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
3.2.1.6
-
RECOMMENDED NAME
GeneOntology No.
endo-1,3(4)-beta-glucanase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
-
-
-
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 is not in rapid equilibrium
-
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
substrates include laminarin, lichenin, and cereal D-glucans, different from EC 3.2.1.52 beta-L-N-acetylhexosaminidase
-
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
substrates include laminarin, lichenin, and cereal D-glucans, different from EC 3.2.1.52 beta-L-N-acetylhexosaminidase
Talaromyces emersonii CBS 814.70
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1,3-(4)-beta-glucanase (endoglucanase)
-
-
1,3-1,4-beta-glucanase EII (barley)
-
-
1,3-beta-D-glucanases
-
-
Agl9A
D7PC10
-
Agl9A
D7PC10
-
-
AkLam36
-
-
beta-1,3-1,4-glucanase
-
-
beta-1,3-1,4-glucanase
Q8GMY0
-
beta-1,3-1,4-glucanase
Bacillus licheniformis EGW039
-
-
-
beta-1,3-1,4-glucanase
-
-
beta-1,3-1,4-glucanase
A8CGP1
-
beta-1,3-1,4-glucanase
Bacillus subtilis MA139
A8CGP1
-
-
beta-1,3-1,4-glucanase
Q55365
-
beta-1,3-1,4-glucanase
-
-
beta-1,3-1,4-glucanase
Talaromyces emersonii CBS 814.70
-
-
-
beta-1,3-glucanase
-
-
beta-1,3-glucanase
-
-
beta-1,3:1,4 glucanase
-
-
beta-glucanase
Saccharomyces lactis
-
-
beta-glucanase
-
-
bglBC1
Bacillus circulans ATCC21367
-
-
-
enda-beta-(1-3),(1-4)-glucanase
-
-
enda-beta-(1-3),(1-4)-glucanase
Bacillus circulans ATCC21367
-
-
-
endo beta-1,3-glucanase IV
Flavobacterium dormitator
-
-
endo-1,3(4)-beta-D-glucanase
Flavobacterium dormitator
-
-
endo-1,3(4)-beta-glucanase
Q874E3
-
endo-1,3(4)-beta-glucanase
-
-
endo-1,3-1,4-beta-D-glucanase
-
-
endo-1,3-1,4-beta-D-glucanase
Talaromyces emersonii CBS 814.70
-
-
-
endo-1,3-beta-D-glucanase
-
-
endo-1,3-beta-D-glucanase
Talaromyces emersonii CBS 814.70
-
-
-
endo-1,3-beta-glucanase
-
-
endo-1,3-beta-glucanase
Cherax destructor Clark
-
-
-
endo-1,3-beta-glucanase
-
-
endo-1,3-beta-glucanase
-
-
endo-1,3-beta-glucanase
Q000P7
-
endo-1,3-beta-glucanase
Q000P7
-
-
endo-1,3-beta-glucanase
-
-
endo-beta-(1-3)-D-glucanase
-
-
endo-beta-(1-3)-D-glucanase
-
-
endo-beta-1,3(4)-glucanase
-
-
endo-beta-1,3(4)-glucanase
Phaffia rhodozyma CBS 6938
-
-
-
endo-beta-1,3-1,4-D-glucanase
-
-
endo-beta-1,3-1,4-glucanase
-
-
endo-beta-1,3-1,4-glucanase
Bacillus subtilis BF7658
-
-
-
endo-beta-1,3-glucanase
Flavobacterium dormitator
-
-
endo-beta-1,3-glucanase
-
-
endo-beta-1,3-glucanase
-
-
Fsbeta-glucanase
-
-
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
LamA
Q000P7
-
lamarinase
-
-
lamarinase
Cherax destructor Clark
-
-
-
laminaranase
-
-
laminaranase
Talaromyces emersonii CBS 814.70
-
-
-
laminarinase
-
-
laminarinase
-
-
laminarinase
-
-
laminarinase
-
-
laminarinase
Q000P7
-
laminarinase
Q000P7
-
-
laminarinase
-
-
laminarinase 16A
Q874E3
-
laminarinase II
-
-
laminarinase Lam16A
-
-
nonlytic endo-beta-1,3-glucanase I
Flavobacterium dormitator
-
-
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
A8CGP1
the bacterial beta-1,3-1,4-glucanase belongs to the glycosyl hydrolase family 16, GH16, possessing the conserved EIDIEF motif
additional information
Bacillus subtilis MA139
A8CGP1
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
-
LamR belongs to glycosyl hydrolase family 16
additional information
-
the enzyme belongs to the glycosyl hydrolase family 81, GH81
CAS REGISTRY NUMBER
COMMENTARY
62213-14-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
-
D7PC10
UniProt
Manually annotated by BRENDA team
-
D7PC10
UniProt
Manually annotated by BRENDA team
ATCC21367
-
-
Manually annotated by BRENDA team
Bacillus circulans ATCC21367
ATCC21367
-
-
Manually annotated by BRENDA team
strain EGW039
-
-
Manually annotated by BRENDA team
Bacillus licheniformis EGW039
strain EGW039
-
-
Manually annotated by BRENDA team
mutant strain ZJF-1A5
-
-
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
Bacillus subtilis BF7658
strain BF7658, gene gls
-
-
Manually annotated by BRENDA team
Bacillus subtilis MA139
strain MA139, isolated from pig intestine
UniProt
Manually annotated by BRENDA team
strain Clark 1936
-
-
Manually annotated by BRENDA team
Cherax destructor Clark
strain Clark 1936
-
-
Manually annotated by BRENDA team
Flavobacterium dormitator
var. glucanolyticae FA-5
-
-
Manually annotated by BRENDA team
Cytophaga
-
-
Manually annotated by BRENDA team
Polyporus tulipiferae
-
-
Manually annotated by BRENDA team
shiitake mushroom
-
-
Manually annotated by BRENDA team
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
-
-
Manually annotated by BRENDA team
strain CCRC 17245
UniProt
Manually annotated by BRENDA team
strain CCRC 17245
UniProt
Manually annotated by BRENDA team
adult, female
-
-
Manually annotated by BRENDA team
CBS 6938
-
-
Manually annotated by BRENDA team
Phaffia rhodozyma CBS 6938
CBS 6938
-
-
Manually annotated by BRENDA team
DSM 1330
-
-
Manually annotated by BRENDA team
member of glycosyl hydrolase family 16
UniProt
Manually annotated by BRENDA team
Saccharomyces lactis
-
-
-
Manually annotated by BRENDA team
several strains, overview
-
-
Manually annotated by BRENDA team
Streptococcus bovis JB1
-
-
-
Manually annotated by BRENDA team
strain CBS 814.70, two endo-beta-D-glucanases EG VI and EG VII
-
-
Manually annotated by BRENDA team
Talaromyces emersonii CBS 814.70
strain CBS 814.70, two endo-beta-D-glucanases EG VI and EG VII
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
D7PC10
enzyme is highly resistant to trypsin, alpha-chymotrypsin, collagenase and Neutrase 0.8L
metabolism
-
enzyme is highly resistant to trypsin, alpha-chymotrypsin, collagenase and Neutrase 0.8L
-
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
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
Talaromyces emersonii, Talaromyces emersonii CBS 814.70
-
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-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
Q59328
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
Q000P7
-
-
-
?
beta-1,3-1,4-glucan + H2O
?
show the reaction diagram
-
from Hordeum vulgare
-
-
?
beta-1,3-1,4-glucan + H2O
?
show the reaction diagram
A8CGP1, -
from Hordeum vulgare, preferred substrate
-
-
?
beta-1,3-1,4-glucan + H2O
?
show the reaction diagram
Bacillus subtilis MA139
A8CGP1
from Hordeum vulgare, preferred substrate
-
-
?
beta-D-glucan
?
show the reaction diagram
Q59328
source yeast cell wall
-
-
?
beta-D-glucan + H2O
?
show the reaction diagram
D7PC10
source of substrate: barley
-
-
?
beta-D-glucans + H2O
?
show the reaction diagram
-
-
-
-
?
beta-D-glucans + H2O
?
show the reaction diagram
Streptococcus bovis JB1
-
-
-
-
?
beta-D-glucans + H2O
?
show the reaction diagram
Saccharomyces lactis
-
role in budding process and cell wall growth
-
-
?
beta-D-glucans + H2O
?
show the reaction diagram
-
in vivo probably facilitation of solubilisation of cell wall glucan
-
-
?
beta-D-glucans + H2O
?
show the reaction diagram
-
enzyme involved in cell wall metabolism
-
-
?
beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
beta-glucan + H2O
?
show the reaction diagram
-, Q8GMY0
-
-
-
?
beta-glucan + H2O
?
show the reaction diagram
-
barley beta-glucan
-
-
?
beta-glucan + H2O
?
show the reaction diagram
-
barley beta-glucan
-
-
?
beta-glucan + H2O
?
show the reaction diagram
Q55365, -
the enzyme hydrolyses the beta-1,4-glycosidic linkage of barley beta-glucan through an inverting mechanism
-
-
?
beta-glucan + H2O
?
show the reaction diagram
Bacillus circulans ATCC21367
-
-
-
-
?
beta-glucan + H2O
?
show the reaction diagram
Bacillus licheniformis EGW039
-
barley beta-glucan
-
-
?
beta-glucan + H2O
laminaridextrins
show the reaction diagram
-
-
-
?
beta-glucan + H2O
laminaridextrins
show the reaction diagram
-
-
-
?
beta-glucan + H2O
laminaridextrins
show the reaction diagram
-
-
D-glucose + cellobiose
?
beta-glucan + H2O
laminaridextrins
show the reaction diagram
Flavobacterium dormitator
-
yeast glucan
-
?
beta-glucan + H2O
laminaridextrins
show the reaction diagram
Flavobacterium dormitator
-
yeast glucan
-
-
?
beta-glucan + H2O
laminaridextrins
show the reaction diagram
-
1-4)-beta-glucan
-
?
beta-glucan + H2O
laminaridextrins
show the reaction diagram
-
yeast cell-wall 1,3-beta-glucan
-
-
-
beta-glucan + H2O
laminaridextrins
show the reaction diagram
-
beta-(1-3)-beta-(1-4)mixed-linked, from barley
-
-
beta-glucan + H2O
laminaridextrins
show the reaction diagram
-
beta-(1-3)-beta-(1-4)mixed-linked, from barley
-
?
beta-glucan + H2O
laminaridextrins
show the reaction diagram
Streptococcus bovis JB1
-
beta-(1-3)-beta-(1-4)mixed-linked, from barley
-
?
beta-glucan + H2O
laminaridextrins
show the reaction diagram
Phaffia rhodozyma CBS 6938
-
-
-
?
carboxymethyl-cellulose + H2O
?
show the reaction diagram
D7PC10
15% of the activity with beta-D-glucan
-
-
?
carboxymethylcellulose + H2O
D-glucose
show the reaction diagram
-
-
-
?
carboxymethylcellulose + H2O
cellobiose + cellotriose + glucose
show the reaction diagram
Talaromyces emersonii, Talaromyces emersonii CBS 814.70
-
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
show the reaction diagram
-
-
-
?
carboxymethylpachyman + H2O
D-glucose + carboxymethyl-(1-3,1-4)-beta-D-glucan
show the reaction diagram
-
-
-
?
carboxymethylpachyman + H2O
D-glucose + carboxymethyl-(1-3,1-4)-beta-D-glucan
show the reaction diagram
-
-
-
?
cellobiose + H2O
D-glucose
show the reaction diagram
-
-
-
?
cellodextrin + H2O
cellobiose + cellotriose + higher oligosaccharides
show the reaction diagram
-
-
-
?
cellulose + H2O
?
show the reaction diagram
Q59328
bacterial crystalline cellulose
-
-
?
chitin + H2O
?
show the reaction diagram
Q59328
-
-
-
?
chitosan + H2O
?
show the reaction diagram
Q59328
-
-
-
?
CM-curdlan + H2O
?
show the reaction diagram
-
80.7% of the activity with CM-curdlan
-
-
?
curdlan + H2O
?
show the reaction diagram
Q000P7
from Alcaligenes faecalis
-
-
?
curdlan + H2O
?
show the reaction diagram
-
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
-
-
?
curdlan + H2O
laminaripentaose
show the reaction diagram
Flavobacterium dormitator
-
-
-
-
-
curdlan + H2O
laminaripentaose
show the reaction diagram
Flavobacterium dormitator
-
paramylon
main product
?
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
Talaromyces emersonii, Talaromyces emersonii CBS 814.70
-
from Laminaria digitata, 1,3-beta-glucan
-
-
?
laminaribiose + H2O
D-glucose
show the reaction diagram
-
-
-
?
laminaribiose + H2O
D-glucose
show the reaction diagram
Saccharomyces lactis
-
-
-
?
laminaribiose + H2O
D-glucose
show the reaction diagram
-
0.03% of the rate of laminarin
-
?
laminariheptaose + H2O
?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
show the reaction diagram
-
-
-
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
show the reaction diagram
-
-
-
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
show the reaction diagram
-
-
-
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
show the reaction diagram
-
-
-
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
show the reaction diagram
-
-
laminaritriose
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
show the reaction diagram
-
-
laminaridextrins + D-glucose
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
show the reaction diagram
-
-
laminaridextrins + D-glucose
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
show the reaction diagram
-
-
laminaridextrins + D-glucose
-
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
show the reaction diagram
-
-
laminaridextrins + D-glucose
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
show the reaction diagram
Saccharomyces lactis
-
-
laminaridextrins + D-glucose
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
show the reaction diagram
-
-
laminaridextrins + D-glucose
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
show the reaction diagram
-
-
reducing sugars
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
show the reaction diagram
-
-
reducing sugars
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
show the reaction diagram
Streptococcus bovis JB1
-
-
reducing sugars
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
show the reaction diagram
Flavobacterium dormitator
-
-
main product laminaripentaose
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
show the reaction diagram
-
-
D-glucose + laminaribiose
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
show the reaction diagram
Flavobacterium dormitator
-
-
D-glucose + laminaribiose, laminaritriose + D-glucose
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose + laminaritetraose + laminaripentaose + laminarihexaose
show the reaction diagram
-
-
70-90% D-glucose, small amounts of laminaribiose and D-glucose oligomers of 3-4 D-glucose units
?
laminarin + H2O
?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
Flavobacterium dormitator
-
use as carbon source
-
-
?
laminarin + H2O
?
show the reaction diagram
-
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
?
show the reaction diagram
-
33.2% of the activity with CM-curdlan
-
-
?
laminarin + H2O
?
show the reaction diagram
-
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, 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
?
show the reaction diagram
D7PC10
6.2% of the activity with beta-D-glucan
-
-
?
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
6-O-glucosyl-laminaritriose + ?
show the reaction diagram
Q874E3
6-O-glucosyl-laminaritriose is produced as one of the major products
-
-
?
laminarin + H2O
D-glucose + laminarioligosaccharides
show the reaction diagram
Cherax destructor, Cherax destructor Clark
-
-
-
-
?
laminarin + H2O
laminaritriose
show the reaction diagram
Q000P7
from Laminaria digitata
-
-
?
laminarin + H2O
laminaribiose + D-glucose
show the reaction diagram
-
-
-
-
?
laminaritetraose + 2 H2O
laminaribiose + 2 D-glucose
show the reaction diagram
-
-, 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
?
show the reaction diagram
-
-
-
-
?
laminaritriose + H2O
?
show the reaction diagram
Saccharomyces lactis
-
-
-
-
?
laminaritriose + H2O
?
show the reaction diagram
-
-
-
-
?
laminaritriose + H2O
laminaribiose + D-glucose
show the reaction diagram
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-, Q8GMY0
-
-
-
?
lichenan + H2O
?
show the reaction diagram
Q55365, -
-
-
-
?
lichenan + H2O
?
show the reaction diagram
Q874E3
-
-
-
?
lichenan + H2O
?
show the reaction diagram
Q000P7
-
-
-
?
lichenan + H2O
?
show the reaction diagram
A8CGP1, -
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
67.27% of the activity with CM-curdlan
-
-
?
lichenan + H2O
?
show the reaction diagram
D7PC10
109% of the activity with beta-D-glucan
-
-
?
lichenan + H2O
?
show the reaction diagram
Bacillus subtilis MA139
A8CGP1
-
-
-
?
lichenan + H2O
?
show the reaction diagram
Bacillus licheniformis EGW039
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
D7PC10
109% of the activity with beta-D-glucan
-
-
?
lichenan + H2O
cellooligosaccharide
show the reaction diagram
Talaromyces emersonii, Talaromyces emersonii CBS 814.70
-
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
beta-D-glucopyranosyl-(1-3)-beta-D-glucopyranosyl-(1-4)-D-glucopyranose + ?
show the reaction diagram
-
-
-
-
?
lichenan + H2O
4-O-glucosyl-laminaribiose + ?
show the reaction diagram
Q874E3
4-O-glucosyl-laminaribiose is produced as one of the major products
-
-
?
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
-
-
?
lichenin + H2O
3-beta-glycosyl-cellobiose + higher oligomers
show the reaction diagram
-
-
-
?
lichenin + H2O
3-beta-glycosyl-cellobiose + higher oligomers
show the reaction diagram
-
-
-
?
lichenin + H2O
3-beta-glycosyl-cellobiose + higher oligomers
show the reaction diagram
Streptococcus bovis JB1
-
-
-
?
lichenin + H2O
3-beta-glycosyl-cellobiose + higher oligomers
show the reaction diagram
-
-
laminaripentaose + D-glucose
?
lichenin + H2O
3-beta-glycosyl-cellobiose + higher oligomers
show the reaction diagram
-
-
laminaripentaose + D-glucose
?
lichenin + H2O
3-beta-glycosyl-cellobiose + higher oligomers
show the reaction diagram
Flavobacterium dormitator
-
-
laminaripentaose main product
?
lichenin + H2O
3-beta-glycosyl-cellobiose + higher oligomers
show the reaction diagram
Flavobacterium dormitator
-
weak activity of enzyme I
-
?
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
-
-
?
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
Q000P7
-
-
-
?
pachyman + H2O
laminarisaccharides
show the reaction diagram
-
-
-
?
pachyman + H2O
laminarisaccharides
show the reaction diagram
Flavobacterium dormitator
-
-
-
?
pachyman + H2O
laminarisaccharides
show the reaction diagram
-
more active on short-chain pachyman
-
?
pachyman + H2O
laminarisaccharides
show the reaction diagram
Flavobacterium dormitator
-
weak activity of enzyme I
-
-
-
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
Q59328
-
-
-
?
pustulan + H2O
?
show the reaction diagram
Saccharomyces lactis
-
slight activity
-
-
?
xylan + H2O
?
show the reaction diagram
Q59328
-
-
-
?
zymosan A + H2O
?
show the reaction diagram
Q000P7
from Saccharomyces cerevisiae
-
-
?
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
-
?
additional information
?
-
-
transglycosylase activity
-
-
?
additional information
?
-
Flavobacterium dormitator
-
transglycosylase activity
-
-
?
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, a group in LIC 1 with pK of 4.9 is necessary for substrate binding
-
-
-
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
?
-
-
one active site per enzyme molecule
-
-
-
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
?
-
Q55365, -
SsGlc functions in salt stress tolerance in Synechocystis PCC6803
-
-
-
additional information
?
-
-, Q8GMY0
no activity on cellulose
-
-
-
additional information
?
-
Q55365, -
no activity towards cellulose, curdlan or laminarin
-
-
-
additional information
?
-
Q874E3
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
?
-
-
laminarinase hydrolyses both beta-1,3-glycosidic bonds and beta-1,4-glycosidic bonds
-
-
-
additional information
?
-
Q000P7
no activity with carboxymethylcellulose and xylan of all truncated proteins of LamA
-
-
-
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
?
-
-
HdLam33 degrades laminarin and laminarioligosaccharides to laminaribiose and glucose
-
-
-
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, 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
?
-
Q59328
determination of binding constants and binding capacity for substrates tested, in presence and absence of Ca2+
-
-
-
additional information
?
-
Cherax destructor Clark
-
laminarinase hydrolyses both beta-1,3-glycosidic bonds and beta-1,4-glycosidic bonds
-
-
-
additional information
?
-
Talaromyces emersonii CBS 814.70
-
one active site per enzyme molecule
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-D-glucans + H2O
?
show the reaction diagram
-
-
-
-
?
beta-D-glucans + H2O
?
show the reaction diagram
Streptococcus bovis JB1
-
-
-
-
?
beta-D-glucans + H2O
?
show the reaction diagram
Saccharomyces lactis
-
role in budding process and cell wall growth
-
-
?
beta-D-glucans + H2O
?
show the reaction diagram
-
in vivo probably facilitation of solubilisation of cell wall glucan
-
-
?
beta-D-glucans + H2O
?
show the reaction diagram
-
enzyme involved in cell wall metabolism
-
-
?
beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
Flavobacterium dormitator
-
use as carbon source
-
-
?
laminarin + H2O
?
show the reaction diagram
-
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
laminaribiose + 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
-
?
laminaritetraose + 2 H2O
laminaribiose + 2 D-glucose
show the reaction diagram
-
-
-
-
?
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
?
-
Q55365, -
SsGlc functions in salt stress tolerance in Synechocystis PCC6803
-
-
-
additional information
?
-
-
HdLam33 degrades laminarin and laminarioligosaccharides to laminaribiose and glucose
-
-
-
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
32% increase of activity by 10 mM
Ca2+
O52754
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
Ca2+
Q59328
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+
Co2+
Q8GMY0
activates
Co2+
D7PC10
2 mM, 113% of initial activity
Fe2+
Q8GMY0
activates
Fe2+
A8CGP1
9% activation at 10 mM
Mn2+
Q8GMY0
activates
Na2SeO3
A8CGP1
9% activation at 10 mM
NaCl
A8CGP1
12.5% activation at 10 mM
Ni2+
Flavobacterium dormitator
-
1.5fold activity in the presence of 10 mM NiSO4
Mn2+
D7PC10
2 mM, 123% of initial activity
additional information
A8CGP1
the enzyme activity is not affected by Mg2+, Ca2+, KI, and sucrose at 10 mM
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
75% loss of activity by 1%
Ag+
Flavobacterium dormitator
-
72% inhibition of beta-1,3-glucanase activity after incubation with 1 mM at 5C, pH 6.0, for 3 h
Ag+
-
very little effect
Ag+
Flavobacterium dormitator
-
87% of activity with 10 mM
Ag+
D7PC10
2 mM, complete loss of activity
Cr3+
D7PC10
2 mM, 78% of initial activity
Cu2+
A8CGP1
97% inhibition at 10 mM
Cu2+
D7PC10
2 mM, 23% of initial activity
D-glucono-delta-lactone
-
-
D-glucose
-
75% loss of activity by 2 mM
EDTA
A8CGP1
28.5% inhibition at 10 mM
EDTA
D7PC10
2 mM, 64% of initial activity
epoxyalkyl-beta-glycosides
-
of D-glucose, cellobiose, cellotriose, laminaribiose, laminaritriose, irreversible inactivation of enzyme
-
epoxyalkyl-beta-glycosides
-
active site directed inhibition
-
Hg2+
-
33% loss of activity by 0.5 mM
Hg2+
-
87% loss of activity by 0.1 mM
Hg2+
Flavobacterium dormitator
-
96% inhibition of beta-1,3-glucanase IV activity after incubation with 1 mM at 5C, pH 6.0, for 3 h, no inhibition in presence of beta-mercaptoethanol
Hg2+
-
60% loss of activity by 0.1 mM
Hg2+
Flavobacterium dormitator
-
99% inhibition with 10 mM
Hg2+
-
complete inhibition by 2 mM HgSO4
Hg2+
D7PC10
2 mM, complete loss of activity
KMnO4
-
56% loss of activity by 0.5 mM, complete inactivation by 2 mM
Mn2+
-
50% loss of activity by 0.5 mM
N-bromosuccinimide
-
81% loss of activity by 0.5 mM, complete inactivation by 2 mM
Na2MoO4
A8CGP1
20% inhibition at 10 mM
Phenylmercuric nitrate
-
loss of 93% of activity after preincubation of enzyme for with 5 mg/ml for 30 min
Zn2+
A8CGP1
7.6% inhibition at 10 mM
Mn2+
A8CGP1
54% inhibition at 10 mM
additional information
-
not inhibited by laminarin or lichenin
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
Q8GMY0
0.1%, activates
2-mercaptoethanol
D7PC10
2 mM, 119% of initial activity
arginine
A8CGP1
8% activation at 10 mM
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
9.09
-
D-glucose
-
-
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
0.19
-
oxidized laminarin
-
-
-
0.004
-
short-chain pachyman
-
-
-
1.763
-
Glc-beta(1,4)-Glc-beta(1,3)-Glc-methylumbelliferyl
-
mutant enzyme Q18A
additional information
-
Laminarin
Q000P7
1.1 mg/ml, truncated protein C of LamA; 1.8 mg/ml, truncated protein CF of LamA; 2.4 mg/ml, truncated protein CB3 of LamA; 2.4 mg/ml, truncated protein SC of LamA; 2.9 mg/ml, truncated protein CBF of LamA
0.21
-
Laminarin
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
Streptococcus bovis JB1
-
-
-
additional information
-
additional information
-
kinetic data
-
additional information
-
additional information
-
pH 5, 50C, 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
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
Km-value for beta-glucan is 1.87 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
A8CGP1
kinetics
-
additional information
-
additional information
-
kinetics, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
114.8
-
1,3-1,4-beta-D-glucan
-
pH 5, 50C, soluble, from barley, EG VII
-
281.2
-
1,3-1,4-beta-D-glucan
-
pH 5, 50C, soluble, from barley, EG VI
-
7207
-
beta-1,3-1,4-glucan
A8CGP1
pH 6.4, 40C, purified recombinant His-tagged enzyme, substrate from Hordeum vulgare
26.7
-
beta-Glucan
-
mutant enzyme F41A
83
-
beta-Glucan
-
mutant enzyme K260A
135
-
beta-Glucan
-
mutant enzyme E70A
250
-
beta-Glucan
-
mutant enzyme Y115A
383
-
beta-Glucan
-
mutant enzyme Q18A
433
-
beta-Glucan
-
mutant enzyme E258A
1233
-
beta-Glucan
-
wild-type enzyme
1300
-
beta-Glucan
-
mutant enzyme N157A
1417
-
beta-Glucan
-
mutant enzyme W114A
2250
-
beta-Glucan
-
mutant enzyme W72A
15600
-
beta-Glucan
-
-
142.6
-
Carboxymethylcellulose
-
pH 5, 50C, EG VII
-
632.8
-
Carboxymethylcellulose
-
pH 5, 50C, EG VI
-
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
23.1
-
Laminarin
-
pH 6.0, 30C
750
-
Laminarin
-
pH 6, 30C
0.21
-
laminaritetraose
-
pH 6.0, 30C
0.047
-
lichenan
-
pH 7.2, 50C, mutant enzyme E131Q
8.08
-
lichenan
-
pH 7.2, 50C, mutant enzyme E63Q
27
-
lichenan
-
pH 7.2, 50C, mutant enzyme E63D
40.4
-
lichenan
-
pH 7.2, 50C, mutant enzyme Y123A
40.5
-
lichenan
-
pH 7.2, 50C, mutant enzyme W192A
112.6
-
lichenan
-
pH 7.2, 50C, mutant enzyme E63D
147.1
-
lichenan
-
pH 7.2, 50C, mutant enzyme H99R
163.8
-
lichenan
-
pH 7.2, 50C, mutant enzyme W184Y
174.7
-
lichenan
-
pH 5, 50C, EG VI
262
-
lichenan
-
pH 7.2, 50C, mutant enzyme N26A
276
-
lichenan
-
pH 7.2, 50C, mutant enzyme H99D
302.4
-
lichenan
-
pH 7.2, 50C, mutant enzyme E131Q
324
-
lichenan
-
pH 7.2, 50C, mutant enzyme S90A
325
-
lichenan
-
pH 7.2, 50C, mutant enzyme Y24A
481
-
lichenan
-
pH 7.2, 50C, mutant enzyme Y24F
627
-
lichenan
-
pH 7.2, 50C, mutant enzyme Y123F
787
-
lichenan
-
pH 7.2, 50C, mutant enzyme Y24W
811
-
lichenan
-
pH 7.2, 50C, mutant enzyme R65A
908
-
lichenan
-
pH 7.2, 50C, mutant enzyme A98W
1191
-
lichenan
-
pH 7.2, 50C, wild-type enzyme
1350
-
lichenan
A8CGP1
pH 6.4, 40C, substrate from Hordeum vulgare
1050
-
lichenin
-
pH 6, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
0.4
-
-
lichenin as substrate
0.46
-
Flavobacterium dormitator
-
yeast glucan as substrate
1.32
-
-
DEAE anion exchange chromatography
1.38
-
Flavobacterium dormitator
-
pachyman as substrate
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
-
Streptococcus bovis JB1
-
laminarin as substrate
25
-
Flavobacterium dormitator
-
purified enzyme, laminarin as substrate
66
-
-
short-chain pachyman as substrate
68
-
-
purified native enzyme
172
-
-
purified enzyme
303.5
-
Streptococcus bovis JB1
-
lichenin as substrate
338.3
-
Streptococcus bovis JB1
-
barley beta-glucan as substrate
350
-
-
purified enzyme
379.1
-
A8CGP1
purified recombinant His-tagged enzyme, substrate lichenan
728.8
-
A8CGP1
purified recombinant His-tagged enzyme, substrate beta-glucan from Hordeum vulgare
6900
-
-
purified enzyme, beta-glucan as substrate
additional information
-
-
-
additional information
-
Q000P7
0.3 U/nmol with substrate curdlan, truncated protein C of LamA; 0.3 U/nmol with substrate pachyman, truncated protein C of LamA; 0.4 U/nmol with substrate barley beta-glucan, truncated protein C of LamA; 0.4 U/nmol with substrate lichenan, truncated protein CF of LamA; 0.4 U/nmol with substrate lichenan, truncated protein C of LamA; 0.4 U/nmol with substrate pachyman, truncated protein CF of LamA; 0.4 U/nmol with substrate zymosan A, truncated protein C of LamA; 0.5 U/nmol with substrate barley beta-glucan, truncated protein CF of LamA; 0.5 U/nmol with substrate zymosan A, truncated protein CF of LamA; 0.6 U/nmol with substrate curdlan, truncated protein CF of LamA; 0.6 U/nmol with substrate pachyman, truncated protein SC of LamA; 0.7 U/nmol with substrate barley beta-glucan, truncated protein SC of LamA; 0.7 U/nmol with substrate curdlan, truncated protein SC of LamA; 0.7 U/nmol with substrate lichenan, truncated protein SC of LamA; 0.7 U/nmol with substrate zymosan A, truncated protein SC of LamA; 0.8 U/nmol with substrate pachyman, truncated protein CB3 of LamA; 0.8 U/nmol with substrate zymosan A, truncated protein CB3 of LamA; 0.9 U/nmol with substrate barley beta-glucan, truncated protein CB3 of LamA; 0.9 U/nmol with substrate lichenan, truncated protein CB3 of LamA; 1.0 U/nmol with substrate curdlan, truncated protein CB3 of LamA; 1.3 U/nmol with substrate lichenan, truncated protein CBF of LamA; 1.3 U/nmol with substrate pachyman, truncated protein CBF of LamA; 1.4 U/nmol with substrate laminarin, truncated protein C of LamA; 1.5 U/nmol with substrate barley beta-glucan, truncated protein CBF of LamA; 1.6 U/nmol with substrate zymosan A, truncated protein CBF of LamA; 1.7 U/nmol with substrate laminarin, truncated protein CF of LamA; 2.0 U/nmol with substrate curdlan, truncated protein CBF of LamA; 2.6 U/nmol with substrate laminarin, truncated protein CB3 of LamA; 3.7 U/nmol with substrate laminarin, truncated protein CBF of LamA; 4.6 U/nmol with substrate laminarin, truncated protein SC of LamA; no activity with carboxymethylcellulose and xylan of all truncated proteins of LamA
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
-
assay at
5.5
-
-
in 0.05 M sodium succinate buffer with laminarin as substrate
5.5
-
Flavobacterium dormitator
-
-
5.5
-
Q000P7
toward laminarin hydrolysis for truncated proteins CBF and C
5.6
-
-
recombinant enzyme
5.8
-
-
in 100 mM acetate buffer
5.8
-
D7PC10
-
6
6.5
Flavobacterium dormitator
-
pH 6.0 with yeast glucan, pH 6.5 with laminarin as substrate
6
-
Q8GMY0
recombinant enzyme
6
-
-
assay at
6.4
-
A8CGP1
recombinant enzyme
6.5
-
Streptococcus bovis JB1
-
in 50 mM sodium phosphate buffer
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
8
-
pH 4.5: about 60% of maximal activity, pH 8: about 50% of maximal activity
4.5
8
Q8GMY0
pH 4.5: abput 40% of maximal activity, pH 8.0: about 55% of maximal activity
5
8
A8CGP1
profile, overview
5
8
D7PC10
more than 65% of maximum activity within
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
assay at
40
55
Flavobacterium dormitator
-
40C with yeast glucan, 55C with laminarin as substrate
40
55
Flavobacterium dormitator
-
55C laminarin as substrate
40
-
-
recombinant enzyme
40
-
Q000P7
for truncated protein CBF, pH 5.5
40
-
A8CGP1
recombinant enzyme
45
-
Q8GMY0
recombinant enzyme
50
-
-
assay at
50
-
Q000P7
for truncated protein C, pH 5.5
50
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
65
A8CGP1
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
-
D7PC10
rapid loss of activity above
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.55
-
A8CGP1
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
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
Manually annotated by BRENDA team
Streptococcus bovis JB1
-
-
Manually annotated by BRENDA team
Phaffia rhodozyma CBS 6938
-
-
-
Manually annotated by BRENDA team
-
aleurone and scutellar epithelium
Manually annotated by BRENDA team
Cherax destructor Clark
-
-
-
Manually annotated by BRENDA team
-
LIC 1 is secreted by the salivary glands
Manually annotated by BRENDA team
-
germinated
Manually annotated by BRENDA team
-
young leaves and roots
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
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
Manually annotated by BRENDA team
Streptococcus bovis JB1
-
-
-
Manually annotated by BRENDA team
Phaffia rhodozyma CBS 6938
-
-
-
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
16600
-
-
gel filtration
17000
-
-
-
21000
-
-
SDS-PAGE, gel filtration
22000
-
-
gel filtration
24100
-
Streptococcus bovis JB1
-
-
27000
-
Flavobacterium dormitator
-
SDS-PAGE
29000
-
-
SDS-PAGE
31900
33000
Flavobacterium dormitator
-
gel filtration, SDS-PAGE, ultracentrifugation
38200
-
Q000P7
calculated molecular mass of expressed C of LamA
41000
-
-
SDS-PAGE, a second band of 62000 Da is detected
51600
-
Q000P7
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
-
Q000P7
calculated molecular mass of expressed SC of LamA
92000
-
Q000P7
calculated molecular mass of expressed CB3 of LamA
144600
-
Q000P7
calculated molecular mass of expressed CBF of LamA
160000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 25000, SDS-PAGE
?
-
x * 36000, SDS-PAGE
?
-
x * 28000, recombinant enzyme, SDS-PAGE
?
Q8GMY0
x * 34000, SDS-PAGE
?
-
x * 39700, SDS-PAGE
?
A8CGP1
x * 24440, sequence calculation, x * 25500, recombinant His-tagged enzyme, SDS-PAGE
?
-
x * 33000, SDS-PAGE
?
-
x * 36000, SDS-PAGE
?
D7PC10
x * 60000, SDS-PAGE, x * 60700, calculated
?
-
x * 60000, SDS-PAGE, x * 60700, calculated
-
?
Bacillus licheniformis EGW039
-
x * 28000, recombinant enzyme, SDS-PAGE
-
?
Bacillus subtilis MA139
-
x * 24440, sequence calculation, x * 25500, recombinant His-tagged enzyme, SDS-PAGE
-
monomer
Flavobacterium dormitator
-
1 * 27000
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
additional information
-
HdLam33 primary structure, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
Q8GMY0
-
glycoprotein
-
acidic glycoprotein
glycoprotein
Flavobacterium dormitator
-
10.3% carbohydrate, 17 hexose units
proteolytic modification
Flavobacterium dormitator
-
beta-1,3-glucanase I is formed by proteolysis of beta-1,3-glucanase II
glycoprotein
-
-
glycoprotein
-
glycosylation at Asn43
glycoprotein
-
the degree of glycosylation is similar in the wild-type and recombinant proteins
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
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
O52754
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
5
Streptococcus bovis JB1
-
at pH 5 69%, at pH 4 23%, at pH 3 2% of maximal activity
3
9
-
4C, 48 h stable with 5-20% loss of activity
3
-
Q8GMY0
12 h, enzyme retains 80% of its original activity
3.8
11.2
D7PC10
1 h, more than 60% residual activity
4
10
A8CGP1
purified recombinant His-tagged enzyme, 40C, 1 h, stable
4
6
Q8GMY0
stable
4
8
-
stable in the range
6
9
Flavobacterium dormitator
-
enzymes I, II and IV: 10 min, 55C, stable, unstable below pH 6 and above pH 9
6
9
Flavobacterium dormitator
-
-
8
-
Q8GMY0
12 h, enzyme retains 80% of its original activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
A8CGP1
purified recombinant His-tagged enzyme, 80% remaining activity after 2 h
42
-
-
50% inactivation
50
60
Streptococcus bovis JB1
-
stable for 20 min at 50C, at 60C loss of 75% of maximal activity
50
70
Flavobacterium dormitator
-
enzyme IV: 80% of activity after heating at 50C for 10 min
50
70
Flavobacterium dormitator
-
enzyme I: full activity on heating at 55C at pH 6.0 for 10 min, substantial loss of activity by heating at 70C for 10 min
50
-
-
7% loss of activity after incubation for 10 min
50
-
Q8GMY0
30 min, 5% loss of activity
50
-
A8CGP1
purified recombinant His-tagged enzyme, 70% remaining activity after 2 h
50
-
-
purified native enzyme, 15 min, loss of 50% activity
50
-
-
free recombinant enzyme, 2 h, 51.9% remaining activity
60
-
-
absence of substrate, 10 min, complete loss of activity
60
-
Q8GMY0
30 min, 40% loss of activity
60
-
A8CGP1
purified recombinant His-tagged enzyme, 20% remaining activity after 30 min, below 10% after 60 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
-
D7PC10
1 h, more than 70% residual activity
70
-
Q8GMY0
30 min, complete loss of activity
70
-
-
1 min, 4% loss of activity at high protein concentration
70
-
A8CGP1
purified recombinant His-tagged enzyme, inactivation within 10 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
-
D7PC10
30 min, 20% residual activity
71
-
-
Tm-value for wild-type enzyme is 71.4C
75
-
-
Tm-value for mutant enzyme N207D is 75.3C
80
-
-
2 days, stable
80
-
-
1 min, 6% loss of activity at high protein concentration
80
-
A8CGP1
purified recombinant His-tagged enzyme, inactivation within 5 min
90
-
-
1 min, 19% loss of activity at high protein concentration
95
100
-
incubation at 100C: 82% of initial activity at 95C, 57% at 100C
additional information
-
-
thermostable enyzme
additional information
-
-
EG VI and EG VII are thermostable
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
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
resistant against proteolysis by trypsin and chymotrypsin, slow digestion by protease V8, complete digestion by thermolysin
-
stable against proteolysis, full activity after papain treatment for 20 h
Flavobacterium dormitator
-
about 66% of activity lost after dialysis against distilled water at 2C for 18 h
-
stabilization of activity at 37C for 3 h by bovine serum albumin, no effect for longer periods
-
complete inactivation by 1% SDS
-
LIC 1 is stable in the presence of Periplaneta americana proteinases
-
unaffected by pepsin, pancreatin and bile extract
-
30% of activity at 1% SDS w/v after 20 min incubation
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ethanol
-
40% of activity after 20 min incubation with 10% v/v ethanol
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, 0.1 M McIlvaine buffer, pH 5.8, retains almost all initial activity after 1 week of storage
D7PC10
0C, 7 days, no detectable loss of activity
-
-20C, cell paste, without appreciable loss of activity
Saccharomyces lactis
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
native enzyme 126fold by ammonium sulfate fractionation, several steps of cation exchange chromatography, and gel filtration
-
recombinant enzyme
-
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography
A8CGP1
affinity chromatography
-
precipitation, a combination of anion exchange, hydrophobic interaction and gel filtration chromatography, all chromatography is carried out at 4C
-
-
Flavobacterium dormitator
-
beta-1,3-glucanase II from periplasmic fraction of Escherichia coli clone cells
Flavobacterium dormitator
-
native enzyme 340fold from digestive fluid by ammonium sulfate fractionation, hydrophobic interaction and cation exchange chromatography, and gel filtration to homogeneity
-
immobilized Ni2+ affinity chromatography, gel filtration chromatography
Q000P7
from midgut and salivary gland
-
recombinant enzyme
-
recombinant LamR, from transformed Escherichia coli cells
-
partial
Saccharomyces lactis
-
-
Streptococcus bovis JB1
-
EG VI and EG VII
-
from recombinant Escherichia coli cells
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Pichia pastoris
D7PC10
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
-
expression in Escherichia coli BL21 (DE3)
-
expression in Pichia pastoris. The beta-1,3-1,4-glucanase gene is modified and expressed according to its preferred codon usage
Q8GMY0
DNA and amino acid sequence determination and analysis, expression of the His-tagged enzyme in Escherichia coli strain Bl21
A8CGP1
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
-
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
-
expression of recombinant truncated proteins in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
Flavobacterium dormitator
-
HdLam33, DNA and amino acid sequence determination and analysis
-
expression of five truncated proteins of LamA in Escherichia coli BL21(DE3)
Q000P7
expression in Pichia pastoris
-
recombinantly expressed in Pichia pastoris
-
placing of gene eng2+ under the control of a repressible promoter
-
expression in Escherichia coli, Enterococcus faecalis, Lactococcus lactis
Streptococcus bovis JB1
-
expression in Escherichia coli
Q55365, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
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
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
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
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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
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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
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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
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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
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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
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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
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turnover-number for lichenan is 1.5fold lower than wild-type value, turnover-number for laminarin is 1.9fold higher than wild-type value
N207D
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increase in Tm-value to 75.3C, compared to wild-type Tm-value of 71.4C
additional information
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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
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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
Bacillus subtilis BF7658
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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
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additional information
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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 65C to 75C, but that of family-9 carbohydrate-binding module to rCM and rCM-22-CM does not affect the optimum temperature
additional information
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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
K260A
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kcat/Km for beta-glucan is 31fold lower than wild-type value
additional information
Q59328
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
E115S
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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
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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
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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
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
food industry
D7PC10
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
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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%
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synthesis
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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
Bacillus circulans ATCC21367
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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
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nutrition
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reducing the amount of high-molecular-mass beta-glucans during malting in brewing industry, improvement of digestibility in broiler chicks production
biotechnology
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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
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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
analysis
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use in structural analysis of polysaccharides
agriculture
-
synergistic effect with fungicide Fongarid
nutrition
-
reducing the amount of high-molecular-mass beta-glucans during malting in brewing industry, improvement of digestibility in broiler chicks production
drug development
Q000P7
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
drug development
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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
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nutrition
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endo-beta-D-glucanases EG VI and EG VII are ideal candidates for tailored modification of macromolecular beta-glucan in industrial applications
nutrition
Talaromyces emersonii CBS 814.70
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endo-beta-D-glucanases EG VI and EG VII are ideal candidates for tailored modification of macromolecular beta-glucan in industrial applications
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agriculture
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disease protection of plants because of antimycotic activity in combination with chitinases