Information on EC 3.2.1.39 - glucan endo-1,3-beta-D-glucosidase

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

EC NUMBER
COMMENTARY
3.2.1.39
-
RECOMMENDED NAME
GeneOntology No.
glucan endo-1,3-beta-D-glucosidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans
show the reaction diagram
Different from EC 3.2.1.6 endo-1,3(4)-beta-glucanase. Very limited action on mixed-link (1,3-1,4-)-beta-D-glucans. Hydrolyses laminarin, paramylon and pachyman
-
-
-
hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans
show the reaction diagram
E94 reacts as nucleophile, E236 as proton donor
-
hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans
show the reaction diagram
AkLam36 mode of action, overview
-
hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans
show the reaction diagram
the enzyme is an endoglucanase that hydrolyzes beta-1,3-glucans as laminarin and yeast beta-1,3-1,6-glucan, but is inactive toward other polysaccharides, e.g. unbranched beta-1,3-glucans or mixed beta-1,3-1,4-glucan from cereals, or disaccharides. TLam has two ionizable groups involved in catalysis, and His, Tyr and Arg residues plus a divalent ion at the active site. A Cys residue important for TLam activity is exposed after laminarin binding. Residues E174, E179, H204, Y304, R127 and R181 at the active site of the enzyme are important for TLam activity
C6GFH7, -
hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans
show the reaction diagram
D422, E499 and E503 are involved in catalysis.E499 is the catalytic base, F425 plays a major role in substrate binding possibly mediated by aromatic ring stacking with the sugar substrate
-
hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans
show the reaction diagram
D422, E499 and E503 are involved in catalysis.E499 is the catalytic base, F425 plays a major role in substrate binding possibly mediated by aromatic ring stacking with the sugar substrate
Thermobifida fusca YX-ER1
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
transglycosylation
-
-
PATHWAY
KEGG Link
MetaCyc Link
Starch and sucrose metabolism
-
SYSTEMATIC NAME
IUBMB Comments
3-beta-D-glucan glucanohydrolase
Different from EC 3.2.1.6 endo-1,3(4)-beta-glucanase. Very limited action on mixed-link (1->3,1->4)-beta-D-glucans. Hydrolyses laminarin, paramylon and pachyman.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
(1-3)-beta-D-glucan endohydrolase
-
-
(1-3)-beta-D-glucanase
-
three isoforms, GI, GII and GIII
(1-3)-beta-glucanase GI
-
-
(1->3)-beta-glucan endohydrolase
-
-
-
-
(1->3)-beta-glucan endohydrolase BGN13.1
-
-
-
-
(1->3)-beta-glucan endohydrolase GI
-
-
-
-
(1->3)-beta-glucan endohydrolase GII
-
-
-
-
(1->3)-beta-glucan endohydrolase GIII
-
-
-
-
(1->3)-beta-glucan endohydrolase GIV
-
-
-
-
(1->3)-beta-glucan endohydrolase GV
-
-
-
-
(1->3)-beta-glucan endohydrolase GVI
-
-
-
-
(1->3)-beta-glucanase
-
-
-
-
(1->3)-beta-glucanase A1
-
-
-
-
(1->3)-beta-glucanase BGN13.1
-
-
-
-
(1->3)-beta-glucanase isoenzyme GI
-
-
-
-
(1->3)-beta-glucanase isoenzyme GII
-
-
-
-
(1->3)-beta-glucanase isoenzyme GIII
-
-
-
-
(1->3)-beta-glucanase isoenzyme GIV
-
-
-
-
(1->3)-beta-glucanase isoenzyme GV
-
-
-
-
(1->3)-beta-glucanase isoenzyme GVI
-
-
-
-
(13)-beta-glucan 3-glucanohydrolase
-
-
-
-
(13)-beta-glucan endohydrolase
-
-
-
-
1,3-beta-glucan 3-glucanohydrolase
-
-
-
-
1,3-beta-glucan hydrolase
-
-
1,3-beta-glucanase I
-
-
Acidic beta-1,3-glucanase
-
-
-
-
AkLam36
-
-
Anther-specific protein A6
-
-
-
-
Ban-Gluc
-
-
Basic beta-1,3-endoglucanase BGN13.1
-
-
-
-
Basic beta-1,3-glucanase
-
-
-
-
beta-(1-3)-glucanase
-
-
beta-1,3 glucanase
-
-
beta-1,3-endoglucanase
-
-
beta-1,3-endoglucanase
-
two isoforms, pH 8.7 and pH 10.5 glucanases
beta-1,3-endoglucanase
B3VTS4
-
Beta-1,3-endoglucanase GI
-
-
-
-
Beta-1,3-endoglucanase GII
-
-
-
-
Beta-1,3-endoglucanase GIII
-
-
-
-
Beta-1,3-endoglucanase GIV
-
-
-
-
Beta-1,3-endoglucanase GV
-
-
-
-
Beta-1,3-endoglucanase GVI
-
-
-
-
Beta-1,3-endoglucanase, basic
-
-
-
-
beta-1,3-glucan hydrolase
-
-
beta-1,3-glucanase
-
-
-
-
beta-1,3-glucanase
-
-
beta-1,3-glucanase
O68641
-
beta-1,3-glucanase
B4XEK5
-
beta-1,3-glucanase
C6L684
-
beta-1,3-glucanase
Q02126
-
beta-1,3-glucanase
-
-
beta-1,3-glucanase
Hypocrea koningii ALL 13
-
-
-
beta-1,3-glucanase
-
-
beta-1,3-glucanase
-
-
beta-1,3-glucanase
Q000P7
-
beta-1,3-glucanase
Paenibacillus sp. BCRC
Q000P7
-
-
beta-1,3-glucanase
B4XEK7
-
beta-1,3-glucanase
-
-
beta-1,3-glucanase
C6GFH7
-
beta-1,3-glucanase
-
-
beta-1,3-glucanase
Thermobifida fusca YX-ER1
-
-
-
beta-1,3-glucanase
Trichoderma asperellum, Trichoderma sp.
-
-
beta-1,3-glucanase
-
-
beta-1,3-glucanase I
-
-
beta-1,3-glucanase II
-
-
beta-glucanase
-
-
BglS27
C3VPJ1
-
callase
-
-
-
-
endo-(1,3)-beta-D-glucanase
-
-
-
-
endo-(1-3)-beta-glucanase
-
two different forms, glucanase I and glucanase II
endo-(13)-beta-D-glucanase
-
-
-
-
endo-1,3-beta-D-glucanase
-
-
-
-
endo-1,3-beta-D-glucanase
-
-
endo-1,3-beta-D-glucanase
-
-
endo-1,3-beta-D-glucanase
-
-
endo-1,3-beta-D-glucanase
C3VPJ1
-
endo-1,3-beta-glucanase
-
-
-
-
endo-1,3-beta-glucanase
-
-
endo-1,3-beta-glucanase
Gecarcoidea natalis Pocock 1888
-
-
-
endo-1,3-beta-glucanase
-, Q1ERF7, Q1ERF8, Q1ERF9, Q1ERG0, Q1ERG1, Q1ERG2
-
endo-1,3-beta-glucosidase
-
-
-
-
endo-1,3-glucanase
-
-
-
-
endo-1,3;4-beta-glucanase
C6L684
-
endo-beta-1,3-glucanase
-
-
endo-beta-1,3-glucanase
-
-
endo-beta-1,3-glucanase
C1IE32
-
endo-beta-1,3-glucanase
-
-
endo-beta-1,3-glucanase
-
-
endo-beta-1,3-glucanase
-
-
endo-beta-1,3-glucanase
-
-
-
endo-beta-1,3-glucanase
-
-
endo-beta-1,3-glucanase
-
-
endo-beta-1,3-glucanase
O73951
-
endo-beta-1,3-glucanase
Rhizopus sp.
-
-
endo-beta-1,3-glucanase
-
-
endo-beta-1,3-glucanase
Saccharomyces cerevisiae YPA84
-
-
-
endo-beta-1,3-glucanase
-
-
endo-beta-1,3-glucanase
-
-
Eng2 protein
-
-
Eng2 protein
Saccharomyces cerevisiae YPA84
-
-
-
exo-beta-1,3-glucanase
-
-
Gbl2a
Q1ERG2
-
Gbl2b
Q1ERG1
-
Gbl2c
Q1ERG0
-
Gbl2d
Q1ERF9
-
Gbl2e
Q1ERF8
-
Gbl2f
Q1ERF7
-
Glu1
G9M5R4
-
GLUB20-2
Q70C53
isoform
glucan endo-1,3-beta-glucosidase
-
-
-
-
Glucanase GLA
-
-
-
-
Glucanase GLB
-
-
-
-
glucanase Lo
-
-
HdLam33
C6L684
-
kitalase
-
-
-
-
Lam81A
Thermobifida fusca YX-ER1
-
-
-
LamA
Paenibacillus sp. BCRC, Paenibacillus sp. CCRC 17245
Q000P7
-
-
LamA
O73951
gene name
laminaranase
-
-
-
-
laminarinase
-
-
-
-
laminarinase
-
-
laminarinase
-
-
laminarinase
Gecarcoidea natalis Pocock 1888
-
-
-
laminarinase
C6GFH7
-
Lic16A
Clostridium thermocellum F7
Q59328
-
-
lytic beta-(1-3)-glucanase I
-
-
oligo-1,3-glucosidase
-
-
-
-
OsGlu1
Q9SXY6
-
OsGlu2
Q9SXY8
gene name
PCEng2p
B3VTS4
-
PfLamA
O73951
-
PpGns1
-
-
-
-
PR-2B
-
-
-
-
PR-35
-
-
-
-
PR-36
-
-
-
-
PR-37
-
-
-
-
TLam
C6GFH7
-
YlCrh1Sp
-
soluble enzyme form lacking the C-terminal consensus sequence for GPI anchoring and showing glycosidase activity on laminarin
YlCrh2Sp
-
soluble enzyme form lacking the C-terminal consensus sequence for GPI anchoring and showing glycosidase activity on laminarin
lytic beta-(1-3)-glucanase II
-
-
additional information
C1IE32
the enzyme belongs to the glycosyl hydrolase family 16, GH16
additional information
C6L684
the enzyme belongs to the glycoside hydrolase family 16
additional information
Q000P7
LamA contains a catalytic module of the glycoside hydrolase family 16, GH16
additional information
Paenibacillus sp. BCRC
Q000P7
LamA contains a catalytic module of the glycoside hydrolase family 16, GH16
-
additional information
B3VTS4
the enzyme shows similarities to fungal glycosyl hydrolases GH family 81
additional information
-
the enzyme belongs to the glycosyl hydrolase family 81, GH81
additional information
C3VPJ1
the bacterial enzyme belongs to glycosylhydrolase family GH16
additional information
C6GFH7
the enzyme belongs to glycoside hydrolase family 16
additional information
-
Lam81A is a single domain family 81 beta-1,3-endoglucanase
additional information
Thermobifida fusca YX-ER1
-
Lam81A is a single domain family 81 beta-1,3-endoglucanase
-
CAS REGISTRY NUMBER
COMMENTARY
9025-37-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
enzyme synthesis induced by culturing on media containing Agaricus bisporus fruiting body cell walls and fructose
-
-
Manually annotated by BRENDA team
strain ATCC 76739
-
-
Manually annotated by BRENDA team
strain NHB-10
Uniprot
Manually annotated by BRENDA team
strain NHB-10
Uniprot
Manually annotated by BRENDA team
member of glycosyl hydrolase family 16
-
-
Manually annotated by BRENDA team
enhanced activity if grown in the presence of NaCl
-
-
Manually annotated by BRENDA team
Bacillus clausii NM-1
NM-1
-
-
Manually annotated by BRENDA team
alkalophilic strain K-12-5
-
-
Manually annotated by BRENDA team
enzyme synthesis induced in pachyman-containing medium
-
-
Manually annotated by BRENDA team
enzyme expression is decreased during the hyphal transition
-
-
Manually annotated by BRENDA team
enzyme comprises a catalytic domain of the glycoside hydrolase family 16 and a C-terminal carbohydrate-binding module family 13
-
-
Manually annotated by BRENDA team
formerly Oerskovia xanthineolytica, strain LLG109
UniProt
Manually annotated by BRENDA team
Cellulosimicrobium cellulans DK-1
enzyme comprises a catalytic domain of the glycoside hydrolase family 16 and a C-terminal carbohydrate-binding module family 13
-
-
Manually annotated by BRENDA team
mexican lime
-
-
Manually annotated by BRENDA team
strain DSM 1237, induction of enzyme by glucans containing 1-3-linkages; strain F7, induction of enzyme by glucans containing 1-3-linkages
SwissProt
Manually annotated by BRENDA team
Clostridium thermocellum F7
strain F7, induction of enzyme by glucans containing 1-3-linkages
SwissProt
Manually annotated by BRENDA team
Delftia tsuruhatensis MV01
-
-
-
Manually annotated by BRENDA team
member of glycosyl hydrolase family 81
-
-
Manually annotated by BRENDA team
Eulota maakii
-
-
-
Manually annotated by BRENDA team
Flavobacterium dormitator
-
-
-
Manually annotated by BRENDA team
Fungi imperfecti
non-identified strain
-
-
Manually annotated by BRENDA team
strain Pocock 1888
-
-
Manually annotated by BRENDA team
Gecarcoidea natalis Pocock 1888
strain Pocock 1888
-
-
Manually annotated by BRENDA team
soybean
-
-
Manually annotated by BRENDA team
Pacific abalone
UniProt
Manually annotated by BRENDA team
L. cv. Clipper
SwissProt
Manually annotated by BRENDA team
strain ALL 13
-
-
Manually annotated by BRENDA team
Hypocrea koningii ALL 13
strain ALL 13
-
-
Manually annotated by BRENDA team
enzyme synthesis induced by growing on chitin-containing medium
-
-
Manually annotated by BRENDA team
enzyme synthesis repressed by glucose, induced by fungal cell wall polymers or autoclaved mycelia from fungi
-
-
Manually annotated by BRENDA team
Rifai T24
-
-
Manually annotated by BRENDA team
Hypocrea lixii Rifai T24
Rifai T24
-
-
Manually annotated by BRENDA team
Glu1 does not belong to existing GH families containing EC 3.2.1.39 glucanases
UniProt
Manually annotated by BRENDA team
Littorina kurila
-
-
-
Manually annotated by BRENDA team
cv. Jonagold
-
-
Manually annotated by BRENDA team
banana
-
-
Manually annotated by BRENDA team
AAA group, subgroup Cavendish, cv. Giant governor
-
-
Manually annotated by BRENDA team
different cultivars Rasthali, Kanthali, and Monthan
-
-
Manually annotated by BRENDA team
cv. Xanthi nc.
-
-
Manually annotated by BRENDA team
fragment; L. cv. Jinheung
SwissProt
Manually annotated by BRENDA team
L. cv. Jinheung
SwissProt
Manually annotated by BRENDA team
strain BCRC 17245, gene lamA
UniProt
Manually annotated by BRENDA team
Paenibacillus sp. BCRC
strain BCRC 17245, gene lamA
UniProt
Manually annotated by BRENDA team
-
B4XEK7
TrEMBL
Manually annotated by BRENDA team
member of glycosyl hydrolase family 16
-
-
Manually annotated by BRENDA team
infected by Orobanche crenata
-
-
Manually annotated by BRENDA team
isolated from female Long Evans rats, gene PCEng2
UniProt
Manually annotated by BRENDA team
cv. Bruine biggareau
-
-
Manually annotated by BRENDA team
gene lamA
-
-
Manually annotated by BRENDA team
differentiation into lytic and non-lytic endo-(1-3)-beta-glucanases against yeast cell walls, three lytic forms, L-1, L-2 and L-4, two non-lytic forms, N-1and N-2
-
-
Manually annotated by BRENDA team
Rhizopus sp.
-
-
-
Manually annotated by BRENDA team
isoform Bgl2
-
-
Manually annotated by BRENDA team
strain YPA84
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae YPA84
strain YPA84
-
-
Manually annotated by BRENDA team
defective in exo-beta-1,3-glucanase formation
-
-
Manually annotated by BRENDA team
several strains, overview
-
-
Manually annotated by BRENDA team
Sclerotium glucanicum
-
-
-
Manually annotated by BRENDA team
(Moench) Garcke, strain Oberna behen (L.) Ikonn
-
-
Manually annotated by BRENDA team
isoform GLUB20-2
UniProt
Manually annotated by BRENDA team
member of glycosyl hysrolase family 16
UniProt
Manually annotated by BRENDA team
grown on purified cell wall of Rhizotonia solani
-
-
Manually annotated by BRENDA team
strain S27, ACCC41168, gene bglS27
UniProt
Manually annotated by BRENDA team
strain YX-ER1
-
-
Manually annotated by BRENDA team
Thermobifida fusca YX-ER1
strain YX-ER1
-
-
Manually annotated by BRENDA team
member of glycosyl hydrolase family 16
UniProt
Manually annotated by BRENDA team
member of glycosyl hydrolase family 16
UniProt
Manually annotated by BRENDA team
Trichoderma sp.
isolated from Brazilian Cerrado soil
-
-
Manually annotated by BRENDA team
amino acid sequence; cultivar Norin 61
-
-
Manually annotated by BRENDA team
cv. Suwon 11, gene TaGlu
Uniprot
Manually annotated by BRENDA team
Glb2a; cultivar Norin 61
UniProt
Manually annotated by BRENDA team
Glb2b; cultivar Norin 61
UniProt
Manually annotated by BRENDA team
Glb2c; cultivar Norin 61
UniProt
Manually annotated by BRENDA team
Glb2d; cultivar Norin 61
UniProt
Manually annotated by BRENDA team
Glb2e; cultivar Norin 61
UniProt
Manually annotated by BRENDA team
Glb2f; cultivar Norin 61
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
B3VTS4, -
PCEng2 plays a significant role in cell wall regulation, the glucan-rich cyst cell wall is essential for cel viability, and regulation of cyst cell wall beta-glucans is a fundamental process during completion of the Pneumocystis life cycle
physiological function
C3VPJ1
BglS27 has the ability to inhibit the growth of phytopathogenic fungi Rhizoctonic solani and Fusarium oxysporum and some mycotoxin-producing fungi Fusarium crookwellense and Paecilomyces variotii
physiological function
-
When Schizosaccharomyces pombe diploid cells undergo meiosis, they differentiate into asci containing four haploid ascospores that are highly resistant to environmental stress. beta-Glucanase Eng2 and endo-alpha-1,3-glucanase Agn2 are required for ascus wall endolysis after sporulation in Schizosaccharomyces pombe
physiological function
O82716
role of beta-1,3-glucanase in the resistance response of wheat to stripe rust pathogen Puccinia striiformis f. sp. tritici
physiological function
-
growth of a deletion strain in various media in solid and liquid cultures at different temperatures does not show a growth phenotype
physiological function
-
enzyme is involved in the autolytic cell wall degradation resulting from carbon starvation of the fungus. The deletion of either engA or chiB encoding an endochitinase, causes highly reduced production of hydrolases in general
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)-beta-D-glucan + H2O
laminaritriose + laminaritetraose
show the reaction diagram
Bacillus clausii, Bacillus clausii NM-1
-
if derived from marine organisms, other(1-3)-beta-D-glucans are not substrate
main products
-
?
(1-3:1-4)-beta-D-glucan + H2O
?
show the reaction diagram
-
very low activity, lichenan
-
?
(1-3:1-4)-beta-D-glucan + H2O
?
show the reaction diagram
-
lichenan
-
?
(1-3:1-4)-beta-D-glucan + H2O
?
show the reaction diagram
-
lichenan
-
?
(1-3:1-4)-beta-D-glucan + H2O
?
show the reaction diagram
Flavobacterium dormitator
-
lichenan
-
?
(1-3:1-4)-beta-D-glucan + H2O
?
show the reaction diagram
-
from cereals, limited action, due to action at few consecutive beta-1,3-linked glucose residues
-
?
(1-3:1-4)-beta-D-glucan + H2O
?
show the reaction diagram
-
release of cellobiose as main product
-
?
3-O-beta-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
smallest substrate, products are smaller oligosaccharides and glucose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
releases laminaribiose and glucose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
Flavobacterium dormitator
-
releases laminaribiose and glucose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
laminaritriose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
laminaritriose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
laminaritriose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
laminaritriose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
Flavobacterium dormitator
-
laminaritriose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
low activity
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
low activity
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
end-product laminaribiose, no glucose release
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
end-products are laminaritriose, laminaribiose and glucose, exhibits weak glucosyltransferase activity
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
products are smaller oligosaccharides and glucose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
release of laminaritriose and glucose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
laminaritetraose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
laminaritetraose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
laminaritetraose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
laminaritetraose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
laminaritetraose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
laminaritetraose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
laminaritetraose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
laminaritetraose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
low activity
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
end-products laminaritriose and laminaribiose, no glucose release
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
laminaripentaose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
laminaripentaose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
laminaripentaose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
laminaripentaose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
laminaripentaose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
main product laminaritriose, small amounts laminaritriose and laminaribiose, no glucose release
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
laminarihexaose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
laminarihexaose
-
?
3-O-beta-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc-D-Glc + H2O
?
show the reaction diagram
-
laminariheptaose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
show the reaction diagram
-
low activity, laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
show the reaction diagram
-
laminaribiose
-
?
3-O-beta-D-glucopyranosyl-D-glucopyranose + H2O
beta-D-glucose + D-glucose
show the reaction diagram
Flavobacterium dormitator
-
laminaribiose
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
show the reaction diagram
-
2% of activity compared to laminaran from Laminaria cichorioides
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucopyranose
show the reaction diagram
-
7% of activity compared to laminaran from Laminaria cichorioides
-
-
?
6-O-beta-D-glucopyranosyl-D-glucose + H2O
beta-D-glucose + D-glucose
show the reaction diagram
-
gentiobiose, low activity
-
?
alkali soluble 1,3-beta-glucan + H2O
reducing sugar + ?
show the reaction diagram
-
produced by solubilised 1,3-beta-glucan synthase complex of A. fumigatus
-
?
alpha-laminaribiosyl fluoride + H2O
?
show the reaction diagram
-
-
-
-
?
avicel + H2O
?
show the reaction diagram
Q000P7
-
-
-
?
avicel + H2O
?
show the reaction diagram
Q000P7
i.e. microcrystalline cellulose
-
-
?
avicel + H2O
?
show the reaction diagram
C6GFH7, -
microcrystalline cellulose
-
-
?
avicel + H2O
?
show the reaction diagram
Paenibacillus sp. BCRC
Q000P7
i.e. microcrystalline cellulose
-
-
?
azurine-crosslinked beta-1,3-glucan + H2O
?
show the reaction diagram
-
AZCL-pachyman
-
?
azurine-crosslinked beta-1,3:1,4-glucan + H2O
?
show the reaction diagram
-
AZCL-barley-beta-glucan, 100fold less active than on AZCL-pachyman
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-, Q59328
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
Q000P7
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
main linkage type beta-1,3-1,4(Glc), about 10% of the specific activity compared to laminarin
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
Clostridium thermocellum F7
Q59328
-
-
-
?
barley glucan + H2O
?
show the reaction diagram
-
8% activity compared to laminarin
-
-
?
beta-1,3-1,4-glucan + H2O
?
show the reaction diagram
C6GFH7, -
substrate from Hordeum vulgare, substrate of EC 3.2.1.6, endo-1,3(4)-beta-glucanase
-
-
?
beta-1,3-glucan + H2O
laminaribiose + D-glucose
show the reaction diagram
B4XEK5
-
-
-
?
beta-1,3-glucan + H2O
laminaribiose + D-glucose
show the reaction diagram
B4XEK7
-
-
-
?
beta-1,3-glucan + H2O
?
show the reaction diagram
Delftia tsuruhatensis, Delftia tsuruhatensis MV01
-
sources: Pediococcus parvalus and yeast
-
-
?
beta-D-glucan + H2O
?
show the reaction diagram
Flavobacterium dormitator
-
-
-
-
-
beta-D-glucan + H2O
?
show the reaction diagram
A5IL44, -
-
-
-
?
beta-D-glucan + H2O
?
show the reaction diagram
A5IL44
-
-
-
?
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
Trichoderma sp., Trichoderma asperellum
-
-
-
-
?
beta-glucan + H2O
?
show the reaction diagram
-
low activity
-
?
beta-glucan + H2O
?
show the reaction diagram
-
low activity
-
?
beta-glucan + H2O
?
show the reaction diagram
-
low activity
-
?
beta-glucan + H2O
?
show the reaction diagram
-
from yeast
-
?
beta-glucan + H2O
?
show the reaction diagram
-
from yeast
-
-
?
beta-glucan + H2O
?
show the reaction diagram
-
from yeast
-
?
beta-glucan + H2O
?
show the reaction diagram
-
from yeast
-
?
beta-glucan + H2O
?
show the reaction diagram
-
from yeast
-
?
beta-glucan + H2O
?
show the reaction diagram
-
from yeast
-
?
beta-glucan + H2O
?
show the reaction diagram
-
from yeast
-
?
beta-glucan + H2O
?
show the reaction diagram
Rhizopus sp.
-
from yeast
-
?
beta-glucan + H2O
?
show the reaction diagram
-
from yeast
-
?
beta-glucan + H2O
?
show the reaction diagram
Flavobacterium dormitator
-
from yeast
-
?
beta-glucan + H2O
?
show the reaction diagram
Fungi imperfecti
-
from yeast
-
?
beta-glucan + H2O
?
show the reaction diagram
-
from oat
-
?
beta-glucan + H2O
?
show the reaction diagram
-
31.2% activity
-
?
beta-glucan + H2O
?
show the reaction diagram
-
beta-glucanases I and II differ in substrate affinity according to the degree of its polymerization, complete degradation of yeast glucan is determined by synergistic activities of more than one beta-glucanase
-
?
beta-glucan + H2O
?
show the reaction diagram
Rhizopus sp.
-
rapid reduction up to 60% on the turbidity of substrate suspension, slow and very little release of glucose and reducing sugars
-
?
beta-glucan + H2O
?
show the reaction diagram
-
from yeast cell wall
-
?
beta-glucan + H2O
?
show the reaction diagram
-
from barley
-
?
beta-glucan + H2O
?
show the reaction diagram
-
from barley
-
?
beta-glucan + H2O
?
show the reaction diagram
-
beta-1,3- and beta-1,4-linkages
-
?
beta-glucan + H2O
?
show the reaction diagram
-
beta-1,3- and beta-1,4-linkages, major product cellobiose
-
?
beta-glucan + H2O
?
show the reaction diagram
Fungi imperfecti
-
beta-1,3-glucanase of the random type, producing more higher oligosaccharides
-
?
beta-glucan + H2O
?
show the reaction diagram
C3VPJ1
Barley beta-glucan, 1,3-1,4-beta-glucose monomers, high activity
-
-
?
beta-glucan + H2O
?
show the reaction diagram
-
from cell wall polysaccharide extracts of fruits or from barley, activites and substrate specificities of enzymes from different cultivars, overview
-
-
?
beta-glucan + H2O
?
show the reaction diagram
Trichoderma sp., Trichoderma asperellum
-
macro- and micro-assay method development and evaluation, overview
-
-
?
beta-glucan + H2O
?
show the reaction diagram
Thermobifida fusca YX-ER1
-
-
-
-
?
callose + H2O
?
show the reaction diagram
Q02126
-
-
-
?
carboxy-methylated pachyman + H2O
?
show the reaction diagram
-
-
-
-
?
carboxymethyl curdlan + H2O
?
show the reaction diagram
G9M5R4
13.7% of the activity with laminarin
-
-
?
carboxymethyl curdlan-Remazol Brilliant Blue + H2O
?
show the reaction diagram
-
-
-
-
?
carboxymethyl pachyman + H2O
?
show the reaction diagram
-
135% of the activity with laminarin
-
-
?
carboxymethyl pachyman + H2O
?
show the reaction diagram
G9M5R4
9.1% of the activity with laminarin
-
-
?
carboxymethyl pachyman + H2O
?
show the reaction diagram
Delftia tsuruhatensis MV01
-
135% of the activity with laminarin
-
-
?
carboxymethyl-cellulose + H2O
?
show the reaction diagram
-
carboxymethyl-cellulose is only hydrolyzed by YlCrh1Sp
-
-
?
carboxymethyl-curdlan + H2O
?
show the reaction diagram
O68641
-
-
-
?
carboxymethylated curdlan + H2O
?
show the reaction diagram
Q70C53, -
-
-
-
?
carboxymethylated pachyman + H2O
D-glucose + ?
show the reaction diagram
-
14% of activity compared to laminaran from Laminaria cichorioides
-
-
?
carboxymethylated pachyman + H2O
D-glucose + ?
show the reaction diagram
-
24% of activity compared to laminaran from Laminaria cichorioides
-
-
?
carboxymethylated pachyman + H2O
D-glucose + ?
show the reaction diagram
Eulota maakii
-
7% of activity compared to laminaran from Laminaria cichorioides
-
-
?
carboxymethylated pachyman + H2O
oligoglucosides
show the reaction diagram
-
86% of activity compared to laminarin from Laminaria digitata
-
-
?
carboxymethylated pachyman + H2O
?
show the reaction diagram
Q70C53, -
-
-
-
?
carboxymethylcellulose + H2O
?
show the reaction diagram
-
-
-
-
?
carboxymethylcellulose + H2O
?
show the reaction diagram
C6GFH7, -
-
-
-
?
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
-
-
-
?
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
-
from yeast
-
?
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
-
from yeast
-
?
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
-
from different fungi, containing beta-1,3-, beta-1,4 and/or beta-1,6-linkages
-
?
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
-
putative role during cell wall morphogenesis
-
?
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
-
from yeast and different fungi, slight activity, involvement in mycoparasitism
-
-
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
-
involved in modification and limited degradation of the cell wall during cell life cycle
-
?
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
-
from Phytophthora megasperma, carbohydrate release to elicit glyceollin accumulation in cotyledons
-
-
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
-
from fungi
-
?
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
-
from Fusarium oxysporum f. sp. apii, possible inducible antimicrobial defense system in plants
-
?
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
Rhizopus sp.
-
living yeast cells
-
?
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
Flavobacterium dormitator
-
living yeast cells
-
?
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
Fungi imperfecti
-
living yeast cells
-
?
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
-
cell wall autolysis
-
?
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
-
cell wall autolysis
-
?
chitin + H2O
?
show the reaction diagram
Paenibacillus sp., Paenibacillus sp. BCRC
Q000P7
-
-
-
?
curdlan + H2O
?
show the reaction diagram
-
-
-
-
?
curdlan + H2O
?
show the reaction diagram
-
-
-
-
?
curdlan + H2O
?
show the reaction diagram
-
-
-
?
curdlan + H2O
?
show the reaction diagram
-
-
-
-
?
curdlan + H2O
?
show the reaction diagram
Q9L816, -
-
-
-
?
curdlan + H2O
?
show the reaction diagram
Q000P7
-
-
-
?
curdlan + H2O
?
show the reaction diagram
-
from Alcaligenes faecalis, insoluble reduced 1,3-beta-glucan
-
?
curdlan + H2O
?
show the reaction diagram
-
insoluble reduced 1,3-beta-glucan
-
?
curdlan + H2O
?
show the reaction diagram
G9M5R4
9.1% of the activity with laminarin
-
-
?
curdlan + H2O
?
show the reaction diagram
-
-
-
-
?
curdlan + H2O
D-glucose + laminaritriose + laminaribiose
show the reaction diagram
-
-
-
-
?
insoluble yeast glucan + H2O
?
show the reaction diagram
-
-
-
-
?
laminaran + H2O
?
show the reaction diagram
Littorina kurila
-
-
-
-
?
laminaran + H2O
?
show the reaction diagram
Q4FCS2
-
-
-
?
laminaran from Laminaria cichorioides + H2O
D-glucose + ?
show the reaction diagram
-
-
glucose content in products about 33%, retention of the glycoside bond configuration
-
?
laminaran from Laminaria cichorioides + H2O
D-glucose + ?
show the reaction diagram
-
-
glucose content in products about 40%
-
?
laminaran from Laminaria cichorioides + H2O
D-glucose + ?
show the reaction diagram
Eulota maakii
-
-
glucose content in products about 90%
-
?
laminariheptaose + H2O
?
show the reaction diagram
-
-
-
-
?
laminariheptaose + H2O
?
show the reaction diagram
Cellulosimicrobium cellulans, Cellulosimicrobium cellulans DK-1
-
-
-
-
?
laminarihexaose + H2O
?
show the reaction diagram
-
-
-
-
?
laminarihexaose + H2O
?
show the reaction diagram
Flavobacterium dormitator
-
-
-
-
-
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
-
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
A4PHQ5, -
-
-
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
-
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
-
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
-
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
-
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
-
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
-
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
-
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
-
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
-
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
-
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
-
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
Fungi imperfecti
-
-
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
O68641
-
-
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
preferred substrate
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
from Laminaria digitata, lower rates are from Laminaria hyperborea and Eisenia bicyclis, best substrates are unbranched (1-3)-beta-D-glucans
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
highly specific to hydrolyse beta-1,3-glycosidic bonds
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
highly specific to hydrolyse beta-1,3-glycosidic bonds
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
best substrate, specific for for 1,3-beta-glucans in which 1,6-beta-linkages are present
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
release of laminaritetraose, laminaritriose, laminaribiose and glucose
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
end-products are laminarihexaose to laminaritriose, some glucose and little gentiobiose for lytic beta-(1-3)-glucanase I
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
accumulation of the enzyme after inoculation with fungi, involvement in pathogenesis in relation to active plant defense
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
accumulation of the enzyme after inoculation with fungi, involvement in pathogenesis in relation to active plant defense
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
soluble laminarin, no glucose release
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
end-products are laminaritriose, laminaribiose and glucose
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
product distribution consistent of 20% laminaribiose, 30% laminaritriose and 50% higher oligosaccharides
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
strong substrate affinity
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
specifically hydrolyzes (1-3)-beta-glycosidic linkages, predominant products are laminaribiose and laminaritriose, minor amounts of glucose and higher oligosaccharides
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
specifically hydrolyzes (1-3)-beta-glycosidic linkages, predominant products are laminaribiose and laminaritriose, minor amounts of glucose and higher oligosaccharides
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
lower activity than on mycolaminarin
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
hydrolysis at highest rates by isoform GI, lower hydrolysis by isoform GII, enzyme requires a long run of contiguous beta-1,3-D-glucosidic linkages, where glucosyl units neither substituted nor branched
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
functional opportunities to inhibit the advance of pathogenic fungi
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
major products are glucose, laminaribiose, laminaritriose, laminaritetraose and higher liminarioligosaccharides
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
major products are glucose, laminaribiose, laminaritriose, laminaritetraose and higher liminarioligosaccharides
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
Flavobacterium dormitator
-
major products are glucose, laminaribiose, laminaritriose, laminaritetraose and higher liminarioligosaccharides
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
release of laminarisaccharides with polymerization degree from 1-7
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
Rhizopus sp.
-
action of enzyme requires oligomers with glucose units more than 9
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
very active against substrates containing beta-1,3-linkages, mainly disaccharides and oligosaccharides produced, involvement in mycoparasitism
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
specifically hydrolyzes beta-1,3-bonds, final products are glucose, laminaribiose and laminaritetraose
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
Sclerotium glucanicum
-
specifically hydrolyzes beta-1,3-bonds, final products are glucose, laminaribiose and laminaritetraose
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
different product patterns for glucanases I, IIIB, IV and V
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
soluble reduced 1,3-beta-glucan, release of reducing 1,3-beta-oligosaccharides of variable size, presence of a single 1,6-beta branched glucose every three glucose units of a linear 1,3-beta-glucan chain prevents hydrolysis
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
highest rates from Laminaria digitata, major products are laminaribiose and laminaritriose for isoforms GII and GIII, GI yields predominantly (1-3)-beta-D-oligoglucosides greater than 4 units
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
major products are laminaribiose and laminaritriose
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
devoid of debranching activity, depolymerizes the unbranched portions of the beta-(1-3), beta-(1-6)-glucan, down to laminaritriose, retaining the anomeric configuration
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
only active against glucans containing beta-1,3-linkages
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
100% activity
-
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
reducing sugar + ?
show the reaction diagram
Hypocrea koningii ALL 13
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
O73951
-
-
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
Q9L816, -
-
-
-
?
laminarin + H2O
?
show the reaction diagram
Q70C53, -
-
-
-
?
laminarin + H2O
?
show the reaction diagram
Q000P7
-
-
-
?
laminarin + H2O
?
show the reaction diagram
C1IE32, -
-
-
-
?
laminarin + H2O
?
show the reaction diagram
C3VPJ1
-
-
-
?
laminarin + H2O
?
show the reaction diagram
A6YQV6
-
-
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
-
best substrate
-
-
?
laminarin + H2O
?
show the reaction diagram
-, Q59328
13% of activity compared to barley beta-glucan
-
-
?
laminarin + H2O
?
show the reaction diagram
C3VPJ1
1,3-beta-glucose monomers, best substrate
-
-
?
laminarin + H2O
?
show the reaction diagram
C6GFH7, -
substrate from Laminaria digitata
-
-
?
laminarin + H2O
?
show the reaction diagram
-
main linkage type beta-1,3-(Glc). The enzyme cleaves laminarin randomly, yielding glucose, laminaribiose, and higher laminari-oligosaccharides
-
-
?
laminarin + H2O
?
show the reaction diagram
Thermobifida fusca YX-ER1
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
Paenibacillus sp. BCRC
Q000P7
-
-
-
?
laminarin + H2O
?
show the reaction diagram
Hypocrea lixii Rifai T24
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
Cellulosimicrobium cellulans DK-1
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
Clostridium thermocellum F7
Q59328
13% of activity compared to barley beta-glucan
-
-
?
laminarin + H2O
glucose + laminaribiose + ?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
laminaribiose + laminaritriose + laminaritetraose
show the reaction diagram
Saccharomyces cerevisiae, Schizosaccharomyces pombe, Saccharomyces cerevisiae YPA84
-
-
main reaction products
-
?
laminarin + H2O
D-glucose + laminaribiose
show the reaction diagram
-
more specific for compounds having beta-1,3-glucosidic linkages
-
-
?
laminarin + H2O
D-glucose + laminarioligosaccharides
show the reaction diagram
-
-
-
-
?
laminarin + H2O
D-glucose + laminarioligosaccharides
show the reaction diagram
-
-
-
-
?
laminarin + H2O
D-glucose + laminarioligosaccharides
show the reaction diagram
G9M5R4
endolytic depolymerization of glucans composed of beta-1,3-linked main chains
-
-
?
laminarin + H2O
D-glucose + laminarioligosaccharides
show the reaction diagram
Delftia tsuruhatensis MV01
-
-
-
-
?
laminarin + H2O
D-glucose + laminarioligosaccharides
show the reaction diagram
Gecarcoidea natalis Pocock 1888
-
-
-
-
?
laminarin + H2O
laminaritriose
show the reaction diagram
Q000P7
preferred substrate
main product
-
?
laminarin + H2O
laminaribiose + beta-D-glucose
show the reaction diagram
-
-
-
-
?
laminarin + H2O
laminaribiose + beta-D-glucose
show the reaction diagram
C6L684, -
-
-
-
?
laminarin + H2O
D-glucose + laminaribiose + laminaritriose
show the reaction diagram
C1IE32, -
CaLam digests laminarin and laminarioligosaccharides except laminaribiose as an endo-beta-1,3-glucanase, releasing glucose, laminaribiose and laminaritriose as the major products
-
-
?
laminarin + H2O
D-glucose + glucooligosaccharides
show the reaction diagram
-
-
if the degree of cleavage of laminarin under exhaustive hydrolysis reaches 74%, the major products are glucose and di-, tri-, and tetrasaccharides
-
?
laminarin + H2O
glucose + laminaribiose + laminaritriose
show the reaction diagram
A5IL44, -
-
major products, enzyme most frequently attacks the bond between the 3rd and 4th residue from the non-reducing end
-
?
laminarin + H2O
glucose + laminaribiose + laminaritriose
show the reaction diagram
A5IL44
-
major products, enzyme most frequently attacks the bond between the 3rd and 4th residue from the non-reducing end
-
?
laminarin from Eisenia bicyclis + H2O
oligoglucosides
show the reaction diagram
-
9% of activity compared to laminarin from Laminaria digitata
-
-
?
laminarin from Laminaria digitata + H2O
oligoglucosides
show the reaction diagram
-
-
mixture with different chain length
-
?
laminarioligosaccharide + H2O
laminaribiose + beta-D-glucose
show the reaction diagram
C6L684, -
-
-
-
?
laminarioligosaccharide + H2O
laminaribiose + beta-D-glucose
show the reaction diagram
C6L684, -
substrate specificities and products, overview
-
-
?
laminarioligosaccharide + H2O
laminaribiose + beta-D-glucose
show the reaction diagram
-
e.g. laminaritetraose
-
-
?
laminarioligosaccharide + H2O
D-glucose + laminaribiose + laminaritriose
show the reaction diagram
C1IE32, -
CaLam digests laminarin and laminarioligosaccharides except laminaribiose as an endo-beta-1,3-glucanase, releasing glucose, laminaribiose and laminaritriose as the major products
-
-
?
laminaripentaose + H2O
?
show the reaction diagram
-
-
-
-
?
laminaripentaose + H2O
?
show the reaction diagram
Cellulosimicrobium cellulans, Cellulosimicrobium cellulans DK-1
-
-
-
-
?
laminaripentaose + H2O
D-glucose + laminaritriose + laminaribiose
show the reaction diagram
-
more specific for compounds having beta-1,3-glucosidic linkages
-
-
?
laminaritetraose + H2O
?
show the reaction diagram
-
-
-
-
?
laminaritetraose + H2O
?
show the reaction diagram
-
-
-
-
?
laminaritetraose + H2O
?
show the reaction diagram
-
smallest substrate accepted
-
-
?
laminaritetraose + H2O
D-glucose + ?
show the reaction diagram
-
more specific for compounds having beta-1,3-glucosidic linkages
-
-
?
laminaritriose + H2O
D-glucose + ?
show the reaction diagram
-
more specific for compounds having beta-1,3-glucosidic linkages
-
-
?
lentinan + H2O
?
show the reaction diagram
G9M5R4
4.4% of the activity with laminarin
-
-
?
lichenan + H2O
?
show the reaction diagram
O73951
-
-
-
?
lichenan + H2O
?
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
Q9L816, -
-
-
-
?
lichenan + H2O
?
show the reaction diagram
Q70C53, -
-
-
-
?
lichenan + H2O
?
show the reaction diagram
Q000P7
-
-
-
?
lichenan + H2O
?
show the reaction diagram
A5IL44, -
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-, Q59328
90% of activity compared to barley beta-glucan
-
-
?
lichenan + H2O
?
show the reaction diagram
-
lichenan is only hydrolyzed by YlCrh1Sp
-
-
?
lichenan + H2O
?
show the reaction diagram
C3VPJ1
1,3-1,4-beta-glucose monomers, high activity
-
-
?
lichenan + H2O
?
show the reaction diagram
C6GFH7, -
substrate from Cetraria islandica
-
-
?
lichenan + H2O
?
show the reaction diagram
-
main linkage type beta-1,3-1,4(Glc), about 10% of the specific activity compared to laminarin
-
-
?
lichenan + H2O
?
show the reaction diagram
Thermobifida fusca YX-ER1
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
Paenibacillus sp. BCRC
Q000P7
-
-
-
?
lichenan + H2O
?
show the reaction diagram
A5IL44
-
-
-
?
lichenan + H2O
?
show the reaction diagram
Clostridium thermocellum F7
Q59328
90% of activity compared to barley beta-glucan
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
-
?
lichenan + H2O
D-glucose + ?
show the reaction diagram
O68641
-
-
-
?
lichenan + H2O
D-glucose + ?
show the reaction diagram
Eulota maakii
-
16% of activity compared to laminaran from Laminaria cichorioides
-
-
?
lichenan + H2O
D-glucose + ?
show the reaction diagram
-
20% of activity compared to laminaran from Laminaria cichorioides
-
-
?
lichenan + H2O
D-glucose + ?
show the reaction diagram
-
22% of activity compared to laminaran from Laminaria cichorioides
-
-
?
mycolaminarin + H2O
reducing sugar
show the reaction diagram
-
highest activity
no glucose release, approximately four glycosidic linkages hydrolyzed per molecule mycolaminarin, predominant product are tetrasaccharides
?
O-carboxymethyl-(1,3:1,6)-beta-D-glucan + H2O
?
show the reaction diagram
-
from yeast, low activity
-
?
O-carboxymethyl-(1,3:1,6)-beta-D-glucan + H2O
?
show the reaction diagram
-
from yeast, low activity
-
?
O-carboxymethyl-pachyman + H2O
?
show the reaction diagram
-
-
-
?
O-carboxymethyl-pachyman + H2O
?
show the reaction diagram
-
-
-
?
O-carboxymethyl-pachyman + H2O
?
show the reaction diagram
-
preferred substrate
-
?
O-carboxymethyl-pachyman + H2O
?
show the reaction diagram
-
faster hydrolysis by isoform GII than by isoform GI, isoform GII may play a role in response to fungal infection
-
?
O-carboxymethyl-pachyman + H2O
?
show the reaction diagram
-
release of laminarisaccharides ranging in polymerization degree from 1-7
-
?
O-carboxymethyl-pachyman + H2O
?
show the reaction diagram
-
rate of hydrolysis decreases as degree of substitutions increases, requirement for three unsubstituted beta-1,3-glycosyl residues
-
?
O-carboxymethyl-pachyman + H2O
?
show the reaction diagram
-
unbranched (1-3)-beta-glucan from Poria cocos
-
?
oat glucan + H2O
?
show the reaction diagram
-
15% activity compared to laminarin
-
-
?
pachyman + H2O
?
show the reaction diagram
-
-
-
?
pachyman + H2O
?
show the reaction diagram
-
-
-
?
pachyman + H2O
?
show the reaction diagram
-
-
-
-
?
pachyman + H2O
?
show the reaction diagram
-
-
-
?
pachyman + H2O
?
show the reaction diagram
Flavobacterium dormitator
-
-
-
?
pachyman + H2O
?
show the reaction diagram
Fungi imperfecti
-
-
-
?
pachyman + H2O
?
show the reaction diagram
-
-
-
-
?
pachyman + H2O
?
show the reaction diagram
-
-
-
-
?
pachyman + H2O
?
show the reaction diagram
Q9L816, -
-
-
-
?
pachyman + H2O
?
show the reaction diagram
Q000P7
-
-
-
?
pachyman + H2O
?
show the reaction diagram
-
low activity
-
?
pachyman + H2O
?
show the reaction diagram
-
release of laminarisaccharides in polymerization degree form 1-7
-
?
pachyman + H2O
?
show the reaction diagram
-
insoluble pachyman, more affinity than on soluble, short-chain pachyman, forms L-1 and L-2 release predominantly pentaose, form L-4 yields a mixture from biose to heptaose
-
?
pachyman + H2O
?
show the reaction diagram
C6GFH7, -
substrate from Poria cocos
-
-
?
pachyman + H2O
?
show the reaction diagram
G9M5R4
14.9% of the activity with laminarin
-
-
?
pachyman + H2O
?
show the reaction diagram
Thermobifida fusca YX-ER1
-
-
-
-
?
pachyman + H2O
?
show the reaction diagram
-
-
-
-
?
pachyman + H2O
D-glucose + ?
show the reaction diagram
-
10% of activity compared to laminaran from Laminaria cichorioides
-
-
?
pachyman + H2O
D-glucose + ?
show the reaction diagram
-
13% of activity compared to laminaran from Laminaria cichorioides
-
-
?
pendulan + H2O
reducing sugar + ?
show the reaction diagram
-
acts in random fashion, reaction product with high molecular weight, major role in decreasing the molecular weight of pendulan during fermentation
-
?
periodate-oxidized laminaran + H2O
D-glucose + ?
show the reaction diagram
Eulota maakii
-
0.5% of activity compared to laminaran from Laminaria cichorioides
-
-
?
periodate-oxidized laminaran + H2O
D-glucose + ?
show the reaction diagram
-
85% of activity compared to laminaran from Laminaria cichorioides
-
-
?
periodate-oxidized laminaran + H2O
D-glucose + ?
show the reaction diagram
-
90% of activity compared to laminaran from Laminaria cichorioides
-
-
?
periodate-oxidized laminaran + H2O
?
show the reaction diagram
Littorina kurila
-
95% of the rate with laminaran
-
-
?
periodate-oxidized laminarin + H2O
?
show the reaction diagram
-
-
-
?
periodate-oxidized laminarin + H2O
?
show the reaction diagram
-
-
-
?
periodate-oxidized laminarin + H2O
?
show the reaction diagram
-
-
-
?
periodate-oxidized laminarin + H2O
?
show the reaction diagram
-
-
-
?
periodate-oxidized laminarin + H2O
?
show the reaction diagram
-
-
-
?
periodate-oxidized laminarin + H2O
?
show the reaction diagram
Flavobacterium dormitator
-
-
-
?
periodate-oxidized laminarin + H2O
?
show the reaction diagram
-
100% of the activity with laminarin
-
-
?
polysaccharide + H2O
ethanol-soluble sugar + ?
show the reaction diagram
-
crude fraction from unripe bananas, not active in polysaccharide fraction from ripe bananas, possible involvement in ripening and/or softening process
-
?
pustulan + H2O
?
show the reaction diagram
-
beta-1,6-glucan, low activity
-
?
pustulan + H2O
?
show the reaction diagram
-
beta-1,6-glucan, low activity
-
?
pustulan + H2O
?
show the reaction diagram
-
beta-1,6-glucan, low activity
-
?
pustulan + H2O
?
show the reaction diagram
-
enzyme can also cleave beta-1,6 glucans
-
-
?
pustulan + H2O
?
show the reaction diagram
-
4% activity compared to laminarin
-
-
?
pustulan + H2O
?
show the reaction diagram
-
pustulan is only hydrolyzed by YlCrh1Sp
-
-
?
reduced laminarihexaose + H2O
?
show the reaction diagram
-
-
-
-
?
reduced laminarioligosaccharide + H2O
?
show the reaction diagram
-
19 glucose units
-
-
?
reduced laminarioligosaccharides + H2O
laminaribiose + laminaritriose + laminaritetraose + laminaripentaose
show the reaction diagram
-
velocity of catalytic reaction increases with the number of 1,3-beta-glucosidic bonds, preferentially cleaves between the glucose residues at positions 2 and 3 from the reducing end
-
?
schizophyllan + H2O
?
show the reaction diagram
-
low activity
-
?
schizophyllan + H2O
?
show the reaction diagram
-
from Schizophyllum commune, low activity
-
?
schizophyllan + H2O
?
show the reaction diagram
-
from Schizophyllum commune, low activity
-
?
scleroglucan + H2O
?
show the reaction diagram
Sclerotium glucanicum
-
low activity
-
?
short-chain pachyman + H2O
?
show the reaction diagram
-
low affinity
-
?
translam + H2O
?
show the reaction diagram
Littorina kurila
-
86% of the rate with laminaran
-
-
?
translam + H2O
?
show the reaction diagram
-
32.1% of the activity with laminarin
-
-
?
zymosan A + H2O
?
show the reaction diagram
-
-
-
-
?
zymosan A + H2O
?
show the reaction diagram
Q9L816, -
-
-
-
?
zymosan A + H2O
?
show the reaction diagram
O68641
-
-
-
?
zymosan A + H2O
?
show the reaction diagram
Q000P7
-
-
-
?
lichenin from Cetraria islandica + H2O
oligoglucosides
show the reaction diagram
-
6% of activity compared to laminarin from Laminaria digitata
-
-
?
additional information
?
-
-
enzyme hydrolyzes soluble and insoluble (1-3)-beta-D-glucan chains
-
-
-
additional information
?
-
-
no substrate: cellulose, xylan, amylose
-
-
-
additional information
?
-
Eulota maakii
-
no substrate: pachyman, p-nitrophenyl-beta-D-glucopyranoside
-
-
-
additional information
?
-
-
no substrate: starch, cellulose, chitin, chitosan
-
-
-
additional information
?
-
Q9L816, -
no substrates : cellulose, xylan, amylose, starch, beta-cyclodextrin
-
-
-
additional information
?
-
-
specifically cleaves beta-1,3-linkages in polysaccharides
-
-
-
additional information
?
-
-
besides endo-activity, enzyme has some exo-activity, and catalyzes hydrolysis of mixed-linked oligosaccharides with both beta-1,3 and beta-1,4 specificities
-
-
-
additional information
?
-
-
no substrate: pustulan, p-nitrophenyl-beta-D-glucopyranoside
-
-
-
additional information
?
-
Q9SXY6, Q9SXY8
OsGlu1 may act in the defense response to pathogen attack
-
-
-
additional information
?
-
-
laminaribiose and laminaritriose are no substrates, laminaritetraose is very inefficiently cleaved
-
-
-
additional information
?
-
-
no activity towards chitosan, lichenan, carboxymethylcellulose, amylose, and p-nitrophenyl beta-D-glucopyranoside
-
-
-
additional information
?
-
-
YlCrh2Sp does not hydrolyze carboxymethyl-cellulose, pustulan, and lichenan
-
-
-
additional information
?
-
-
role as a regulator for the acid trehalase activity by association in the enzyme aggregate
-
-
-
additional information
?
-
Q000P7
the catalytic module has an inhibitory effect on the growth of Candida albicans and Rhizoctonia solani. The presence of the carbohydrate-binding module and the analogue of coagulation factor Fa5/8C enhance the inhibitory effect
-
-
-
additional information
?
-
-
enzyme does not hydrolyze beta-1,4 linkages present in cellooligosaccharides such as cellobiose, cellotriose, cellotetraose and cellopentaose
-
-
-
additional information
?
-
-
laminarinase mainly hydrolyses beta?1,3-glycosidic bonds, with negligible activity towards beta-1,4-glycosidic bonds
-
-
-
additional information
?
-
Littorina kurila
-
narrow substrate specificity, hydrolyzes only the (1-3)-beta-D-glucosidic bonds in the mixed (1-3),(1-6)- and (1-3),(1-4)-beta-D-glucans down to glucose and glucooligosaccharides. Enzyme acts with retention of the anomeric configuration and additionally catalyzes transglycosylation reactions
-
-
-
additional information
?
-
Q000P7
the catalytic module specifically hydrolyzes beta-1,3- and beta-1,3-1,4-glucan. The catalytic module has an inhibitory effect on the growth of Candida albicans and Rhizoctonia solani. The presence of the carbohydrate-binding module and the analogue of coagulation factor Fa5/8C enhance the inhibitory effect
-
-
-
additional information
?
-
C3VPJ1
BglS27 preferentially catalyzes the hydrolysis of glucans with a beta-1,3-linkage using an endolytic mode of action
-
-
-
additional information
?
-
C6GFH7, -
the enzyme is an endoglucanase that hydrolyzes beta-1,3-glucans as laminarin and yeast beta-1,3-1,6-glucan, but is inactive toward other polysaccharides, e.g. unbranched beta-1,3-glucans or mixed beta-1,3-1,4-glucan from cereals, or disaccharides
-
-
-
additional information
?
-
-
AkLam36 specific for beta-1,3-glucosyl linkages. AkLam36 is an endolytic enzyme degrading laminarin and laminarioligosaccharides to laminaritriose, laminaribiose, and D-glucose. AkLam36 shows higher activity toward beta-1,3-glucans with a few beta-1,6-linked glucose branches such as Laminaria digitata laminarin than highly branched beta-1,3-glucans such as Eisenia bicyclis laminarin
-
-
-
additional information
?
-
C6L684, -
HdLam33 possesses transglycosylation activity splitting glycoside linkage in a retaining manner, overview. It also shows activity of EC 3.2.1.6, endo-1,3(4)-beta-glucanase
-
-
-
additional information
?
-
C3VPJ1
no activity with oat spelt xylan and carboxymethyl cellulose
-
-
-
additional information
?
-
-
substrate specificities of wild-type and mutant enzymes, overview
-
-
-
additional information
?
-
-
enzyme is involved in the autolytic cell wall degradation resulting from carbon starvation of the fungus and liberates reducing sugars from cell debris
-
-
-
additional information
?
-
-
enzyme cleaves cell wall debris of yeast Pichia fermentans, Zygosaccharomyces bailii, Saccharomycodes ludwigii, Dekkera bruxellensis. No substrate: xylan, pustulan, carboxymethyl cellulose, dextran
-
-
-
additional information
?
-
-
enzyme preferentially acts on soluble beta-1,3-glucans. Additional transferase activity for oligosaccharides of a low degree of polymerization
-
-
-
additional information
?
-
A6YQV6
Enzyme shows low processivity of 0.4. No substrate: yeast beta-1,3-1,6-glucan or other polysaccharides. enzyme is unable to lyse Saccharomyces cerevisiae cells
-
-
-
additional information
?
-
G9M5R4
no substrate: beta-1,3-1,4-glucans such as barley glucan or lichenan, or beta-1,6 glucans such as pustulan
-
-
-
additional information
?
-
-
no substrate: laminaribiose or laminaritriose, carboxymethyl cellulose, chitin, and pustulan
-
-
-
additional information
?
-
-
poor substrates: yeast glucan, pachyman, amylopectin, carboxymethy cellulose, and pustulan
-
-
-
additional information
?
-
A5IL44, -
specific cleavage of internal beta-1,3-bonds. No substrate: avicel, carboxymethyl cellulose and cellopentaose, xylan, arabinan and manan containing polysaccharides
-
-
-
additional information
?
-
-
no activity with cellulose, xylan and chitin
-
-
-
additional information
?
-
Thermobifida fusca YX-ER1
-
substrate specificities of wild-type and mutant enzymes, overview
-
-
-
additional information
?
-
Hypocrea lixii Rifai T24
-
specifically cleaves beta-1,3-linkages in polysaccharides
-
-
-
additional information
?
-
Saccharomyces cerevisiae YPA84
-
laminaribiose and laminaritriose are no substrates, laminaritetraose is very inefficiently cleaved
-
-
-
additional information
?
-
Cellulosimicrobium cellulans DK-1
-
no substrate: laminaribiose or laminaritriose, carboxymethyl cellulose, chitin, and pustulan
-
-
-
additional information
?
-
Delftia tsuruhatensis MV01
-
enzyme cleaves cell wall debris of yeast Pichia fermentans, Zygosaccharomyces bailii, Saccharomycodes ludwigii, Dekkera bruxellensis. No substrate: xylan, pustulan, carboxymethyl cellulose, dextran
-
-
-
additional information
?
-
A5IL44
specific cleavage of internal beta-1,3-bonds. No substrate: avicel, carboxymethyl cellulose and cellopentaose, xylan, arabinan and manan containing polysaccharides
-
-
-
additional information
?
-
Gecarcoidea natalis Pocock 1888
-
laminarinase mainly hydrolyses beta?1,3-glycosidic bonds, with negligible activity towards beta-1,4-glycosidic bonds
-
-
-
additional information
?
-
-
the catalytic module has an inhibitory effect on the growth of Candida albicans and Rhizoctonia solani. The presence of the carbohydrate-binding module and the analogue of coagulation factor Fa5/8C enhance the inhibitory effect, the catalytic module specifically hydrolyzes beta-1,3- and beta-1,3-1,4-glucan. The catalytic module has an inhibitory effect on the growth of Candida albicans and Rhizoctonia solani. The presence of the carbohydrate-binding module and the analogue of coagulation factor Fa5/8C enhance the inhibitory effect
-
-
-
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
alkali soluble 1,3-beta-glucan + H2O
reducing sugar + ?
show the reaction diagram
-
produced by solubilised 1,3-beta-glucan synthase complex of A. fumigatus
-
?
beta-1,3-glucan + H2O
laminaribiose + D-glucose
show the reaction diagram
B4XEK5
-
-
-
?
beta-1,3-glucan + H2O
laminaribiose + D-glucose
show the reaction diagram
B4XEK7
-
-
-
?
beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
beta-glucan + H2O
?
show the reaction diagram
Trichoderma sp., Trichoderma asperellum
-
-
-
-
?
callose + H2O
?
show the reaction diagram
Q02126
-
-
-
?
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
-
-
-
?
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
-
from yeast
-
?
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
-
from yeast
-
?
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
-
from different fungi, containing beta-1,3-, beta-1,4 and/or beta-1,6-linkages
-
?
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
-
putative role during cell wall morphogenesis
-
?
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
-
from yeast and different fungi, slight activity, involvement in mycoparasitism
-
-
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
-
involved in modification and limited degradation of the cell wall during cell life cycle
-
?
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
-
from Phytophthora megasperma, carbohydrate release to elicit glyceollin accumulation in cotyledons
-
-
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
-
from fungi
-
?
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
-
from Fusarium oxysporum f. sp. apii, possible inducible antimicrobial defense system in plants
-
?
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
Rhizopus sp.
-
living yeast cells
-
?
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
Flavobacterium dormitator
-
living yeast cells
-
?
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
Fungi imperfecti
-
living yeast cells
-
?
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
-
cell wall autolysis
-
?
cell wall glucan + H2O
reducing sugar + ?
show the reaction diagram
-
cell wall autolysis
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
-
?
laminarin + H2O
?
show the reaction diagram
Q000P7
-
-
-
?
laminarin + H2O
?
show the reaction diagram
C1IE32, -
-
-
-
?
laminarin + H2O
?
show the reaction diagram
C3VPJ1
-
-
-
?
laminarin + H2O
laminaribiose + beta-D-glucose
show the reaction diagram
C6L684, -
-
-
-
?
laminarin + H2O
?
show the reaction diagram
Paenibacillus sp. BCRC
Q000P7
-
-
-
?
pendulan + H2O
reducing sugar + ?
show the reaction diagram
-
acts in random fashion, reaction product with high molecular weight, major role in decreasing the molecular weight of pendulan during fermentation
-
?
polysaccharide + H2O
ethanol-soluble sugar + ?
show the reaction diagram
-
crude fraction from unripe bananas, not active in polysaccharide fraction from ripe bananas, possible involvement in ripening and/or softening process
-
?
laminarioligosaccharide + H2O
laminaribiose + beta-D-glucose
show the reaction diagram
C6L684, -
substrate specificities and products, overview
-
-
?
additional information
?
-
Q9SXY6, Q9SXY8
OsGlu1 may act in the defense response to pathogen attack
-
-
-
additional information
?
-
-
role as a regulator for the acid trehalase activity by association in the enzyme aggregate
-
-
-
additional information
?
-
Q000P7
the catalytic module has an inhibitory effect on the growth of Candida albicans and Rhizoctonia solani. The presence of the carbohydrate-binding module and the analogue of coagulation factor Fa5/8C enhance the inhibitory effect
-
-
-
additional information
?
-
C3VPJ1
BglS27 preferentially catalyzes the hydrolysis of glucans with a beta-1,3-linkage using an endolytic mode of action
-
-
-
additional information
?
-
C6GFH7, -
the enzyme is an endoglucanase that hydrolyzes beta-1,3-glucans as laminarin and yeast beta-1,3-1,6-glucan, but is inactive toward other polysaccharides, e.g. unbranched beta-1,3-glucans or mixed beta-1,3-1,4-glucan from cereals, or disaccharides
-
-
-
additional information
?
-
-
enzyme is involved in the autolytic cell wall degradation resulting from carbon starvation of the fungus and liberates reducing sugars from cell debris
-
-
-
additional information
?
-
-
the catalytic module has an inhibitory effect on the growth of Candida albicans and Rhizoctonia solani. The presence of the carbohydrate-binding module and the analogue of coagulation factor Fa5/8C enhance the inhibitory effect
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ba2+
-
increases activity
Ca2+
-
slight activation at 2 mM
Ca2+
-
3fold activation at 50 mM
Ca2+
-
nearly 3fold activation at 5 mM
Ca2+
-
one calcium ion is bound on the convex face of the protein, suggesting to play a role in stabilizing the protein structure
Ca2+
-
contains one calcium ion for each monomer. The calcium ion is located on the opposite side with respect to the catalytic cleft; one ion per monomer, crystallization data
Ca2+
-
bound to the enzyme. Calcium binding results in relatively small chemical shift changes in a region distant from the active site of pfLamA and thus causes only minor conformational modifications. Removal of calcium does not significantly alter the denaturation temperature of pfLamA, implying that calcium does not stabilize the enzyme against global unfolding
Co2+
-
increases activity
Co2+
C3VPJ1
14.1% activation at 1 mM, 30% at 5 mM
Hg2+
-
42% residual activity at 1 mM HgCl2
K3Fe(CN)6
Rhizopus sp.
-
activation on hydrolysis of laminarin, not on lytic activity of living yeast cells
Mg2+
-
replaces activation by Ca2+
Mg2+
-
3.5fold activation at 5 mM
Mg2+
Flavobacterium dormitator
-
15% activation at 1 mM
Mn2+
-
224% activation at 1 mM
Mn2+
C3VPJ1
20.4% activation at 1 mM
Na+
-
50% increasing activity at 300 mM for form EG-1, activity of form EG-2A not enhanced
Na+
-
slight activation at 5 mM
Zn2+
-
slight activation at 2 mM
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
(2,3)-epoxypropyl beta-D-laminaribiose
-
number of glucosyl residues in the inhibitor affects aglycon chain length specificity and correct positioning of the substrate at the active site
1-ethyl-3(-dimethylaminopropyl)carbodiimide
-
85% residual activity at 10 mM (pH 5.0)
2-Hydroxy-5-nitrobenzylbromide
-
inhibition at 10 mM
2-mercaptoethanol
-
1 mM concentration, activity loss 49%
3,4-epoxybutyl-beta-D-cellobioside
-
-
4-chloromercuribenzoate
-
strong inhibition at 1 mM
4-chloromercuribenzoate
-
45% inhibition at 1 mM
4-chloromercuribenzoate
Flavobacterium dormitator
-
45% inhibition at 1 mM
4-chloromercuribenzoate
Rhizopus sp.
-
slight inhibition on laminarin hydrolysis, strong inhibition on disruption of living cells
AgNO3
-
complete inhibition at 1 mM
AgNO3
Rhizopus sp.
-
inhibition on both laminarin hydrolysis and disruption of living yeast cells
AgNO3
-
inhibition at 1 mM
Ca2+
-
slight inhibition at 1 mM
Ca2+
-
45% inhibition at 1 mM
Ca2+
-
slight inhibition at 1 mM
Ca2+
C3VPJ1
loss of 11.5% activity at 5 mM
carbodiimide
-
inhibition at 100 mM
Co2+
-
slight inhibition at 1 mM
Cr2(SO4)3
-
36% inhibition at 1 mM
Cr3+
C3VPJ1
loss of 11.6% activity at 5 mM
Cu2+
-
21% inhibition at 2 mM
Cu2+
-
reduced activity to 41% and 50% at 1 and 5 mM
Cu2+
-
inhibition at 1 mM
Cu2+
-
43% inhibition at 1 mM
Cu2+
-
strong inhibition at 1 mM
Cu2+
Flavobacterium dormitator
-
strong inhibition at 1 mM
Cu2+
-
55% inhibition at 1 mM
Cu2+
-
inhibition at 1 mM
Cu2+
-
inhibition at 20 mM
Cu2+
Q59328
1-5 mM, strong
Cu2+
C3VPJ1
loss of 24.4% activity at 5 mM
diethyl dicarbonate
-
complete loss of activity at 36 mM (pH 6.0)
EDTA
-
nearly complete inhibition at 1 mM
EDTA
-
40% inhibition at 1 mM
EDTA
Flavobacterium dormitator
-
nearly complete inhibition at 1 mM
EDTA
-
1 mM concentration, activity loss 28%
Fe2+
-
strong inhibition at 1 mM
-
Fe2+
Q59328
1-5 mM, strong
-
Fe2+
C3VPJ1
loss of 22.6% activity at 5 mM
-
GSSG
-
slight inhibition at 1 mM
Hexadecyltrimethylammonium bromide
-
strong inhibition at 1 mM
Hexadecyltrimethylammonium bromide
-
50% inhibition at 1 mM
Hg2+
-
52% inhibition for laminarin, 62% inhibition for pustulan
Hg2+
-
inhibition at 0.4 mM
Hg2+
-
strong inhibition at 2 mM
Hg2+
-
complete inhibition at 1 mM
Hg2+
Sclerotium glucanicum
-
inhibition at 1 mM
Hg2+
-
marked inhibition at 1 mM
Hg2+
-
marked inhibition at 1 mM
Hg2+
-
marked inhibition at 1 mM
Hg2+
Flavobacterium dormitator
-
36% inhibition at 1 mM
Hg2+
-
marked inhibition at 1 mM
Hg2+
Rhizopus sp.
-
inhibition on both laminarin hydrolysis and disruption of living yeast cells
Hg2+
-
inhibition at 1 mM
Hg2+
-
inhibition at 0.2 mM
Hg2+
-
5 mM, 93% inhibition
Hg2+
Q59328
1-5 mM, strong
Iodine
Flavobacterium dormitator
-
30% inhibition at 1 mM
Iodine
-
inhibition at 2 mM
iodoacetamide
-
slight inhibition
iodoacetamide
-
slight inhibition
K3Fe(CN)6
Flavobacterium dormitator
-
slight inhibition at 1 mM
KBr
-
slight inhibition at 1 mM
KMnO4
-
55% inhibition for laminarin, 85% inhibition for pustulan
KMnO4
Flavobacterium dormitator
-
complete inhibition at 1 mM
KMnO4
Rhizopus sp.
-
nearly complete inhibition of laminarin hydrolysis and disruption of living yeast cells
Laminarin
-
25% inhibition above 2.5 mg/ml for beta-glucanase IIIB
Laminarin
-
slight inhibition above 1 mg/ml for glucanase I, above 0.5 mg/ml inhibitory for glucanase II
Lespedeza cuneata cellulase inhibitor
-
inhibition at 0.2 mg/ml
-
Mg2+
-
slight inhibition at 1 mM
Mg2+
-
slight inhibition at 1 mM
Mg2+
Rhizopus sp.
-
inhibition on hydrolysis of laminarin, not on disruption of living yeast cells
Mn2+
-
72% inhibition at 1 mM
Mn2+
-
complete inhibition at 1 mM
Mn2+
Rhizopus sp.
-
slight inhibition in hydrolysis of laminarin, not on disruption of living yeast cells
N-Acetylimidazole
-
inhibition at 23 mM
N-bromosuccinimide
-
-
N-bromosuccinimide
-
inhibition at 5 mM
N-bromosuccinimide
-
complete loss of activity at 0.1 mM (pH 4.0)
N-ethylmaleimide
-
slight inhibition at 1 mM
Na2WO4
-
36% inhibition at 1 mM
NaAsO2
Flavobacterium dormitator
-
slight inhibition at 1 mM
NaAsO2
-
39% inhibition at 1 mM
NaN3
Flavobacterium dormitator
-
slight inhibition at 1 mM
Ni2+
Flavobacterium dormitator
-
slight inhibition at 1 mM
p-hydroxymercuribenzoate
Sclerotium glucanicum
-
strong inhibition at 1 mM
Pb2+
-
inhibition at 1 mM
Pb2+
Flavobacterium dormitator
-
59% inhibition at 1 mM
Pb2+
-
45% inhibition at 1 mM
Pb2+
Rhizopus sp.
-
inhibition on hydrolysis of laminarin, only slight inhibition in disruption of living yeast cells
Phenylmercurinitrate
-
-
Phenylmercurinitrate
-
inhibition at 2 mM
propylene oxide
-
15% residual activity at 6 M (pH 4.0)
SDS
-
43% inhibition at 2 mM
SDS
-
52% inhibition at 1 mM
SDS
-
complete inhibition at 1 mM
Semicarbazide
Flavobacterium dormitator
-
slight inhibition at 1 mM
Sn2+
-
25% inhibition at 1 mM
Sodium 7-deoxycholate
-
38% inhibition at 1 mM
Sodium 7-deoxycholate
-
55% inhibition at 1 mM
Zn2+
-
complete inhibition at 1 mM
Zn2+
Flavobacterium dormitator
-
25% inhibition at 1 mM
Zn2+
-
59% inhibition at 1 mM
Zn2+
Q59328
1-5 mM, strong
Zn2+
C3VPJ1
loss of 22.0% activity at 5 mM
Mn2+
C3VPJ1
loss of 24.2% activity at 5 mM
additional information
Q59328
not inhibitory: dithiothreitol, EDTA, ethanol up to 10%, SDS up to 20 mM, NaCl up to 50 mM
-
additional information
-
not inhibitory: glucono-delta-lactone
-
additional information
-
not inhibited by EDTA, p-chloromercuribenzoate, iodoacetamide, N-ethylmaleimide, Ellman's reagent, N-acetylimidazole, tetranitromethane, 2,4-pentanedione, and trinitrobenzolsulfonic acid
-
additional information
-
Ca2+, Cu2+,Fe3+, Mg2+, permanganate, and N-Br-succinimide have no effect on enzymatic activity
-
additional information
-
Ca2+, Cu2+, Fe3+, Mg2+, permanganate, and N-Br-succinimide have no effect on enzymatic activity
-
additional information
-
cobalt and ferric ions do not inhibit enzyme activity, ions of magnesium, zinc, copper, calcium, nickel and manganese show a remaining activity between 65 and 90%
-
additional information
C6GFH7, -
the enzyme is not inhibited by high substrate concentrations
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
C3VPJ1
9,6-10% activation at 1-5 mM
Bovine serum albumin
-
marked stimulation dependent on buffer concentration, especially at low concentration
-
Bovine serum albumin
-
-
-
NaCl
-
the optimal concentration is 0.1-0.25 M
NaCl
-
the optimal concentration is 0.01-0.3 M
Sodium diethyldithiocarbamate
Flavobacterium dormitator
-
10% activation at 1 mM
sodium salicylate
-
increases induction of both intracellular and extracellular beta 1,3-glucanases in calli
-
Trypsin
-
stimulation of release from cell walls
-
CaCl2
-
in presence of, increase in optimum temperature and thermostability
additional information
-
PR-1 silencing specifically increases beta-(1-3)-glucanase activity, suggesting a role for acidic PR-1 in the negative regulation of beta-(1-3)-glucanase activity
-
additional information
Q02126
enzyme is upregulated in Russian wheat aphid-infested tissue
-
additional information
-
protein level and enzymatic activity of beta-1,3-glucanase are substantially increased with considerable decrease in fruit firmness by ethylene treatment and reduced exposure to white light conditions
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
9.7
-
alpha-laminaribiosyl fluoride
-
pH 6.2, 30C, mutant E231G
19.8
-
alpha-laminaribiosyl fluoride
-
pH 6.2, 30C, mutant E231S
0.066
-
Laminariheptaose
-
-
0.2
-
Laminariheptaose
-
recombinant catalytic domain, pH 7.0, 25C
0.02
-
Laminarin
-
beta-glucanase I
0.04
-
Laminarin
-
-
0.04
-
Laminarin
-
beta-glucanase IIIB
0.16
-
Laminarin
-
-
0.17
-
Laminarin
-
isoform GI
0.18
-
Laminarin
-
isoform GIII
0.2
-
Laminarin
-
pH 6.5, 90C, soluble S296C variant
0.21
-
Laminarin
-
isoform GII
0.21
-
Laminarin
-
beta-glucanase V
0.32
-
Laminarin
-
-
0.35
-
Laminarin
O68641
mutant enzyme F160L, at 37C
0.41
-
Laminarin
O68641
wild type enzyme, at 37C
0.44
-
Laminarin
O68641
mutant enzyme T149A/A344V, at 37C
0.46
-
Laminarin
O68641
mutant enzyme G145D, at 37C
0.48
-
Laminarin
O68641
mutant enzyme T149A/G145D/A344V, at 37C
0.688
-
Laminarin
-
pH 8.0, 37C
0.77
-
Laminarin
-
pH 6.5, 90C, S296C variant immobilized on beads of 0.02-0.04 mM size
1
-
Laminarin
-
pH 6.5, 90C, S296C variant immobilized on beads of 0.063-0.09 mM size
2.9
-
Laminarin
-
pH 6.5, 90C, S296C variant immobilized on beads of 0.15-0.3 mM size
0.11
-
Laminaripentaose
-
-
0.32
-
Laminaripentaose
-
native enzyme, pH 7.0, 25C
25.9
-
alpha-laminaribiosyl fluoride
-
pH 6.2, 30C, mutant E231A
additional information
-
Glucan
Flavobacterium dormitator
-
value in mg/ml: 1.8
0.75
-
Laminariheptaose
-
native enzyme, pH 7.0, 25C
additional information
-
Laminarihexaose
Flavobacterium dormitator
-
value in mg/ml: 1.18
0.067
-
Laminarihexaose
-
-
additional information
-
Laminarin
-
0.35; value in mg/ml
additional information
-
Laminarin
-
0.02; value in mg/ml
additional information
-
Laminarin
-
1.18; value in mg/ml
additional information
-
Laminarin
-
1.24, isoform GI; 1.33 isoform GII; value in mg/ml
additional information
-
Laminarin
-
3.3; value in mg/ml
additional information
-
Laminarin
-
0.28; value in mg/ml
additional information
-
Laminarin
Sclerotium glucanicum
-
2.5; value in mg/ml
additional information
-
Laminarin
-
0.1; value in mg/ml
additional information
-
Laminarin
-
1.6 at 18C; 2.1 at 23C; 3.7 at 37C; value in mg/ml
additional information
-
Laminarin
-
3.04; value in mg/ml
additional information
-
Laminarin
-
value in mg/ml
additional information
-
Laminarin
-
0.15 , glucanase I; 0.69 glucanase II; value in mg/ml
additional information
-
Laminarin
-
0.25; value in mg/ml
additional information
-
Laminarin
Flavobacterium dormitator
-
0.26; value in mg/ml
additional information
-
Laminarin
-
1.05 lytic beta-(1-3)-glucanase I; value in mg/ml
additional information
-
Laminarin
-
3.4; value in mg/ml
additional information
-
Laminarin
-
0.24; value in mg/ml
additional information
-
Laminarin
-
the apparent KM for the purified enzyme is 0.78 mg/ml
additional information
-
Laminarin
-
KM value 0.3 mg/ml, pH 6.2, 37C
additional information
-
Laminarin
-
2.8 mg/ml, pH 6.5, 80C, wild-type enzyme. 3.5 mg/ml, pH 6.5, 80C, mutant enzyme delMet174
0.36
-
Laminaripentaose
-
recombinant catalytic domain, pH 7.0, 25C
additional information
-
laminaritetraose
Flavobacterium dormitator
-
value in mg/ml: 2.0
0.12
-
laminaritetraose
-
-
additional information
-
lichenan
-
4.7 mg/ml, pH 6.5, 80C, wild-type enzyme. 4.9 mg/ml, pH 6.5, 80C, mutant enzyme delMet174
additional information
-
additional information
Q4FCS2
Km value for hydrolysis of laminaran is 0.75 mg/ml
-
additional information
-
additional information
C3VPJ1
1.89 mg/ml for laminarin, recombinant enzyme
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
C1IE32, -
kinetics
-
additional information
-
additional information
C6GFH7, -
kinetics, overview
-
additional information
-
additional information
-
kinetics of wild-type and mutant enzymes, overview
-
additional information
-
additional information
A5IL44, -
Km value for laminarin is 3.3 mg/ml
-
additional information
-
additional information
-
KM value for carboxymethyl curdlan-Remazol Brilliant Blue 0.8 mg/ml, pH 6.2, 37C
-
0.13
-
O-carboxymethyl-pachyman
-
-
-
additional information
-
pustulan
-
value in mg/ml: 0.07
-
additional information
-
reduced curdlan
-
value in mg/ml: 1.18
-
additional information
-
reduced lamanrihexaose
-
value in mg/ml: 0.2
-
additional information
-
reduced laminarin, reduced laminarioctaose, reduced laminaripentaose
-
value in mg/ml: 0.3
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
30
-
Laminariheptaose
-
recombinant catalytic domain, pH 7.0, 25C
69
-
Laminariheptaose
-
native enzyme, pH 7.0, 25C
0.84
-
Laminarin
G9M5R4
pH 4.2, 37C
1.4
-
Laminarin
C6GFH7, -
pH 6.0, 30C
2.1
-
Laminarin
O68641
mutant enzyme T149A/A344V, at 37C
14.88
-
Laminarin
-
pH 8.0, 37C
23.01
-
Laminarin
-
-
29
-
Laminarin
A6YQV6
pH 9.0, 30C
35.9
-
Laminarin
O68641
wild type enzyme, at 37C
51.5
-
Laminarin
O68641
mutant enzyme F160L, at 37C
62.4
-
Laminarin
O68641
mutant enzyme G145D, at 37C
72.8
-
Laminarin
O68641
mutant enzyme T149A/A344V, at 37C
126.6
-
Laminarin
O68641
mutant enzyme T149A/G145D/A344V, at 37C
138
-
Laminarin
O68641
mutant enzyme T149A/G145D/A344V, at 37C
395
-
Laminarin
-
pH 4.5, 40C
680.3
-
Laminarin
A5IL44, -
pH 6.0, 91C
42
-
Laminaripentaose
-
recombinant catalytic domain, pH 7.0, 25C
75
-
Laminaripentaose
-
native enzyme, pH 7.0, 25C
0.19
-
laminaritetraose
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
93
-
Laminariheptaose
-
native enzyme, pH 7.0, 25C
12490
156
-
Laminariheptaose
-
recombinant catalytic domain, pH 7.0, 25C
12490
118
-
Laminaripentaose
-
recombinant catalytic domain, pH 7.0, 25C
12493
237
-
Laminaripentaose
-
native enzyme, pH 7.0, 25C
12493
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1
-
Hexadecyltrimethylammonium bromide
-
-
3.5
-
Laminarin
-
pH 6.5, 90C, S296C variant immobilized on beads of 0.02-0.04 mM size
6.5
-
Laminarin
-
pH 6.5, 90C, soluble S296C variant
22.7
-
Laminarin
-
pH 6.5, 90C, S296C variant immobilized on beads of 0.063-0.09 mM size
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.0025
0.015
-
activites of purified recombinant enzymes from different cultivars, overview
0.01
-
-
isoform GII
0.013
-
-
isoform GI
0.042
-
-
pH 5.0, 37C
0.048
-
-
pH 4.0, 37C
0.08
-
Q70C53
wild-type, substrate lichenan
0.095
-
-
crude extract
0.096
-
-
homogenate
0.114
-
-
pH 5.0, 37C
0.18
-
-
pH 4.0, 37C
0.18
-
-
substrate curdlan, pH 6.2, 37C
0.23
-
-
substrate lichenan, pH 6.2, 37C
0.252
-
-
after DEAE anion exchange chromatography
0.26
-
-
more specific for compounds having beta-1,3-glucosidic linkages
0.285
-
Littorina kurila
-
-
0.5
-
-
beta-glucanase IV
0.71
-
-
substrate laminarin, pH 6.2, 37C
0.86
-
-
substrate laminarioligosaccharide, pH 6.2, 37C
0.945
-
-
after HIC chromatography
1.12
-
-
beta-glucanase I
1.16
-
-
substrate laminarihexaose, pH 6.2, 37C
1.21
-
-
beta-glucanase V
1.85
-
G9M5R4
pH 4.2, 37C
1.89
-
-
for glucanase I
2.6
-
-
pH10.7-isoform
3.5
-
-
pH 4.5, 37C
3.69
-
-
culture filtrate, at 50C
3.9
-
-
crude enzyme
4.1
-
-
lytic beta-(1-3)-glucanase I
4.4
-
C6GFH7, -
purified native enzyme
5.89
-
-
for glucanase II
6
-
-
after 65fold purification
7.8
-
-
after gel filtration chromatography
8
-
-
recombinant catalytic domain, pH 7.0, 25C
8.47
-
-
native enzyme, pH 7.0, 25C
9.1
-
-
pH 6.5, temperature not specified in the publication
9.62
-
-
beta-glucanase IIIB
10.1
-
Flavobacterium dormitator
-
-
11.1
-
-
wild-type, substrate lichenan, 40C
15
-
-
-
21.4
-
A5IL44, -
substrate lichenan, pH 6.0, 91C
24
-
Q70C53
mutant C6A, substrate laminarin
40.5
-
-
isoform GIII
41.55
-
A5IL44, -
substrate beta-glucan, pH 6.0, 91C
48.1
-
A5IL44, -
substrate laminarin, pH 6.0, 91C
48.5
-
-
after 13.1fold purification, at 50C
49.1
-
O68641
wild type enzyme, at 37C, using laminarin as the substrate
51
-
-
form L-4
62
-
Q70C53
mutant C6A, substrate lichenan; wild-type, substrate carboxymethylated pachyman
68
-
C6L684, -
purified enzyme
69
-
Sclerotium glucanicum
-
-
70.3
-
O68641
mutant enzyme F160L, at 37C, using laminarin as the substrate
80.6
-
O68641
mutant enzyme T149A/A344V, at 37C, using laminarin as the substrate
82
-
Q70C53
mutant C6A, substrate carboxymethylated pachyman
90
-
Q70C53
wild-type, substrate laminarin
96.2
-
O68641
mutant enzyme G145D, at 37C, using laminarin as the substrate
99
-
-
form L-1
102.8
-
-
mutant lacking residues 72-75, substrate lichenan, 80C
115.7
-
-
mutant lacking residues 72-75, substrate lichenan, 40C; wild-type, substrate lichenan, 70C
126.8
-
-
wild-type, substrate laminarin, 40C
141.4
-
-
mutant lacking residues 72-75, substrate laminarin, 40C
162.7
-
O68641
mutant enzyme T149A/G145D/A344V, at 37C, using laminarin as the substrate
172
-
-
purified native enzyme
174
-
Q70C53
mutant C6A, substrate carboxymethylated curdlan
185
-
-
wild-type, substrate lichenan, 80C
217
-
-
form L-2
220
-
-
pH 6.2, 30C
236
-
C3VPJ1
purified recombinant enzyme, substrate laminarin
240.5
-
-
isoform GII
249
-
-
mutant lacking residues 72-75, substrate laminarin, 80C
263.6
-
-
mutant lacking residues 72-75, substrate lichenan, 70C
281.5
-
-
isoform GI
286
-
-
37C, pH 5.0
334.3
-
-
mutant lacking residues 72-75, substrate laminarin, 70C
340
-
Q59328
substrate laminarin, pH 6.0, 60C
369.6
-
-
-
403
-
-
purified YlCrh2S, using laminarin as substrate, at 30C
409.5
-
-
after 105fold purification
484
-
Q70C53
wild-type, substrate carboxymethylated curdlan
500
-
-
-
549
-
-
pH 4.5, 40C
659.3
-
-
wild-type, substrate laminarin, 70C
1087
-
-
wild-type, substrate laminarin, 80C
2680
-
Q59328
substrate barley beta-glucan, pH 6.0, 60C
3349
-
-
purified YlCrh1S, using laminarin as substrate, at 30C
4480
-
A6YQV6
pH 9.0, 30C
additional information
-
Trichoderma asperellum, Trichoderma sp.
-
activities in macro- and micro-assay, statistics, overview
additional information
-
-
substrate specificities of wild-type and mutant enzymes, overview
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
G9M5R4
-
4.5
-
-
isoform GI
4.7
-
Sclerotium glucanicum
-
-
4.8
5
-
-
4.8
-
-
isoforms GI, GII and GIII
4.8
-
Fungi imperfecti
-
maximum acivity on disruption of living yeast cells
4.8
-
-
wild-type
4.8
-
-
assay at
5
-
-
isoform GII
5
-
-
both forms, glucanase I and glucanase II
5
-
-
hydrolysis of laminarin
5.1
-
-
isoform G1
5.3
-
-
-
5.4
-
-
isoform G2
5.4
-
Littorina kurila
-
-
5.5
6
Q000P7
catalytic module
5.5
-
C3VPJ1
recombinant enzyme
5.7
-
-
hydrolysis of CM-pachyman
5.8
-
Q000P7
assay at
6
-
Flavobacterium dormitator
-
-
6
-
C6GFH7, -
-
6.2
-
A5IL44, -
-
6.5
-
-
-
6.5
-
-
assay at
6.8
-
-
assay at
9
10
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3
10
-
native enzyme
3.6
6.1
-
50% activity at pH 3.6 and pH 6.1
4
6
Fungi imperfecti
-
maximum activity on glucan depolymerization
4
6.5
-
-
4
9.5
C6L684, -
-
4
-
-
loss of activity below, recombinant catalytic domain
4.5
7.5
Littorina kurila
-
-
4.5
8
-
pH 4.5: about 75% of maximal activity, pH 8.0: about 55% of maximal activity
5
6
-
for beta-glucanases I, IIIB and V
5
7
A5IL44, -
more than 80% of maximum activity
5
9
C3VPJ1
activity range
6
10
-
broad, mutant E231G
additional information
-
C6GFH7, -
pH effects on native and chemically modified enzyme, profiles, overview
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
both glucanases I and II
30
-
C6GFH7, -
assay at
37
-
Q000P7
assay at
40
-
Q000P7
catalytic module
40
-
Trichoderma asperellum, Trichoderma sp.
-
assay at
50
-
Flavobacterium dormitator
-
-
50
-
C6L684, -
-
50
-
-
assay at
50
-
-
assay at
50
-
G9M5R4
-
55
-
Sclerotium glucanicum
-
-
60
65
-
-
60
-
-
-
60
-
Fungi imperfecti
-
-
65
-
-
-
65
-
C3VPJ1
recombinant enzyme
80
-
-
assay at
90
-
-
assay at
91
-
A5IL44, -
-
additional information
-
B4XEK5
30-35
additional information
-
B4XEK7
30-35
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
35
B4XEK7
-
30
60
-
-
40
70
C6L684, -
-
62
104
-
active at 62C, most active at 104C, not active at 20C
78
-
A5IL44, -
pH 6.0, 82% of maximum activity
80
115
-
80C: about 50% of maximal activity, 115C: about 30% of maximal activity
95
-
A5IL44, -
pH 6.0, 86% of maximum activity
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.9
-
G9M5R4
isoelectric focusing
4.2
-
-
isoelectric focusing
4.33
-
C6GFH7, -
TLam, sequence calculation
4.45
-
Q1ERF7, Q1ERF8, Q1ERF9, Q1ERG0, Q1ERG1, Q1ERG2, -
isoelectric focusing; isoelectric focusing; isoelectric focusing; isoelectric focusing; isoelectric focusing; isoelectric focusing; isoelectric focusing
5.5
-
-
isoelectric focusing
6
-
-
isoelectric focusing
6
-
-
isoelectric focusing
6.1
-
A6YQV6
calculated
6.2
-
-
isoelectric focusing
7
-
-, Q7Z0T2
deduced from gene sequence
8.53
-
O82716
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
four different isoforms, beta-glucanases I, IIIB, IV and V
Manually annotated by BRENDA team
-
increasing activity with increasing culture age, maximum concentration reached at 7th day
Manually annotated by BRENDA team
-
from derepressed mycelia
Manually annotated by BRENDA team
-
enzyme activation due to factors produced during conjugation and sporulation
Manually annotated by BRENDA team
-
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
-
Tunicase, a crude enzyme preparation from Cellulosimicrobium cellulans DK-1
Manually annotated by BRENDA team
Cellulosimicrobium cellulans DK-1
-
Tunicase, a crude enzyme preparation from Cellulosimicrobium cellulans DK-1
-
Manually annotated by BRENDA team
Sclerotium glucanicum
-
-
Manually annotated by BRENDA team
Flavobacterium dormitator
-
-
Manually annotated by BRENDA team
-
induction of enzyme synthesis by glucan culture medium
Manually annotated by BRENDA team
Rhizopus sp.
-
-
Manually annotated by BRENDA team
Fungi imperfecti
-
best induction of enzyme synthesis by baker's yeast carbon source
Manually annotated by BRENDA team
B3VTS4, -
PCEng2 mRNA expression during the life cycle of Pneumocystis carinii, upregulation in cystic isolates, the protein occurs in both cyst and trophic forms, overview. PCEng2 mRNA expression is largely restricted to cysts and is not pH-responsive
Manually annotated by BRENDA team
-
after germination, exclusively in micropylar region, after wounding, also in lateral endosperm
Manually annotated by BRENDA team
Q9SXY6, Q9SXY8
of 4-month-old rice plant. EXoressin of OsGlu1 is strongly induced by H2O2 and senescence
Manually annotated by BRENDA team
-
cultivar differences in beta-1,3 glucanase gene expression, glucanase activity and fruit pulp softening rates during fruit ripening in three naturally occurring banana cultivars. Low enzyme expressiong during fruit ripening
Manually annotated by BRENDA team
-
of Neosartorya fumigata
Manually annotated by BRENDA team
-
two isoforms, GI and GII
Manually annotated by BRENDA team
-
apoplastic fluid
Manually annotated by BRENDA team
-
two forms, EG-1 and EG2A
Manually annotated by BRENDA team
-
low concentration
Manually annotated by BRENDA team
Littorina kurila
-
-
Manually annotated by BRENDA team
A6YQV6
mRNA coding for SLam is expressed along the whole midgut tissue
Manually annotated by BRENDA team
-
increase of two isoenzymes, G1 and G2, after inoculation by Fusarium solani
Manually annotated by BRENDA team
Q9SXY6, Q9SXY8
of 4-month-old rice plant
Manually annotated by BRENDA team
-
germinating grain
Manually annotated by BRENDA team
-
germinating grain
Manually annotated by BRENDA team
Trichoderma asperellum, Trichoderma sp.
-
-
Manually annotated by BRENDA team
Gecarcoidea natalis Pocock 1888
-
-
-
Manually annotated by BRENDA team
additional information
A6YQV6
mRNA coding for SLam is expressed along the whole midgut tissue, but not in the Malpighian tubules, fat body and carcass
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Clostridium thermocellum F7
-
-
-
Manually annotated by BRENDA team
-
beta-glucanases I, IIIB, IV and V
Manually annotated by BRENDA team
-
two different forms, only present in conjugating and sporulating cells, not present in vegetative cells
Manually annotated by BRENDA team
-
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
Sclerotium glucanicum
-
-
-
Manually annotated by BRENDA team
Flavobacterium dormitator
-
-
-
Manually annotated by BRENDA team
Rhizopus sp.
-
-
-
Manually annotated by BRENDA team
Fungi imperfecti
-
-
-
Manually annotated by BRENDA team
-
the enzyme is secreted to the culture medium
-
Manually annotated by BRENDA team
Hypocrea lixii Rifai T24
-
-
-
-
Manually annotated by BRENDA team
-
beta-glucanases I, IIIB and V
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Zobellia galactanivorans (strain DSM 12802 / CIP 106680 / NCIMB 13871 / Dsij)
Zobellia galactanivorans (strain DSM 12802 / CIP 106680 / NCIMB 13871 / Dsij)
Zobellia galactanivorans (strain DSM 12802 / CIP 106680 / NCIMB 13871 / Dsij)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
12000
-
-
gel filtration
12500
20000
-
form L-4, SDS-PAGE, gel filtration
15000
23000
-
form L-2, SDS-PAGE, gel filtration
16000
22000
-
form L-1, SDS-PAGE, gel filtration
16000
-
-
gel filtration
17000
20000
Flavobacterium dormitator
-
SDS-PAGE, gel filtration
17000
-
-
form EG-1, gel filtration
23000
-
-
gel filtration
24300
-
-
gel filtration
24500
-
Fungi imperfecti
-
gel filtration, sedimentation equilibrium
26000
-
-
form EG-2A, gel filtration
29000
-
-
SDS-PAGE, gel filtration
30000
-
-
gel filtration, SDS-PAGE
32000
33000
-
SDS-PAGE, sedimentation equilibrium
32000
33700
-
native PAGE, SDS-PAGE, MALDI-MS
32000
-
-
isoform GI, SDS-PAGE, gel filtration
32000
-
-
isoforms GI, GII and GIII, SDS-PAGE
32000
-
-
-
32000
-
Littorina kurila
-
gel filtration
32500
-
-
gel filtration
32980
-
Q1ERF7, Q1ERF8, Q1ERF9, Q1ERG0, Q1ERG1, Q1ERG2, -
calculated from sequence of cDNA; calculated from sequence of cDNA; calculated from sequence of cDNA; calculated from sequence of cDNA; calculated from sequence of cDNA; calculated from sequence of cDNA; calculated from sequence of cDNA
33000
-
-
pH 10.7 isoform, SDS-PAGE, gel filtration
33000
-
-
SDS-PAGE
33500
-
-
calculation from DNA sequence
33500
-
-
isoform G1, SDS-PAGE
34300
-
-
isoform G2, SDS-PAGE
34700
-
-
gel filtration
35000
-
-
isoform GII, SDS-PAGE, gel filtration
35000
-
-
SDS-PAGE
35000
-
-
SDS-PAGE
35000
-
-
SDS-PAGE
35000
-
-
gel filtration
35500
-
-
SDS-PAGE, gel filtration
36000
-
-
SDS-PAGE
36000
-
-
gel filtration
36000
-
-
SDS-PAGE
36900
-
-
estimated from amino acid sequence
40000
-
-
SDS-PAGE, gel filtration
40000
-
-
SDS-PAGE
40000
-
O68641
SDS-PAGE
41000
-
-
SDS-PAGE
42000
43000
-
SDS-PAGE, gel filtration
45000
-
-
gel filtration
55000
-
-
SDS-PAGE
60000
-
-
SDS-PAGE
62000
-
-
SDS-PAGE
65000
68000
-
SDS-PAGE, gel filtration
66000
-
-
SDS-PAGE
69200
-
-
beta-glucanase V, native electrophoresis, gel filtration
71000
-
-
gel filtration chromatography
74000
-
-
SDS-PAGE, gel filtration
74000
-
-
gel filtration
74000
-
-
PAGE
75000
79000
-
gel filtration, native PAGE, SDS-PAGE
75000
-
-
SDS-PAGE, gel filtration, glucanase II
75000
-
-
SDS-PAGE
79760
-
A4PHQ5, -
calculated from amino acid sequence
85000
-
Sclerotium glucanicum
-
SDS-PAGE
160500
-
-
SDS-PAGE, gel filtration, glucanase I
190500
-
-
beta-glucanase IIIB, native electrophoresis, gel filtration
218000
-
-
beta-glucanase I, native electrophoresis, gel filtration
230000
-
-
PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 44000, SDS-PAGE
?
-
x * 20000, SDS-PAGE
?
-, Q7Z0T2
x * 38000, mature protein, deduced from gene sequence
?
-
x * 33000, SDS-PAGE
?
-
x * 71000, SDS-PAGE
?
-
x * 35000, SDS-PAGE
?
-
x * 49000, deduced from gene sequence
?
Q59328
x * 148000, deduced from gene sequence, x * 125000, SDS-PAGE
?
-
x * 43000, recombinant protein with his6-tag, SDS-PAGE
?
-
x * 124157, calculated
?
-
x * 37000-41000, SDS-PAGE
?
Q4FCS2
x * 37000, SDS-PAGE
?
B3VTS4, -
x * 75000, recombinant His6-tagged enzyme, SDS-PAGE
?
C3VPJ1
x * 42700, about, sequence calculation
?
-
x * 30135, mass spectrometry
?
C6L684, -
x * 33000, HdLam33, SDS-PAGE, x * 36866, Hdlam33, sequence calculation
?
-
x * 36000, SDS-PAGE
?
C1IE32, -
x * 28983, sequence calculation, x * 46000, recombinant His-tagged and thioredoxin-fused enzyme, SDS-PAGE
?
C6GFH7, -
x * 50000, SDS-PAGE, x * 40117, sequence calculation
?
O82716
x * 32550, sequence calculation
?
-
x * 37000, recombinant His-tagged enzyme, SDS-PAGE
?
G9M5R4
x * 25000, SDS-PAGE, x * 26000, calculated
?
-
x * 29000, SDS-PAGE
?
-
x * 41000, SDS-PAGE, x * 40798, MALDI-TOF
?
-
x * 33000, SDS-PAGE
?
-
x * 65993, calculated, x * 150000, SDS-PAGE of recombinant protein, due to hyperglycosylation
?
A6YQV6
x * 40400, calculated
?
Bacillus clausii NM-1
-
x * 71000, SDS-PAGE
-
?
Cellulosimicrobium cellulans DK-1
-
x * 41000, SDS-PAGE, x * 40798, MALDI-TOF
-
?
Clostridium thermocellum F7
-
x * 148000, deduced from gene sequence, x * 125000, SDS-PAGE
-
?
Delftia tsuruhatensis MV01
-
x * 29000, SDS-PAGE
-
dimer
-
2 * 30000, non-reducing PAGE
dimer
-
1 * 78500, 1 * 82000, glucanase II, SDS-PAGE
dimer
-
2 * 91000, SDS-PAGE
monomer
-
1 * 30000, gel filtration, SDS-PAGE
monomer
-
1 * 75000-79000, gel filtration, SDS-PAGE
monomer
-
1 * 74000, SDS-PAGE, gel filtration
monomer
-
1 * 29000, SDS-PAGE, gel filtration
monomer
-
1 * 32000, isoform GI, SDS-PAGE, gel filtration; 1 * 35000, isoform GII, SDS-PAGE, gel filtration
monomer
-
1 * 34700, gel filtration
monomer
-
1 * 32000-33000, SDS-PAGE, sedimentation equilibrium
monomer
-
1 * 42000-43000, SDS-PAGE, gel filtration
monomer
-
1 * 65000-68000, SDS-PAGE, gel filtration
monomer
-
1 * 75000, glucanase I, SDS-PAGE, gel filtration
monomer
-
1 * 36000, SDS-PAGE
monomer
-
1 * 32500, SDS-PAGE
monomer
Littorina kurila
-
1 * 40000, SDS-PAGE
additional information
-
enzyme has two functional domain, N-terminal part has enzymic activity, C-terminal part is a putative carbohydrate-binding module
additional information
-
41000 SDS-PAGE, 71000 gel filtration chromatography, lamarinase is a dimer or contains a laminarin-binding domain, which is in similar size to the catalytic compound
additional information
Q000P7
putative functional units of the single protein strain include, from N to C terminus, a leader peptide, three repeats of the S-layer homologous module, a catalytic module of glycoside hydrolase family 16, four repeats of the carbohydrate-binding module of family CBM_4_9, and an analogue of coagulation factor Fa5/8C
additional information
C3VPJ1
the encoded protein comprises a catalytic module of glycosyl hydrolase family 16, a short glycine linker region, and a family 13 carbohydrate-binding module
additional information
-
LamA NMR, differential scanning calorimetry, and mass spectrometry structure determination and analysis, modelling, overview
additional information
C1IE32, -
the enzyme contains a putative signal peptide and a typical motif of glycosyl hydrolase family 16, EIDITE, CaLam homology modelling, overview
additional information
C6GFH7, -
homology model of the TLam structure, overview
additional information
Q000P7
the beta-1,3-glucanase LamA is highly modular, containing a signal sequence, three repeats of the S-layer homologous module, a segment with unknown function, a catalytic module of glycoside hydrolase family 16, GH16, four repeats of CBM4 family, and a F5/8C module representing a discoidin domain, DS domain, from N- to C-terminus. The recombinant isolated purified His-tagged DS domain forms dimers
additional information
Gecarcoidea natalis Pocock 1888
-
41000 SDS-PAGE, 71000 gel filtration chromatography, lamarinase is a dimer or contains a laminarin-binding domain, which is in similar size to the catalytic compound
-
additional information
Paenibacillus sp. BCRC
-
the beta-1,3-glucanase LamA is highly modular, containing a signal sequence, three repeats of the S-layer homologous module, a segment with unknown function, a catalytic module of glycoside hydrolase family 16, GH16, four repeats of CBM4 family, and a F5/8C module representing a discoidin domain, DS domain, from N- to C-terminus. The recombinant isolated purified His-tagged DS domain forms dimers
-
additional information
-
putative functional units of the single protein strain include, from N to C terminus, a leader peptide, three repeats of the S-layer homologous module, a catalytic module of glycoside hydrolase family 16, four repeats of the carbohydrate-binding module of family CBM_4_9, and an analogue of coagulation factor Fa5/8C
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
-
no glycoprotein
-
very small or no carbohydrate content
glycoprotein
-
glycosylated with mannose residues, only O-linked
glycoprotein
-
sequence analysis reveals two potential N-glycosylation sites at positions N200GSS and N453GTS
phosphoprotein
-
sequence analysis reveals a GPI modification site at position LSN630GA
proteolytic modification
-
sequence analysis reveals a signal peptide cleavage site at position VSA21-T22A
no glycoprotein
-
-
glycoprotein
-
isoform GII, glycosylated with glucose and/or mannose residues
glycoprotein
-
isoform GIII, 12-17% carbohydrate content, w/w
glycoprotein
-
-
glycoprotein
-
contains two arabinose residues per molecule
glycoprotein
-
6.7% carbohydate content
glycoprotein
-
-
glycoprotein
-
glycosylated Asn284
glycoprotein
A6YQV6
sequence has five putative glycosylation sites at residues T33, S77, S324, E188 and E193
glycoprotein
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
enzyme possesses the eightfold beta/alpha architecture typical for family 17 glycoside hydrolases
-
hanging drop vapour diffusion method with 0.1 M Tris-HCl (pH 8.0), 1.5 M ammonium sulfate, 0.1 M sodium chloride, and 1% (v/v) ethanol
-
hanging drop vapour diffusion technique at 20C, crystal structure is determined at 2.1 A resolution by molecular replacement; to 2.1 A resolution, determination by molecular replacement. Structure reveals a kink of six residues at the entrance of the catalytic cleft
-
catalytic domain, to 1.5 A resolution. The overall structure contains two antiparallel six- and seven-stranded beta-sheets stacked in a beta-sandwich jelly-roll motif. The active-site cleft of the enzyme shows the closure of one end primarily caused by two protruding loop insertions and two key residues, Y38 and Y134
-
small angle X-ray scattering data and homology modeling. Enzyme displays a multi-domain structural architecture of a V-shape envelope with a catalytic domain flanked by two carbohydrate-binding modules
A5IL44, -
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2.6
-
-
60% remaining activity
3
7
-
more than 90% activity is retained after 20 h of incubation at 25C
3
9
G9M5R4
4C, stable for 20 h
3.5
6
-
rapid inactivation below and above
4
6
-
60C, 48 h, incubation does not significantly reduce the activity of the immobilized S296C variant
4.5
-
-
activity decreases rapidly at pH lower 4.5
4.6
-
-
50% remaining activity
5
6
Fungi imperfecti
-
stable within for 10 min at 50C
5
-
-
below less activity for isoform GI than for GII or GIII
5
-
-
65-70% retaining activity
5.3
11.5
-
-
5.5
7
-
stable within during 16 h
5.5
7.3
-
stable within
5.5
-
-
activity decreases rapidly at pH lower 5.5
6
9
Flavobacterium dormitator
-
stable within
6
-
-
isoforms GI and GII retain 17-27% activity, GIII retaines 66% activity
6.2
-
-
60% remaining activity
6.2
-
-
50% remaining activity
7
8
-
most stable within
7
-
-
65-70% retaining activity
7
-
-
most stable
8
10
-
stable within
10
-
-
60C, 48 h, incubation does not significantly reduce the activity of the immobilized S296C variant
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
Q4FCS2
half-life 30 min
37
-
Q4FCS2
half-life 10 min
40
-
-
stable below
40
-
-
half-life more than 24 h
45
-
-
inactivation above
45
-
-
stable for 90 min
45
-
-
form EG-1 stable for 45 min, form EG2A rapidly inactivated
45
-
-
stable below
45
-
-
maximum heat stability
45
-
-
rapid denaturation occurs above 45C
45
-
-
55% residual activity after 90 min at 45C at pH 5.0
45
-
-
half-life 180 min
50
65
-
purified recombinant enzyme, 30 min, stable
50
-
-
50% activity
50
-
-
fully active up to for 1 h
50
-
-
half-life 38 min
50
-
-
rapid loss of activity above
50
-
-
no activity after 90 min at 50C at pH 5.0
50
-
-
thermostable up to 50C
50
-
-
24 h, 17% residual activity
50
-
-
half-life 20 min
55
-
-
stable up to, activity lost at 70C
55
-
-
inactivation temperature
55
-
Sclerotium glucanicum
-
63% activity after 10 min
55
-
-
form EG-1 stable for 45 min
55
-
-
exhibits a half-life of 30 min at 55C
55
-
-
in absence of laminarin, unstable above
60
70
-
activity rapidly lost
60
-
-
stable up to, rapid inactivation above
60
-
-
sharp reduction of activity
60
-
Flavobacterium dormitator
-
complete loss of activity above
60
-
-
half-life 20 min
60
-
-
enzyme completely becomes inactive beyond 60C
60
-
C3VPJ1
purified recombinant enzyme, over 80% activity remaining after 30 min
60
-
G9M5R4
30 min, complete inactivation
60
-
-
bifunctional immobilized S296C enzyme shows high operational stability and pH stability at 60C
65
-
-
inactivation above
65
-
Fungi imperfecti
-
inactivation above
65
-
-
complete inactivation
65
-
Q59328
2 h, stable
70
80
C3VPJ1
purified recombinant enzyme, over 40% activity remaining after 30 min
70
-
-
stable up to
70
-
-
complete inactivation
70
-
-
70 min, 50% residual activity
70
-
Q59328
10 min, 50% residual activity
70
-
-
purified recombinant enzyme, 10 min, partly loss of activity
70
-
A5IL44, -
stable
70
-
-
10 min, complete loss of activity both for catalytic domain and native enzyme
75
-
-
50% activity retains
80
-
A5IL44, -
16 h, 60% residual activity
80
-
-
110 h, stable
90
-
A5IL44, -
half-life 577 min
90
-
-
half-life: 64 h
95
-
A5IL44, -
half-life 126 min
95
-
-
in presence of laminarin, stable up to
100
-
-
half-life: 19 h
110
-
-
half-life: 15 min
additional information
-
B4XEK5
more than 50% of maximal activity at 5C
additional information
-
B4XEK7
more than 50% of maximal activity at 5C
additional information
-
Q000P7
melting temperatures of wild-type and mutant DS domains between 52.3C and 58.3C
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
very unstable during dilution and dialysis, addition of Ca2+ and bovine serum albumin partly restores activity
-
operational stability of the immobilized S296C variant is optimal with milled beads suggesting applicability of the immobilized enzyme on the smallest particles for continuous substrate conversion under industrially relevant conditions. S296C bound to the large beads shows a somewhat lower operational stability
-
The enzyme purified is found to be highly stable between 30 and 40C for 1 h in citrate-phosphate buffer (pH 7.0)
-
beta-glucanase IV highly unstable
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-25C, 2 mM sodium succinate, pH 6.0, two months
-
20C, 48 h, 75% residual activity
-
retains full activity following lyophilization for 3 months if stored at -20C, in solution stable if stored at -20C
-
4C, 50 mM sodium phosphate, pH 7.8, 300 mM NaCl, stable for several weeks
-
25C, 0.05 M sodium acetate buffer at pH 4.5 with 0.25 M sodium chloride, 1 month, no loss of activity
-
37C, 0.05 M sodium acetate buffer at pH 4.5 with 0.25 M sodium chloride, 2 h, complete loss of activity
-
37C, 1 h, no loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
to homogeneity, gel filtration, preparative PAGE
-
ammonium sulfate precipitation and DEAE-Sepharose column chromatography
-
to homogeneity, affinity chromatography
-
to homogeneity, affinity chromatography
-
native enzyme 126fold from digestive fluid by ammonium sulfate fractionation, three steps of cation exchange chromatography, ultrafiltration and gel filtration
-
overexpressed enzyme, partial
-
to homogeneity, 4step chroamtography
-
to homogenety, affinity chromatography
-
to homogeneity by absortion chromatography for lytic beta-(1-3)-glucanase I, partial for lytic beta-(1-3)-glucanase II
-
to homogeneity, 3step chromatography
-
both native enzyme and recombinant catalytic domain
-
nickel metal affinity chromatography
O68641
recombinant enzyme with His6-tag, expression in Escherichia coli
-
from carbon-starving culture
-
partial
Flavobacterium dormitator
-
to homogeneity, continuous-curtain electrophoresis
-
to homogeneity, crystalline form
Fungi imperfecti
-
precipitation, a combination of anion exchange, hydrophobic interaction and gel filtration chromatography, all chromatography is carried out at 4C
-
to homogeneity, 2step chromatography, isoelectric focusing
-
native HdLam33 340fold from digestive fluid by ammonium sulfate fractionation, hydrophobic interaction and cation exchange chromatography, and gel filtration
C6L684, -
to homogeneity, chromatography steps
-
to homogeneity, 2step chromatography
-
to homogeneity, 3step chromatography
-
to homogeneity, 4-5step chromatography
-
Sephacryl S-200 gelfiltration and Phenyl Sepharose CL 4B chromatography
-
to homogeneity, 2step chromatography
-
to homogeneity, 5step chromatography, affinity chromatography
-
from fruiting body
G9M5R4
-
Littorina kurila
-
CM-Sephadex C-50 gel filtration, phenyl-Sepharose CL-4B column chromatography, and Sephadex G-75 gel filtration
-
to homogeneity, 6step chromatography
-
recombinant His-tagged enzymes from Escherichia coli strain M15 by nickel affinity chromatography
-
to homogeneity, chromatography, isoelectric focusing
-
to homogeneity
-
to homogeneity, 3step chromatography
-
to homogeneity, 4step chromatography
-
recombinant His-tagged wild-type and mutant LamA discoidin domains from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Q000P7
to homogeneity, 3step chromatography, isoelectric focusing
-
to homogeneity, 2step chromatography
-
recombinant His6-tagged PCEng2 from Saccharomyces cerevisiae by immunoaffinity chromatography and nickel affinity chromatography
B3VTS4, -
to homogeneity, 5step chromatography
-
partial
-
native LamA from culture medium by hydrophobic interaction chromatography and gel filtration
-
ammonium sulfate precipitation, ion-exchange and gel filtration
-
to homogeneity, three forms separated, L-1, L-2 and L-4, chromatography steps, affinity chromatography
-
in crystalline form
Rhizopus sp.
-
isoform Bgl2 copurifies with acid trehalase
-
to homogeneity
-
to homogeneity, separation of four different beta-1,3-glucanases
-
to homogeneity, 3step chromatography
-
CM-Sepharose Fast Flow column chromatography
-
to homogeneity, 3step chromatography for glucanase I, 4step chromatography for glucanase II
-
to homogeneity, 1step chromatography
Sclerotium glucanicum
-
to homogeneity
-
from larval midgut
A6YQV6
to homogeneity, chromatography, preparative gel electrophoresis
-
recombinant His6-tagged BglS27 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
C3VPJ1
to homogeneity, 4step chromatography
-
to homogeneity, repeated gel filtration steps
-
native enzyme 113fold from midgut to homogeneity by anion exchange and hydrophobic interaction chromatography, and gel filtration
C6GFH7, -
recombinant His-tagged enzyme in Escherichia coli strain BL21(DE3) by nickel affinity chromatography
O82716
ammonium sulfate precipitation and His affinity chromatography using ProBond nickel-chelating resin
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
-
expression in Pichia pastoris
-
expressed in Escherichia coli BL21(DE3) cells
O68641
expression of catalytic domain Ala1-Thr256 in Escherichia coli
-
expression in Escherichia coli
-
gene CaLam, DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis and tree, recombinant expression of His-tagged and thioredoxin-fused enzyme without signal sequence in Escherichia coli strain Rosetta(DE3), subcloning in Escherichia coli strain DH5alpha
C1IE32, -
expression in Escherichia coli
B4XEK5
HdLam33, DNA and amino acid sequence determination and analysis
C6L684, -
cDNA for sequence analysis
-
expression in Pichia pastoris
G9M5R4
cloning from cultivars Rasthali, Kanthali, and Monthan, DNA and amino acid sequence determination and analysis, expression of His-tagged enzymes in Escherichia coli strain M15
-
expression in Pichia pastoris
-
expressed in Escherichia coli strain B834(DE3)
-
expression of the isolated wild-type and mutant LamA discoidin domains as soluble His-tagged proteins in Escherichia coli strain BL21(DE3)
Q000P7
expression in Escherichia coli and Lactococcus lactis
B4XEK7
PCEng2, DNA and amino acid sequence determination and analysis, expression of recombinant His6-tagged PCEng2 in Saccharomyces cerevisiae, complementation of Eng2-deleted Saccharomyces cerevisiae strains with restoration of the cell wall separation defect during proliferation
B3VTS4, -
expressed in Escherichia coli strain BL21(DE3)
-
expression in Escherichia coli
-
overexpressed in Escherichia coli using the T7-expression system
-
expression in yeast
-
placing of gene eng2 under the control of a repressible promoter
-
expression in inactive form in Escherichia coli, expression as active enzyme in Pichia pastoris
A6YQV6
expression in Escherichia coli
-
gene bglS27, DNA and amino acid sequence determination and analysis, expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3)
C3VPJ1
TLam DNA and amino acid sequence determination and analysis, phylogenetic analysisand tree
C6GFH7, -
expression of wild-type and mutant Lam81A in Escherichia coli strain BL21
-
gene TaGlu, DNA and amino acid sequence determination and analysis, quantitative real-time PCR expression analysis, and phylogenetic analysis and tree, overview. Expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
O82716
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
regulation of engA is dependent on the FluG /BrlA asexual sporulation signalling pathway in submerged culture
-
auxin and cold treatment negatively regulate gene expression. Transcript level is markedly decreased by constant exposure to white light
-
wound treatment does not induce beta-1,3-glucanase expression
-
exogenous application of ethylene strongly stimulates beta-1,3-glucanase transcript accumulation, and abscisic acid partially induces the expression of the gene
-
ethylene treatment differentially stimulates beta-1,3 glucanase expression in the three banana cultivars, overview. Noinduction incv. Monthan, slight induction in cv. Kanthali, promninent induction in cv. Rasthali
-
mRNA coding for SLam is expressed along the whole midgut tissue, but not in the Malpighian tubules, fat body and carcass
A6YQV6
induction of TaGlu by phytohormones salicylic acid, methyl jasmonate, and ethepon. Infection with the stripe rust pathogen Puccinia striiformis f. sp. tritici induces the enzyme in wheat
O82716
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E119A
-
variant of catalytic domain, significant decrease in hydrolytic activity for laminarin
E119A/Ldel
-
variant of catalytic domain with deletion of the Gly/Ser-rich linker, Ser244-Thr256, no expression of protein
F160L
O68641
increased activity
G145D
O68641
increased activity
M123del
-
variant of catalytic domain, significant decrease in hydrolytic activity for laminarin
T149A/A344V
O68641
increased activity
T149A/G145D/A344V
O68641
increased activity
E119A
Cellulosimicrobium cellulans DK-1
-
variant of catalytic domain, significant decrease in hydrolytic activity for laminarin
-
E119A/Ldel
Cellulosimicrobium cellulans DK-1
-
variant of catalytic domain with deletion of the Gly/Ser-rich linker, Ser244-Thr256, no expression of protein
-
M123del
Cellulosimicrobium cellulans DK-1
-
variant of catalytic domain, significant decrease in hydrolytic activity for laminarin
-
E231A
-
no enzymic activity with laminarin, in presence of sodium formate, recovery of 75% of activitiy compared to wild type, with substrate alpha-laminaribiosyl fluoride, polymerization to insoluble, crystalline (1,3)-beta-D-glucans
E231G
-
no enzymic activity with laminarin, in presence of sodium formate, recovery of 75% of activitiy compared to wild type, with substrate alpha-laminaribiosyl fluoride, polymerization to insoluble, crystalline (1,3)-beta-D-glucans
E231S
-
no enzymic activity with laminarin, with substrate alpha-laminaribiosyl fluoride, polymerization to insoluble, crystalline (1,3)-beta-D-glucans
W118A
-
the mutant almost abolishes its activity
W118A
-
the mutant almost abolishes its activity
-
W1679A
Q000P7
site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
W1688A
Q000P7
site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
W1729A
Q000P7
site-directed mutagenesis, mutation in the F5/8C module or DS domain, the mutant domain forms inclusion bodies upon expression in Escherichia coli
Y1714A
Q000P7
site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
Y1768A
Q000P7
site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
W1679A
Paenibacillus sp. BCRC
-
site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
-
W1688A
Paenibacillus sp. BCRC
-
site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
-
W1729A
Paenibacillus sp. BCRC
-
site-directed mutagenesis, mutation in the F5/8C module or DS domain, the mutant domain forms inclusion bodies upon expression in Escherichia coli
-
Y1714A
Paenibacillus sp. BCRC
-
site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
-
D287A
-
decreased activity
delI72-G75
-
deletion mutant, lacking residues 72-75, hydrolyses the mixed-linkage beta-1,3-1,4-glucan lichenan at 40C and 70C 10times more efficiently than the wiild-type protein. At 80C, the specific activity of the D-loop mutant is reduced significantly relative to that of the wild-type with both laminarin and lichenan
delMet174
-
the specific activities of the mutant LamA, on both laminarin and lichenan, is about 10fold lower than the respective wild-type value. The methionine deletion leads to an enzyme with 13.1% of wild-type Vmax and a slightly higher Km on laminarin as a substrate. With lichenan as substrate, the mutant LamA has 7.9% of the wild-type Vmax and the same Km value
E170A
-
severely reduced hydrolytic activity, active as a glycosynthase catalysing condensation of alpha-laminaribiosyl fluoride to different acceptors
E53A
-
decreased activity
S296C
-
the immobilized S296C variant shows extreme pH stability and can be repeatedly used at 60C without significant activity loss of activity
D518A
-
no activity
D526A
-
enzymatic activity is similar to that of the wild type protein
D545A
-
enzymatic activity is similar to that of the wild type protein
D570A
-
no activity
D588A
-
no activity
E609A
-
no activity
D518A
Saccharomyces cerevisiae YPA84
-
no activity
-
D526A
Saccharomyces cerevisiae YPA84
-
enzymatic activity is similar to that of the wild type protein
-
D588A
Saccharomyces cerevisiae YPA84
-
no activity
-
E609A
Saccharomyces cerevisiae YPA84
-
no activity
-
D422A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
D422E
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
D424A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
D424H
-
site-directed mutagenesis, the mutation alters the substrate specificity by increasing the rate of cleavage of mixed-linkage beta-glucan and carboxymethylcellulose 60fold and 16fold, respectively, compared to the wild-type enzyme
D424H/S501A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
E499A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
E499D
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
E503A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
E503D
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
F425A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
F425Y
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
H423A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
H426A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
N421A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
S500A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
S501A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
S502A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
W404A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
W444A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
Y427A
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
D422A
Thermobifida fusca YX-ER1
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
-
D424A
Thermobifida fusca YX-ER1
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
-
D424H
Thermobifida fusca YX-ER1
-
site-directed mutagenesis, the mutation alters the substrate specificity by increasing the rate of cleavage of mixed-linkage beta-glucan and carboxymethylcellulose 60fold and 16fold, respectively, compared to the wild-type enzyme
-
E499A
Thermobifida fusca YX-ER1
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
-
W404A
Thermobifida fusca YX-ER1
-
site-directed mutagenesis, the mutant enzyme shows altered activity with polysaccharide substrates compared with the wild-type enzyme
-
additional information
-
enzyme disruption mutant, no further effects on growth rate of mutant strains, but results in formation of chains of cells. Enzyme gene is able to complement eng1 mutants in Saccharomyces cerevisiae
Y1768A
Paenibacillus sp. BCRC
-
site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
-
additional information
-
plants resistant to infection by Orobanche crenata, enzyme is differently expressed in cells near the penetration point
E53A/D287A
-
decreased activity
additional information
-
deletion mutant lacking resiudes 72-75 hydrolyzes the mixed-linkgae beta-(1-3)-(1-4)-glucan lichenan 10times more efficiently than wild-type
E613A
-
no activity
additional information
-
an enzyme deletion strain shows decreased activity of acid trehalase
E613A
Saccharomyces cerevisiae YPA84
-
no activity
-
additional information
-
a point mutation, that destroys the catalytic activity of the protein, results in a phenotype similar to that of the mutant strain with gene eng2 placed under the control of a repressible promoter. Exogenous addition of purified Eng2 releases the ascospores from asci generated by the eng2+-deficient mutant
C6A
Q70C53
significant decrease in activity towards carboxymethyl-curdlan and laminarin, strong increase in activity towards lichenan
additional information
-
C-terminally truncated enzyme without carbohydrate-binding module, about 40% reduction of activity
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
characterization of folded and denatured states of the protein upon heat and chemical treatment, identification of a number of conformational states
-
refolding is started by 20fold dilution of the unfolding mixture, at 20C, into solutions of buffer containing decreasing guanidinium chloride concentrations
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
food industry
-
enzyme is able to hydrolyze both polymers, the beta-1,3-glucan from wine-related lactic acid bacterium Pediococcus parvus and that from yeast cell walls, which can make wine filtration difficult or impossible. Enzyme is still active under wine-relevant parameters such as elevated ethanol, sulfite, and phenol concentrations as well as at low pH values. Enzyme seems to be a useful tool to prevent slime production and undesirable yeast growth during vinification
food industry
Delftia tsuruhatensis MV01
-
enzyme is able to hydrolyze both polymers, the beta-1,3-glucan from wine-related lactic acid bacterium Pediococcus parvus and that from yeast cell walls, which can make wine filtration difficult or impossible. Enzyme is still active under wine-relevant parameters such as elevated ethanol, sulfite, and phenol concentrations as well as at low pH values. Enzyme seems to be a useful tool to prevent slime production and undesirable yeast growth during vinification
-
biotechnology
B4XEK5
beta-1,3-glucanases may be useful in fungal transformations or other biotechnological applications where low-temperature cell wall disintegration is preferred
analysis
-
structural analysis of laminarins
biotechnology
-
enzyme inhibits growth of phytopathogen Scerotium rolfsii with 50% effective dose value of 0.0027 mg/ml
biotechnology
Hypocrea lixii Rifai T24
-
enzyme inhibits growth of phytopathogen Scerotium rolfsii with 50% effective dose value of 0.0027 mg/ml
-
medicine
-
allergenic properties of enzyme are due to IgE-binding epitopes on its surface
agriculture
-
protein level and enzymatic activity of beta-1,3-glucanase are substantially increased with considerable decrease in fruit firmness by ethylene treatment and reduced exposure to white light conditions
biotechnology
-
enzyme is able to damage cell-wall structures of phytopathogenic fungi Pythium aphanidermatum and Rhizoctonic solani Ag-4
biotechnology
B4XEK7
beta-1,3-glucanases may be useful in fungal transformations or other biotechnological applications where low-temperature cell wall disintegration is preferred
agriculture
-
upon infection by Oronbanche crenata, enzyme is differently expressed in cells of a resistant host near the penetration point
agriculture
C3VPJ1
BglS27 is a good candidate for utilization in biotechnological applications such as plant protection, feed, and food preservation
biotechnology
C3VPJ1
BglS27 is a good candidate for utilization in biotechnological applications such as plant protection, feed, and food preservation
food industry
C3VPJ1
BglS27 is a good candidate for utilization in biotechnological applications such as plant protection, feed, and food preservation