show the reaction diagram
-
main products
-
?
curdlan + H2O
laminaripentaose
show the reaction diagram
curdlan + H2O +
?
show the reaction diagram
-
54.6% of the activity with laminarin
-
-
?
gentiotriose + H2O
?
show the reaction diagram
Saccharomyces lactis
-
slight activity
-
-
?
Glc-beta(1,4)-Glc-beta(1,3)-Glc-methylumbelliferyl + H2O
methylumbelliferone + Glc-beta(1,4)-Glc-beta(1,3)-Glc
show the reaction diagram
-
-
-
-
?
konjac glucomannan + H2O
?
show the reaction diagram
40% of the activity with barley beta-1,3-1,4-D-glucan
-
-
?
laminaran + H2O
?
show the reaction diagram
laminaribiose + H2O
2 D-glucose
show the reaction diagram
-
39% of the activity with laminarin
-
-
?
laminaribiose + H2O
D-glucose
show the reaction diagram
laminariheptaose + H2O
?
show the reaction diagram
-
-
-
-
?
laminarihexaose + H2O
D-glucose + laminaribiose + laminaritriose
show the reaction diagram
-
-
-
?
laminarin + H2O
6-O-glucosyl-laminaritriose + ?
show the reaction diagram
6-O-glucosyl-laminaritriose is produced as one of the major products
-
-
?
laminarin + H2O
?
show the reaction diagram
laminarin + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
show the reaction diagram
laminarin + H2O
D-glucose + laminarioligosaccharides
show the reaction diagram
laminarin + H2O
D-glucose + laminaripentaose
show the reaction diagram
-
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
laminaribiose + D-glucose
show the reaction diagram
-
-
-
-
?
laminarin + H2O
laminaritriose
show the reaction diagram
from Laminaria digitata
-
-
?
laminaripentaose + H2O
D-glucose + laminaribiose + laminaritriose
show the reaction diagram
-
-
-
?
laminaritetraose + 2 H2O
laminaribiose + 2 D-glucose
show the reaction diagram
laminaritetraose + H2O
2 laminaribiose
show the reaction diagram
-
-
-
?
laminaritetraose + H2O
?
show the reaction diagram
-
-
-
-
?
laminaritetraose + H2O
D-glucose + laminaribiose + laminaritriose
show the reaction diagram
laminaritriose + H2O
?
show the reaction diagram
laminaritriose + H2O
D-glucose + laminaribiose
show the reaction diagram
laminaritriose + H2O
laminaribiose + D-glucose
show the reaction diagram
-
-
-
-
?
lichenan + H2O
4-O-glucosyl-laminaribiose + ?
show the reaction diagram
4-O-glucosyl-laminaribiose is produced as one of the major products
-
-
?
lichenan + H2O
?
show the reaction diagram
lichenan + H2O
beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-4)-D-glucopyranose + ?
show the reaction diagram
-
-
-
-
?
lichenan + H2O
beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->3)-beta-D-glucopyranose + ?
show the reaction diagram
-
from Cetraria islandica. HdLam33 produces no cellotriose, cellobiose, and glucose from lichenan, but produced the trisaccharide cellobiosyl-beta-1,3-glucose
-
-
?
lichenan + H2O
cellooligosaccharide
show the reaction diagram
lichenin + H2O
3-beta-glycosyl-cellobiose + lichenin oligomers
show the reaction diagram
lichenin + H2O
?
show the reaction diagram
-
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
cellotetraose + cellopentaose + glucose
show the reaction diagram
-
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
show the reaction diagram
-
-
-
?
p-nitrophenyl-beta-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
show the reaction diagram
Saccharomyces lactis
-
slight activity
-
?
pachyman + H2O
?
show the reaction diagram
pachyman + H2O
laminarisaccharides
show the reaction diagram
periodate-oxidized laminarin + H2O
?
show the reaction diagram
-
-
-
?
polysaccharides + H2O
oligosaccharides
show the reaction diagram
-
role in maintenance of channels for communication and translocation through cell walls
-
?
pustulan + H2O
?
show the reaction diagram
zymosan A + H2O
?
show the reaction diagram
from Saccharomyces cerevisiae
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-D-glucans + H2O
?
show the reaction diagram
beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
laminarin + H2O
laminaribiose + D-glucose
show the reaction diagram
-
-
-
-
?
laminaritetraose + 2 H2O
laminaribiose + 2 D-glucose
show the reaction diagram
-
-
-
-
?
polysaccharides + H2O
oligosaccharides
show the reaction diagram
-
role in maintenance of channels for communication and translocation through cell walls
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe3+
1 mM, 116% of initial activity
Mg2+
1 mM, 113% of initial activity
Na2SeO3
9% activation at 10 mM
NaCl
12.5% activation at 10 mM
Ni2+
Flavobacterium dormitator
-
1.5fold activity in the presence of 10 mM NiSO4
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-Hydroxy-5-nitrobenzylbromide
5 mM, 47% inhibition
2-mercaptoethanol
carbodiimide
-
-
D-glucono-delta-lactone
-
-
D-glucose
-
75% loss of activity by 2 mM
dithiothreitol
10 mM, 77% residual activity
epoxyalkyl-beta-glycosides
-
iodoacetic acid
5 mM, 34% inhibition
KMnO4
-
56% loss of activity by 0.5 mM, complete inactivation by 2 mM
N-bromosuccinimide
Na2MoO4
20% inhibition at 10 mM
Pd2+
1 mM, 23% inhibition
Phenylmercuric nitrate
-
loss of 93% of activity after preincubation of enzyme for with 5 mg/ml for 30 min
Urea
10 mM, 85% residual activity
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
arginine
8% activation at 10 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
9.09
D-glucose
-
-
0.011 - 1.763
Glc-beta(1,4)-Glc-beta(1,3)-Glc-methylumbelliferyl
2.73
Laminarihexaose
pH 4.0, 50°C
0.21
Laminarin
-
-
2.39
Laminaripentaose
pH 4.0, 50°C
1.21
laminaritetraose
pH 4.0, 50°C
0.19
oxidized laminarin
-
-
-
0.004
short-chain pachyman
-
-
-
additional information
Barley beta-glucan
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
114.8 - 281.2
1,3-1,4-beta-D-glucan
-
269
Barley beta-glucan
-
pH 5.0, 50°C
7207
beta-1,3-1,4-glucan
pH 6.4, 40°C, purified recombinant His-tagged enzyme, substrate from Hordeum vulgare
26.7 - 15600
beta-Glucan
142.6 - 632.8
carboxymethylcellulose
-
0.000017 - 0.383
Glc-beta(1,4)-Glc-beta(1,3)-Glc-methylumbelliferyl
582
Laminarihexaose
pH 4.0, 50°C
23.1 - 750
Laminarin
355
Laminaripentaose
pH 4.0, 50°C
0.21 - 188
laminaritetraose
0.047 - 1350
lichenan
1050
lichenin
-
pH 6, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
Barley beta-glucan
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0005
-
purified enzyme, periodate-oxidized laminarin as substrate
0.013
Saccharomyces lactis
-
laminarin as substrate
0.03
-
laminarin as substrate
0.12
-
laminarin as substrate
0.13
-
laminarin as substrate
0.16
Flavobacterium dormitator
-
laminarin as substrate
0.17
-
homogenate
0.23
-
carboxymethylcellulose as substrate
0.46
Flavobacterium dormitator
-
yeast glucan as substrate
1.32
-
DEAE anion exchange chromatography
1.38
Flavobacterium dormitator
-
pachyman as substrate
2.22
purified native enzyme, pH 5.0, 50°C
2.8
substrate carboxymethylcellulose, pH 5.0, 50°C
2.83
-
laminarin as substrate
5.3
-
substrate curdlan, pH 5.0, 50°C
6.2
substrate barley beta-1,3-1,4-D-glucan, pH 5.0, 50°C
6.37
-
HIC chromatography
15
-
substrate laminarin, pH 5.0, 50°C
18
Flavobacterium dormitator
-
purified beta-1,3 glucanase II from periplasmic fraction of Escherichia coli clone cells
18.31
-
gel filtration chromatography
24.4
-
laminarin as substrate
25
Flavobacterium dormitator
-
purified enzyme, laminarin as substrate
35.5
substrate laminarin, pH 6.0, 37°C
37.85
purified recombinant enzyme, pH 8.0, 60°C
39.8
substrate periodate-oxidized laminarin, pH 6.0, 37°C
54
-
substrate beta-glucan, pH 5.0, 50°C
56
-
substrate lichenan, pH 5.0, 50°C
58
-
substrate laminarin, pH 6.0, 60°C
66
-
short-chain pachyman as substrate
68
-
purified native enzyme
72.1
substrate carboxymethylpachyman, pH 6.0, 37°C
118.8
substrate barley beta-glucan, pH 6.0, 37°C
303.5
-
lichenin as substrate
338.3
-
barley beta-glucan as substrate
350
-
purified enzyme
379.1
purified recombinant His-tagged enzyme, substrate lichenan
693
substrate barley beta-glucan, pH 5.5, 556°C
728.8
purified recombinant His-tagged enzyme, substrate beta-glucan from Hordeum vulgare
1652
-
substrate lichenan, pH 5.0, 50°C
1963
-
substrate barley beta-glucan, pH 5.0, 50°C
2961
substrate barley beta-glucan, pH 6.5, 75°C
6900
-
purified enzyme, beta-glucan as substrate
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5
recombinant enzyme
5.6
-
recombinant enzyme
6 - 6.5
Flavobacterium dormitator
-
pH 6.0 with yeast glucan, pH 6.5 with laminarin as substrate
6.4
recombinant enzyme
8
recombinant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2.5 - 7.4
-
more than 50% of maximum activity
3.8 - 6
-
more than 50% of maximum activity within
4.5 - 8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 55
90
recombinant enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 65
inactivation above 70°C, profile, overview
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
40 - 60
-
40°C: 34% of maximal activity, 60°C: maximal activity
45 - 70
-
more than 50% of maximum activity within
60
rapid loss of activity above
70
20% of maximum activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.4
-
isoelectric focusing
5.55
sequence calculation
5.78
sequence calculation
7.61
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
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
Manually annotated by BRENDA team
-
aleurone and scutellar epithelium
Manually annotated by BRENDA team
-
LIC 1 is secreted by the salivary glands
Manually annotated by BRENDA team
-
germinated
Manually annotated by BRENDA team
PDB
SCOP
CATH
UNIPROT
ORGANISM
Phanerochaete chrysosporium;
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16600
-
gel filtration
21000
-
SDS-PAGE, gel filtration
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
25000
-
x * 25000, 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
27000
Flavobacterium dormitator
-
SDS-PAGE
28000
-
x * 28000, recombinant enzyme, SDS-PAGE
29000
-
SDS-PAGE
31900 - 33000
Flavobacterium dormitator
-
gel filtration, SDS-PAGE, ultracentrifugation
33000
-
x * 33000, SDS-PAGE
34000
x * 34000, SDS-PAGE
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
38200
calculated molecular mass of expressed C of LamA
39700
-
x * 39700, SDS-PAGE
40000
x * 41561, sequence calculation, x * 40000, SDS-PAGE
40700
-
gel filtration
41000
-
SDS-PAGE, a second band of 62000 Da is detected
41561
x * 41561, sequence calculation, x * 40000, SDS-PAGE
51600
calculated molecular mass of expressed CF of LamA
60000
x * 60000, SDS-PAGE, x * 60700, calculated
60700
x * 60000, SDS-PAGE, x * 60700, calculated
62000
-
gel filtration chromatography; 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
73000
-
SDS-PAGE
77000
calculated molecular mass of expressed SC of LamA
80000
-
gel filtration
92000
calculated molecular mass of expressed CB3 of LamA
99000
-
x * 99000, SDS-PAGE
144600
calculated molecular mass of expressed CBF of LamA
160000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
proteolytic modification
Flavobacterium dormitator
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beta-1,3-glucanase I is formed by proteolysis of beta-1,3-glucanase II
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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crystal structure of truncated Fsbeta-glucanase in complex with beta-1,3-1,4-cellotriose, resolution of 2.3 A
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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
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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
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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
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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
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
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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
2.4 - 8.7
40°C, 30 min, about 50% residual activity
737515
3
12 h, enzyme retains 80% of its original activity
677749
3 - 5
-
at pH 5 69%, at pH 4 23%, at pH 3 2% of maximal activity
136723
3 - 9
-
4°C, 48 h stable with 5-20% loss of activity
136700
3.8 - 11.2
1 h, more than 60% residual activity
713878
4 - 6
stable
677749
4 - 10
4 - 8
-
stable in the range
655725
4.2 - 8
-
60 min, 50°C, stable
738549
5 - 8.5
-
-
136701
5.5 - 8
-
-
693404
5.5 - 9
-
746378
8
12 h, enzyme retains 80% of its original activity
677749
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 60
-
at 20°C 8% loss of activity, loss of 80% of activity after heating at 60°C for 3 min
30 - 75
30 min, pH 7.5, 20 mM Tris-HCl, 35-45% residual activtiy
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
42
-
50% inactivation
50 - 70
50 - 60
-
stable for 20 min at 50°C, at 60°C loss of 75% of maximal activity
71
-
Tm-value for wild-type enzyme is 71.4°C
90