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
strain EGW039
-
-
Manually annotated by BRENDA team
strain BF7658, gene gls
-
-
Manually annotated by BRENDA team
strain MA139, isolated from pig intestine
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain Clark 1936
-
-
Manually annotated by BRENDA team
strain Clark 1936
-
-
Manually annotated by BRENDA team
Clostridium stercorarium
-
-
-
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
strain CCRC 17245
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
strain CBS 814.70, two endo-beta-D-glucanases EG VI and EG VII
-
-
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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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
-
-
?
barley beta-glucan + H2O
?
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-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
cellobiose + cellotriose + glucose
show the reaction diagram
carboxymethylcellulose + H2O
D-glucose
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
-
-
-
?
cellotetraose + H2O
?
show the reaction diagram
-
-
-
?
cellulose + H2O
?
show the reaction diagram
bacterial crystalline cellulose
-
-
?
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
laminaripentaose
show the reaction diagram
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
-
-
-
-
?
laminaran + H2O
?
show the reaction diagram
laminaribiose + H2O
D-glucose
show the reaction diagram
laminariheptaose + H2O
?
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 + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
show the reaction diagram
laminarin + H2O
D-glucose + laminarioligosaccharides
show the reaction diagram
laminarin + H2O
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
-
-
?
laminaritetraose + 2 H2O
laminaribiose + 2 D-glucose
show the reaction diagram
laminaritetraose + H2O
?
show the reaction diagram
-
-
-
-
?
laminaritriose + H2O
?
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 + higher 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
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
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
the enzyme activity is not affected by Mg2+, Ca2+, KI, and sucrose at 10 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
75% loss of activity by 1%
Ca2+
slightly activating, 142% activity at 15 mM, slightly inhibitory at 25 mM with 86% of maximal activity
carbodiimide
-
-
D-glucono-delta-lactone
-
-
D-glucose
-
75% loss of activity by 2 mM
epoxyalkyl-beta-glycosides
KMnO4
-
56% loss of activity by 0.5 mM, complete inactivation by 2 mM
N-bromosuccinimide
-
81% loss of activity by 0.5 mM, complete inactivation by 2 mM
Na2MoO4
20% inhibition at 10 mM
Phenylmercuric nitrate
-
loss of 93% of activity after preincubation of enzyme for with 5 mg/ml for 30 min
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
0.21
Laminarin
-
-
0.19
oxidized laminarin
-
-
-
0.004
short-chain pachyman
-
-
-
additional information
Laminarin
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
114.8 - 281.2
1,3-1,4-beta-D-glucan
7207
beta-1,3-1,4-glucan
Bacillus subtilis
A8CGP1
pH 6.4, 40C, 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
23.1 - 750
Laminarin
0.21
laminaritetraose
Aplysia kurodai
-
pH 6.0, 30C
0.047 - 1350
lichenan
1050
lichenin
Periplaneta americana
-
pH 6, 30C
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, 50C
2.83
-
laminarin as substrate
6.37
-
HIC chromatography
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
37.85
purified recombinant enzyme, pH 8.0, 60C
66
-
short-chain pachyman as substrate
68
-
purified native enzyme
172
-
purified enzyme
303.5
-
lichenin as substrate
338.3
-
barley beta-glucan as substrate
350
-
purified enzyme
379.1
purified recombinant His-tagged enzyme, substrate lichenan
728.8
purified recombinant His-tagged enzyme, substrate beta-glucan from Hordeum vulgare
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
6.5
-
in 50 mM sodium phosphate buffer
8
recombinant enzyme
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 70C, profile, overview
30 - 70
-
30C: about 90% of maximal activity, 70C: about 50% of maximal activity
30 - 80
-
90% of maximal activity at 30C, 40% of maximal activity at 80C
40 - 60
-
40C: 34% of maximal activity, 60C: maximal activity
60
rapid loss of activity above
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
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
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16600
-
gel filtration
21000
-
SDS-PAGE, gel filtration
22000
-
gel filtration
27000
Flavobacterium dormitator
-
SDS-PAGE
29000
-
SDS-PAGE
31900 - 33000
Flavobacterium dormitator
-
gel filtration, SDS-PAGE, ultracentrifugation
38200
calculated molecular mass of expressed C of LamA
41000
-
SDS-PAGE, a second band of 62000 Da is detected
51600
calculated molecular mass of expressed CF of LamA
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
92000
calculated molecular mass of expressed CB3 of LamA
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
-
beta-1,3-glucanase I is formed by proteolysis of beta-1,3-glucanase II
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
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
-
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, 37C for 1 h
729084
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
-
4C, 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
purified recombinant His-tagged enzyme, 40C, 1 h, stable
707190
4 - 8
-
stable in the range
655725
5 - 8.5
-
-
136701
5.5 - 8
-
-
693404
8
12 h, enzyme retains 80% of its original activity
677749
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 60
-
at 20C 8% loss of activity, loss of 80% of activity after heating at 60C for 3 min
30 - 60
-
stable at 30C, 25% of original activity lost after incubation at 40C for 1 h, complete denaturation within 10 min at 60C
37
-
with barley beta-glucan as substrate, 26% of activity after 30 min, no activity after 180 min
40
purified recombinant His-tagged enzyme, 80% remaining activity after 2 h
42
-
50% inactivation
50 - 70
50
-
purified native enzyme, 15 min, loss of 50% activity
50 - 60
-
stable for 20 min at 50C, at 60C loss of 75% of maximal activity
71
-
Tm-value for wild-type enzyme is 71.4C
75
-
Tm-value for mutant enzyme N207D is 75.3C
95 - 100
-
incubation at 100C: 82% of initial activity at 95C, 57% at 100C
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
30% of activity at 1% SDS w/v after 20 min incubation
-
about 66% of activity lost after dialysis against distilled water at 2C for 18 h
-
calcium ion has a general stabilizing effect on Bacillus beta-1,3-1,4 glucanases
complete inactivation by 1% SDS
-
LIC 1 is stable in the presence of Periplaneta americana proteinases
-
resistant against proteolysis by trypsin and chymotrypsin, slow digestion by protease V8, complete digestion by thermolysin
-
stabilization of activity at 37C 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
-
unaffected by pepsin, pancreatin and bile extract
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ethanol
-
40% of activity after 20 min incubation with 10% v/v ethanol
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, cell paste, without appreciable loss of activity
Saccharomyces lactis
-
0C, 7 days, no detectable loss of activity
-
4C, 0.1 M McIlvaine buffer, pH 5.8, retains almost all initial activity after 1 week of storage
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity chromatography
-
beta-1,3-glucanase II from periplasmic fraction of Escherichia coli clone cells
Flavobacterium dormitator
-
EG VI and EG VII
-
from midgut and salivary gland
-
from recombinant Escherichia coli cells
-
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
-
partial
Saccharomyces lactis
-
precipitation, a combination of anion exchange, hydrophobic interaction and gel filtration chromatography, all chromatography is carried out at 4C
-
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 LamR, from transformed Escherichia coli cells
-
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 BL21 (DE3)
-
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
Clostridium stercorarium
-
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
HdLam33, DNA and amino acid sequence determination and analysis
-
placing of gene eng2+ under the control of a repressible promoter
-
recombinantly expressed in Pichia pastoris
-
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
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N207D
-
increase in Tm-value to 75.3C, compared to wild-type Tm-value of 71.4C
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
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
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
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
analysis
-
use in structural analysis of polysaccharides
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
drug development
food industry
nutrition
synthesis
additional information
Show AA Sequence (131 entries)
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