Information on EC 3.2.1.73 - licheninase

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

EC NUMBER
COMMENTARY
3.2.1.73
-
RECOMMENDED NAME
GeneOntology No.
licheninase
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds
show the reaction diagram
-
-
-
-
Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds
show the reaction diagram
mechanism, kinetic model
-
Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds
show the reaction diagram
allosteric activation mechanism, feedback inhibition
-
Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds
show the reaction diagram
beta-1,3-1,4-glucanase catalyzes strict endo-hydrolysis of the beta-1,4-glycosidic linkage adjacent to a 3-O-substituted glucose residue in the mixed-linked beta-glucans via a double-displacement mechanism
Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds
show the reaction diagram
the enzyme might carry out the hydrolysis via retaining mechanism with E113 and E118 serving as the nucleophile and general acid/base, respectively,catalytic mechanism, overview
Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds
show the reaction diagram
the enzyme might carry out the hydrolysis via retaining mechanism with E113 and E118 serving as the nucleophile and general acid/base, respectively,catalytic mechanism, overview
-
Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds
show the reaction diagram
beta-1,3-1,4-glucanase catalyzes strict endo-hydrolysis of the beta-1,4-glycosidic linkage adjacent to a 3-O-substituted glucose residue in the mixed-linked beta-glucans via a double-displacement mechanism
Ruminiclostridium thermocellum DSM 1237
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
(1->3)-(1->4)-beta-D-glucan 4-glucanohydrolase
Acts on lichenin and cereal beta-D-glucans, but not on beta-D-glucans containing only 1,3- or 1,4-bonds.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
(1,3)(1,4)-beta-D-glucan-4-glucanohydrolase
-
-
(1->3,1->4)-beta-glucanase isoenzyme EII
-
-
-
-
1,3-1,4-beta-D-glucan 4-glucanohydrolase
-
-
-
-
1,3-1,4-beta-D-glucan 4-glucanohydrolase
-
-
1,3-1,4-beta-D-glucan 4-glucanohydrolase
Bacillus subtilis A3
-
-
-
1,3-1,4-beta-D-glucan 4-glucanohydrolase
-
-
1,3-1,4-beta-D-glucan glucanohydrolase
-
-
-
-
1,3-1,4-beta-D-glucan-4-glucano hydrolase
-
-
1,3-1,4-beta-D-glucan-4-glucano hydrolase
Bacillus subtilis GN156
-
-
-
1,3-1,4-beta-D-glucanase
-
-
1,3-1,4-beta-D-glucanase
Bacillus subtilis A3
-
-
-
1,3-1,4-beta-D-glucanase
-
-
1,3-1,4-beta-D-glucanase
-
1,3-1,4-beta-D-glucanase
-
-
1,3-1,4-beta-D-glucanase
Ruminiclostridium thermocellum ZJL4
-
-
-
1,3-1,4-beta-glucanase
-
-
1,3-1,4-beta-glucanase
-
-
1,3-1,4-beta-glucanase
-
1,3-1,4-beta-glucanase
Bacillus tequilensis CGX5-1
-
-
1,3-1,4-beta-glucanase
-
1,3-1,4-beta-glucanase
-
-
1,3-1,4-beta-glucanase
-
-
1,3-1,4-beta-glucanase
-
-
1,3-1,4-beta-glucanase
-
-
1,3;1,4-beta-glucan 4-glucanohydrolase
-
-
-
-
1,3;1,4-beta-glucan endohydrolase
-
-
-
-
beta-(1,3-1,4)-glucanase
-
-
beta-(1,3-1,4)-glucanase
Aspergillus niger A-25
-
-
-
beta-(1--> 3), (1--> 4)-D-glucan 4-glucanohydrolase
-
-
-
-
beta-1,3-1,4 glucanase
-
beta-1,3-1,4 glucanase
Bacillus subtilis SU40
-
-
beta-1,3-1,4-D-glucanase
-
-
beta-1,3-1,4-D-glucanase
Penicillium occitanis Pol6
-
-
-
beta-1,3-1,4-glucanase
-
beta-1,3-1,4-glucanase
Bacillus altitudinis YC-9
-
-
beta-1,3-1,4-glucanase
-
-
beta-1,3-1,4-glucanase
Bacillus licheniformis EGW039, Bacillus licheniformis EGW039(CGMCC
-
-
-
beta-1,3-1,4-glucanase
-
beta-1,3-1,4-glucanase
-
-
beta-1,3-1,4-glucanase
-
-
beta-1,3-1,4-glucanase
-
beta-1,3-1,4-glucanase
Bacillus subtilis 168
-
-
beta-1,3-1,4-glucanase
Bacillus subtilis GN156
-
-
-
beta-1,3-1,4-glucanase
-
-
beta-1,3-1,4-glucanase
-
beta-1,3-1,4-glucanase
Malbranchea cinnamomea S168
-
-
beta-1,3-1,4-glucanase
Neocallimastix patriciarum J11
-
-
beta-1,3-1,4-glucanase
-
-
beta-1,3-1,4-glucanase
-
-
beta-1,3-1,4-glucanase
-
beta-1,3-1,4-glucanase
-
-
beta-1,3-1,4-glucanase
-
beta-1,3-1,4-glucanase
-
-
beta-1,3-1,4-glucanase
-
-
beta-1,3-1,4-glucanase
-
beta-1,3-1,4-glucanase
Ruminiclostridium thermocellum DSM 1237
-
-
beta-1,3-1,4-glucanase
-
-
beta-1,3;1,4-glucanase
-
-
beta-1,3;1,4-glucanase
Aspergillus niger US368
-
-
-
beta-1-3, 1-4 glucan 4-glucanohydrolase
Thermomonospora sp.
-
-
beta-glucanase
-
-
beta-glucanase
-
-
beta-glucanase
-
-
beta-glucanase
-
-
beta-glucanase
Trichoderma koningii ZJU-T
-
-
-
BglA13
Neocallimastix patriciarum J11
gene name
-
BglA16
Neocallimastix patriciarum J11
gene name
-
BglA51
Neocallimastix patriciarum J11
gene name
-
BglM2
Neocallimastix patriciarum J11
gene name
-
BglS
Bacillus subtilis 168
-
-
bifunctional xylanase/endoglucanase
RuCelA, a bifunctional xylanase/endoglucanase, EC 3.2.1.8 and EC 3.2.1.73
CtGlu16A
Ruminiclostridium thermocellum DSM 1237
-
-
EG1
Bacillus licheniformis UEB CF
-
-
-
EGL
Penicillium occitanis Pol6
-
-
-
endo-(1,3)(1,4)-beta-glucanase
-
-
endo-(1,3;1,4)-beta-glucanase
-
endo-(1,3;1,4)-beta-glucanase
-
Endo-beta-1,3-1,4 glucanase
-
-
-
-
endo-beta-1,3-1,4-glucanase
-
-
endo-beta-1,3-1,4-glucanase
-
endo-beta-1,3-1,4-glucanase
-
-
endo-beta-1,3-1,4-glucanase
KM079629
-
endo-beta-1,3;1,4-glucan-D-glycosyl hydrolase
-
-
Fsbeta-glucanase
-
-
GHF16 TFsbeta-glucanase
-
-
GHF17 barley 1,3-1,4-beta-D-glucanase
-
-
GluIII
Aspergillus niger A-25
-
-
-
H(A16-M)
-
-
laminarinase
-
-
-
-
laminarinase
Zobellia galactanivorans DSM 12802
-
-
LicB
Ruminiclostridium thermocellum DSM 1237
-
-
-
Lichenase
-
-
-
-
Lichenase
-
-
Lichenase
Aspergillus niger US368
-
-
-
Lichenase
Bacillus altitudinis YC-9
-
-
Lichenase
Bacillus licheniformis UEB CF
-
-
-
Lichenase
Bacillus subtilis 168
-
-
Lichenase
Bacillus subtilis A3
-
-
-
Lichenase
Malbranchea cinnamomea S168
-
-
Lichenase
-
-
Lichenase
-
the multifunctional enzyme domain GH44 possesses cellulase, xylanase, and lichenase activities
Lichenase
Paenibacillus polymyxa GS01
-
the multifunctional enzyme domain GH44 possesses cellulase, xylanase, and lichenase activities
-
Lichenase
Penicillium occitanis Pol6
-
-
-
Lichenase
Ruminiclostridium thermocellum DSM 1237
-
-
Lichenase
Ruminiclostridium thermocellum ZJL4
-
-
-
Lichenase
-
-
Lichenase
KM079629
-
LicMB
Ruminiclostridium thermocellum ZJL4
-
-
-
McLic1
Malbranchea cinnamomea S168
-
-
mHG
Bacillus subtilis A3
-
-
-
Mixed linkage beta-glucanase
-
-
-
-
PlicA
gene name
PlicA
gene name
-
PtLic16A
-
gene name
XynIII
-
bifunctional xylanase showing also beta-(1,3-1,4)-glucanase activity
XynIII
Aspergillus niger A-25
-
bifunctional xylanase showing also beta-(1,3-1,4)-glucanase activity
-
CAS REGISTRY NUMBER
COMMENTARY
37288-51-0
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain A-25
-
-
Manually annotated by BRENDA team
Aspergillus niger A-25
strain A-25
-
-
Manually annotated by BRENDA team
Aspergillus niger US368
-
-
-
Manually annotated by BRENDA team
isolated from spring silt
UniProt
Manually annotated by BRENDA team
Bacillus altitudinis YC-9
isolated from spring silt
UniProt
Manually annotated by BRENDA team
parental enzymes and hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase
-
-
Manually annotated by BRENDA team
parental enzymes, hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase and hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens
-
-
Manually annotated by BRENDA team
isozymes EG1 and EG2
-
-
Manually annotated by BRENDA team
strain EGW039 (CGMCC 0635)
-
-
Manually annotated by BRENDA team
strain EGW039(CGMCC 0635)
-
-
Manually annotated by BRENDA team
Bacillus licheniformis EGW039
strain EGW039 (CGMCC 0635)
-
-
Manually annotated by BRENDA team
Bacillus licheniformis EGW039(CGMCC
strain EGW039(CGMCC 0635)
-
-
Manually annotated by BRENDA team
Bacillus licheniformis UEB CF
isozymes EG1 and EG2
-
-
Manually annotated by BRENDA team
gene bg1314
UniProt
Manually annotated by BRENDA team
hybrid from B. macerans and B. amyloliquefaciens
-
-
Manually annotated by BRENDA team
IMET B 376
-
-
Manually annotated by BRENDA team
gene bg1314
UniProt
Manually annotated by BRENDA team
gene bglS
UniProt
Manually annotated by BRENDA team
gene SU40-glu
UniProt
Manually annotated by BRENDA team
strain A3
-
-
Manually annotated by BRENDA team
strain GN156
-
-
Manually annotated by BRENDA team
Bacillus subtilis 168
gene bglS
UniProt
Manually annotated by BRENDA team
Bacillus subtilis A3
strain A3
-
-
Manually annotated by BRENDA team
Bacillus subtilis A8-8
-
-
-
Manually annotated by BRENDA team
Bacillus subtilis GN156
strain GN156
-
-
Manually annotated by BRENDA team
Bacillus subtilis SU40
gene SU40-glu
UniProt
Manually annotated by BRENDA team
isolated from Asian giant hornet, Vespa mandarinia, nest, gene bgl5-1
UniProt
Manually annotated by BRENDA team
Bacillus tequilensis CGX5-1
isolated from Asian giant hornet, Vespa mandarinia, nest, gene bgl5-1
UniProt
Manually annotated by BRENDA team
Bispora sp.
-
UniProt
Manually annotated by BRENDA team
isoenzyme I and II
-
-
Manually annotated by BRENDA team
var. miniatus
-
-
Manually annotated by BRENDA team
i.e. Malbranchea sulfurea
UniProt
Manually annotated by BRENDA team
Malbranchea cinnamomea S168
i.e. Malbranchea sulfurea
UniProt
Manually annotated by BRENDA team
BglA13; isolated from the feces of water buffalo, gene bglA13
UniProt
Manually annotated by BRENDA team
BglA16; isolated from the feces of water buffalo, gene bglA16
UniProt
Manually annotated by BRENDA team
BglA51; isolated from the feces of water buffalo, gene bglA51
UniProt
Manually annotated by BRENDA team
BglM2; isolated from the feces of water buffalo, gene bglM2
UniProt
Manually annotated by BRENDA team
Neocallimastix patriciarum J11
BglA13; isolated from the feces of water buffalo, gene bglA13
UniProt
Manually annotated by BRENDA team
Neocallimastix patriciarum J11
BglA16; isolated from the feces of water buffalo, gene bglA16
UniProt
Manually annotated by BRENDA team
Neocallimastix patriciarum J11
BglA51; isolated from the feces of water buffalo, gene bglA51
UniProt
Manually annotated by BRENDA team
Neocallimastix patriciarum J11
BglM2; isolated from the feces of water buffalo, gene bglM2
UniProt
Manually annotated by BRENDA team
Orpinomyces sp.
strain PC-2
-
-
Manually annotated by BRENDA team
L. cv. Kirara 397
-
-
Manually annotated by BRENDA team
OsEGL2; cv. Yukihikari, gene OsEGL2
UniProt
Manually annotated by BRENDA team
OsEGL1; cv. Yukihikari, gene OsEGL1
UniProt
Manually annotated by BRENDA team
parental enzymes and hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase
-
-
Manually annotated by BRENDA team
parental enzymes, hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase and hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens
-
-
Manually annotated by BRENDA team
wild-type and mutant enzymes W101F, W101Y, E103D, E103Q, D105N, D105K, E107D, E107Q, and E107H
-
-
Manually annotated by BRENDA team
strain GS01
-
-
Manually annotated by BRENDA team
Paenibacillus polymyxa GS01
strain GS01
-
-
Manually annotated by BRENDA team
gene plicA
UniProt
Manually annotated by BRENDA team
gene plicA
UniProt
Manually annotated by BRENDA team
a hypercellulolytic mutant strain
-
-
Manually annotated by BRENDA team
Penicillium occitanis Pol6
a hypercellulolytic mutant strain
-
-
Manually annotated by BRENDA team
gene RmLic16A
UniProt
Manually annotated by BRENDA team
gene RmLic16A
UniProt
Manually annotated by BRENDA team
variant microsporus
-
-
Manually annotated by BRENDA team
strain ZJL4, gene LicB
-
-
Manually annotated by BRENDA team
Ruminiclostridium thermocellum DSM 1237
-
UniProt
Manually annotated by BRENDA team
Ruminiclostridium thermocellum DSM 1237
-
-
-
Manually annotated by BRENDA team
Ruminiclostridium thermocellum ZJL4
strain ZJL4, gene LicB
-
-
Manually annotated by BRENDA team
cultivar Musketeer
Uniprot
Manually annotated by BRENDA team
Thermomonospora sp.
-
-
-
Manually annotated by BRENDA team
strain MSB8
-
-
Manually annotated by BRENDA team
strain ZJU-T
-
-
Manually annotated by BRENDA team
Trichoderma koningii ZJU-T
strain ZJU-T
-
-
Manually annotated by BRENDA team
isolated from soil metagenome, gene mt-lic
KM079629
GenBank
Manually annotated by BRENDA team
RuCelA, a bifunctional xylanase/endoglucanase, EC 3.2.1.8 and EC 3.2.1.73; isolated from rumen from a yak rumen metagenomic library, chinese yak, Bos grunniens
UniProt
Manually annotated by BRENDA team
gene Zobellia_2431
UniProt
Manually annotated by BRENDA team
Zobellia galactanivorans DSM 12802
gene Zobellia_2431
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
beta-1,3-1,4-glucanases from various microorganisms and plants belong to glycoside hydrolase families 16 and 17, respectively
evolution
the presence of expansion and several predicted secondary structures in the 3' untranslated regions of genes bglA16 and bglM2 suggest that these two genes were duplicated recently, whereas genes bglA13 and bglA16, which contain very short 3'UTRs, were replicated earlier. The activities and some characteristics of enzymes have changed during the horizontal gene transfer event. Duplicated beta-glucanase genes bglA16 and bglM2 increase the reaction efficiency of beta-glucanases and suggest that the catalytic efficiency of beta-glucanase is likely to be a criterion determining the evolutionary fate of duplicate forms in Neocallimastix patriciarum J11; the presence of expansion and several predicted secondary structures in the 3' untranslated regions of genes bglA16 and bglM2 suggest that these two genes were duplicated recently, whereas genes bglA13 and bglA16, which contain very short 3'UTRs, were replicated earlier. The activities and some characteristics of enzymes have changed during the horizontal gene transfer event. Duplicated beta-glucanase genes bglA16 and bglM2 increase the reaction efficiency of beta-glucanases and suggest that the catalytic efficiency of beta-glucanase is likely to be a criterion determining the evolutionary fate of duplicate forms in Neocallimastix patriciarum J11; the presence of expansion and several predicted secondary structures in the 3' untranslated regions of genes bglA16 and bglM2 suggest that these two genes were duplicated recently, whereas genes bglA13 and bglA16, which contain very short 3'UTRs, were replicated earlier. The activities and some characteristics of enzymes have changed during the horizontal gene transfer event. Duplicated beta-glucanase genes bglA16 and bglM2 increase the reaction efficiency of beta-glucanases and suggest that the catalytic efficiency of beta-glucanase is likely to be a criterion determining the evolutionary fate of duplicate forms in Neocallimastix patriciarum J11; the presence of expansion and several predicted secondary structures in the 3' untranslated regions of genes bglA16 and bglM2 suggest that these two genes were duplicated recently, whereas genes bglA13 and bglA16, which contain very short 3'UTRs, were replicated earlier. The activities and some characteristics of enzymes have changed during the horizontal gene transfer event. Duplicated beta-glucanase genes bglA16 and bglM2 increase the reaction efficiency of beta-glucanases and suggest that the catalytic efficiency of beta-glucanase is likely to be a criterion determining the evolutionary fate of duplicate forms in Neocallimastix patriciarum J11
evolution
the enzyme is a member of the glycosylhydrolase family GH16 containing the conserved motif EIDIEF and signal peptide
evolution
the enzyme is a member of the glycosylhydrolase faamily GH16
evolution
the enzyme belongs to the glycohydrolase family GH16
evolution
KM079629
the enzyme belongs to the glycosyl hydrolase family 8 containing the amino acid sequence ATDGDLDIAYALLLASLQW
evolution
the beta-1,3-1,4-glucanases are family-16 glycosyl hydrolases that hydrolyze 1,4-beta-D-glycosidic linkages in beta-D-glucans containing mixed 1,3 and 1,4 linkages, which are abundant polysaccharide components found in the cell walls of grasses and the endosperm of cereals
evolution
Bacillus subtilis 168
-
the beta-1,3-1,4-glucanases are family-16 glycosyl hydrolases that hydrolyze 1,4-beta-D-glycosidic linkages in beta-D-glucans containing mixed 1,3 and 1,4 linkages, which are abundant polysaccharide components found in the cell walls of grasses and the endosperm of cereals
-
evolution
Neocallimastix patriciarum J11
-
the presence of expansion and several predicted secondary structures in the 3' untranslated regions of genes bglA16 and bglM2 suggest that these two genes were duplicated recently, whereas genes bglA13 and bglA16, which contain very short 3'UTRs, were replicated earlier. The activities and some characteristics of enzymes have changed during the horizontal gene transfer event. Duplicated beta-glucanase genes bglA16 and bglM2 increase the reaction efficiency of beta-glucanases and suggest that the catalytic efficiency of beta-glucanase is likely to be a criterion determining the evolutionary fate of duplicate forms in Neocallimastix patriciarum J11; the presence of expansion and several predicted secondary structures in the 3' untranslated regions of genes bglA16 and bglM2 suggest that these two genes were duplicated recently, whereas genes bglA13 and bglA16, which contain very short 3'UTRs, were replicated earlier. The activities and some characteristics of enzymes have changed during the horizontal gene transfer event. Duplicated beta-glucanase genes bglA16 and bglM2 increase the reaction efficiency of beta-glucanases and suggest that the catalytic efficiency of beta-glucanase is likely to be a criterion determining the evolutionary fate of duplicate forms in Neocallimastix patriciarum J11; the presence of expansion and several predicted secondary structures in the 3' untranslated regions of genes bglA16 and bglM2 suggest that these two genes were duplicated recently, whereas genes bglA13 and bglA16, which contain very short 3'UTRs, were replicated earlier. The activities and some characteristics of enzymes have changed during the horizontal gene transfer event. Duplicated beta-glucanase genes bglA16 and bglM2 increase the reaction efficiency of beta-glucanases and suggest that the catalytic efficiency of beta-glucanase is likely to be a criterion determining the evolutionary fate of duplicate forms in Neocallimastix patriciarum J11; the presence of expansion and several predicted secondary structures in the 3' untranslated regions of genes bglA16 and bglM2 suggest that these two genes were duplicated recently, whereas genes bglA13 and bglA16, which contain very short 3'UTRs, were replicated earlier. The activities and some characteristics of enzymes have changed during the horizontal gene transfer event. Duplicated beta-glucanase genes bglA16 and bglM2 increase the reaction efficiency of beta-glucanases and suggest that the catalytic efficiency of beta-glucanase is likely to be a criterion determining the evolutionary fate of duplicate forms in Neocallimastix patriciarum J11
-
evolution
-
the enzyme is a member of the glycosylhydrolase family GH16 containing the conserved motif EIDIEF and signal peptide
-
evolution
-
the enzyme is a member of the glycosylhydrolase faamily GH16
-
evolution
Ruminiclostridium thermocellum DSM 1237
-
beta-1,3-1,4-glucanases from various microorganisms and plants belong to glycoside hydrolase families 16 and 17, respectively
-
physiological function
-
fibrolytic enzyme which plays an important role in the hydrolysis of polysaccharide components. It is responsible for precisely hydrolyzing beta-1,4-glycosidic bonds adjacent to the beta-1,3-linkages in lichenan or mixed-linked beta-D-glucans, yielding mainly cellotriose, cellotetraose and cellopentaose
evolution
Zobellia galactanivorans DSM 12802
-
the enzyme belongs to the glycohydrolase family GH16
-
additional information
-
both the loss of the signal peptide (29 amino acids) and the addition of the His-tag to the peptide backbone do not affect the specific activity of linear enzyme
additional information
-
the enzyme adopts a typical beta-jellyroll fold with a curved surface and the concave face forms an extended ligand binding cleft. Both catalytic residues E113 and E118 are embedded in the strand beta9. The ligand binding cleft is formed by the inner beta-sheets, four associated loops and one alpha-helix, which connect the strands beta2 to beta3 (residues 20-29), beta8 to beta9 (105-112), beta11 to beta12 (150164) and beta16 to alpha6 (250-260). The outer beta-sheets did not involve in the active site formation but might play a structural role in overall folding. Existence of a detailed interaction network in the active site and the intermediate-like configuration, overview
additional information
the enzyme adopts a typical beta-jellyroll fold with a curved surface and the concave face forms an extended ligand binding cleft. Both catalytic residues E113 and E118 are embedded in the strand beta9. The ligand binding cleft is formed by the inner beta-sheets, four associated loops and one alpha-helix, which connect the strands beta2 to beta3 (residues 20-29), beta8 to beta9 (105-112), beta11 to beta12 (150164) and beta16 to alpha6 (250-260). The outer beta-sheets did not involve in the active site formation but might play a structural role in overall folding. Existence of a detailed interaction network in the active site and the intermediate-like configuration, overview
additional information
-
in silico analysis and structure homology modelling of the enzyme's catalytic domain, LicBM3, secondary structure
additional information
the enzyme amino acid sequence shares a conserved motif EIDIEF. The predicted three-dimensional homology model of the enzyme shows the presence of catalytic residues Glu105, Glu109, and Asp107, single disulfide bridge between Cys32 and Cys61 and three calcium binding site residues Pro9, Gly45 and Asp207. Molecular modelling and molecular dynamics simulation studies reveal that the absence of calcium ion fluctuate the active site residues which are responsible for thermostability. Molecular three-dimensional model of the enzyme with bound Ca2+, overview
additional information
-
three-dimensional structure modelling
additional information
involvement of Glu269 in the catalytic machinery of the enzyme
additional information
-
molecular structure modeling and analysis
additional information
-
N-terminal amino acid sequences of isozymes EG1 and EG2 are GAAPIKKGTTKLN and DINGGGATLPQK, respectively
additional information
-
Glu56, Asp58 and Glu60 residues located in the active site cavity of the enzyme play key roles in enzyme catalysis, functioning as general acid-base residues, structure and functional relationships of Fsbeta-glucanase
additional information
the two glutamic acids in the EIDIEF motif are key residues involved in the hydrolytic activity
additional information
Bacillus licheniformis UEB CF
-
N-terminal amino acid sequences of isozymes EG1 and EG2 are GAAPIKKGTTKLN and DINGGGATLPQK, respectively
-
additional information
Bacillus subtilis 168
-
the two glutamic acids in the EIDIEF motif are key residues involved in the hydrolytic activity
-
additional information
Bacillus subtilis SU40
-
the enzyme amino acid sequence shares a conserved motif EIDIEF. The predicted three-dimensional homology model of the enzyme shows the presence of catalytic residues Glu105, Glu109, and Asp107, single disulfide bridge between Cys32 and Cys61 and three calcium binding site residues Pro9, Gly45 and Asp207. Molecular modelling and molecular dynamics simulation studies reveal that the absence of calcium ion fluctuate the active site residues which are responsible for thermostability. Molecular three-dimensional model of the enzyme with bound Ca2+, overview
-
additional information
Zobellia galactanivorans DSM 12802
-
involvement of Glu269 in the catalytic machinery of the enzyme
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(1-3,1-4)-beta-D-glucan + H2O
?
show the reaction diagram
-
i.e. barley (1-3,1-4)-beta-glucan
-
-
?
1,3-1,4-beta-D-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
1,3-1,4-beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
2,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + H2O
2,4-dinitrophenol + beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
show the reaction diagram
-
-
-
-
3,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + H2O
3,4-dinitrophenol + beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
show the reaction diagram
-
-
-
-
4-methylumbelliferyl 3-O-beta-cellobiosyl-beta-D-glucopyranoside + H2O
4-methylumbelliferone + 3-O-beta-cellobiosyl-beta-D-glucopyranoside
show the reaction diagram
-
-
-
?
4-methylumbelliferyl 3-O-beta-cellobiosyl-beta-D-glucoside
4-methylumbelliferone + 3-O-beta-cellobiosyl-beta-D-glucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
4-methylumbelliferyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc + F-
show the reaction diagram
-
-
-
-
4-methylumbelliferyl beta-D-cellobioside + beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc + F-
show the reaction diagram
-
-
-
-
4-methylumbelliferyl beta-D-cellobioside + beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc + F-
show the reaction diagram
-
-
-
-
4-methylumbelliferyl cellobiose + H2O
?
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl laminaribiose + H2O
?
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-(1,3)-beta-D-glucooligosaccharides + H2O
4-methylumbelliferol + beta-D-oligosaccharides
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-beta-D-Gal-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + H2O
?
show the reaction diagram
-
Gal substrate has a 1.3fold higher kcat/KM-value than Glc substrate
-
-
r
4-methylumbelliferyl-beta-D-Glc-(1-3)-beta-D-Glc + H2O
4-methylumbelliferone + beta-D-Glc-(1-3)-beta-D-Glc
show the reaction diagram
-
-
-
-
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + H2O
4-methylumbelliferone + beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
show the reaction diagram
-
-
-
-
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + H2O
?
show the reaction diagram
-
Gal substrate has a 1.3fold higher kcat/KM-value than Glc substrate
-
-
r
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + H2O
4-methylumbelliferone + beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
show the reaction diagram
-
-
-
-
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + H2O
4-methylumbelliferone + beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
show the reaction diagram
-
-
-
-
4-nitrophenyl beta-D-cellobioside + H2O
?
show the reaction diagram
-
1% of the activity with carboxymethyl-cellulose
-
-
?
4-nitrophenyl beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-3)-2-deoxy-beta-D-erythro-pentopyranoside + H2O
?
show the reaction diagram
-
2-deoxy analog is better substrate than corresponding 2-hydroxy substrate
-
-
?
4-nitrophenyl beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-3)-beta-D-arabinopyranoside + H2O
?
show the reaction diagram
-
2-deoxy analog is better substrate than corresponding 2-hydroxy substrate
-
-
?
alpha-laminaribiosyl fluoride + 4-methylumbelliferyl-beta-D-Glc-(1-3)-beta-D-Glc
4-methylumbelliferyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + F-
show the reaction diagram
-
-
-
-
alpha-laminaribiosyl fluoride + 4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc
4-methylumbelliferyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc + F-
show the reaction diagram
-
-
-
-
alpha-laminaribiosyl fluoride + 4-methylumbelliferyl-beta-D-glucopyranoside
4-methylumbelliferyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc + F-
show the reaction diagram
-
-
-
-
alpha-laminaribiosyl fluoride + 4-methylumbelliferyl-beta-D-xylopyranoside
4-methylumbelliferyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Xyl + F-
show the reaction diagram
-
-
-
-
alpha-laminaribiosyl fluoride + 4-nitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc
4-nitrophenyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc + F-
show the reaction diagram
-
-
-
-
alpha-laminaribiosyl fluoride + 4-nitrophenyl-beta-D-glucopyranoside
4-nitrophenyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc + F-
show the reaction diagram
-
-
-
-
alpha-laminaribiosyl fluoride + 4-nitrophenyl-beta-D-xylopyranoside
4-nitrophenyl-beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Xyl + F-
show the reaction diagram
-
-
-
-
alpha-laminaribiosyl fluoride + methyl beta-D-Glc-(1-3)-beta-D-Glc
methyl beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc + F-
show the reaction diagram
-
-
-
-
alpha-laminaribiosyl fluoride + methyl beta-D-Glc-(1-4)-beta-D-Glc
methyl beta-D-Glc-(1-3)-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc + F-
show the reaction diagram
-
-
-
-
arabinoxylan + H2O
?
show the reaction diagram
-
-
-
-
?
avicel + H2O
?
show the reaction diagram
Bacillus subtilis, Bacillus subtilis A8-8
-
50% of the activity with carboxymethyl-cellulose
-
-
?
AZO blue beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
barley beta-D-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
the enzyme produces glucosyl beta-1,3 glucosyl beta-1,4 glucose as the major end product, glucosyl beta-1,4 glucosyl beta-1,3 glucose is not detected
-
?
barley beta-glucan + H2O
?
show the reaction diagram
best substrate
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
best substrate
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
Ruminiclostridium thermocellum DSM 1237
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
Bacillus tequilensis CGX5-1
best substrate
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
Bacillus licheniformis EGW039(CGMCC
-
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
Bacillus licheniformis EGW039
-
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
Bacillus subtilis SU40
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
Trichoderma koningii ZJU-T
-
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
Malbranchea cinnamomea S168
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
Neocallimastix patriciarum J11
best substrate
-
-
?
barley beta-glucan + H2O
3-O-beta-cellobiosyl-D-glucose + 3-O-beta-cellotriosyl-D-glucose + ?
show the reaction diagram
-
-
-
?
barley beta-glucan + H2O
3-O-beta-cellobiosyl-D-glucose + 3-O-beta-cellotriosyl-D-glucose
show the reaction diagram
Bacillus licheniformis, Bacillus licheniformis UEB CF
-
-
oligosaccharides, mainly trisaccharide and tetrasaccharide
?
barley beta-glucan + H2O
cellotriose + cellotetraose + cellobiose + D-glucose
show the reaction diagram
-
-
oligosaccharides (mainly trisaccharide and tetrasaccharide) followed by disaccharide (cellobiose) and glucose are formed as the major products of hydrolysis after a prolonged incubation of 4 h
?
barley beta-glucan + H2O
cellotriose + cellotetraose + cellobiose + D-glucose
show the reaction diagram
-
best substrate
oligosaccharides, mainly trisaccharide and tetrasaccharide
?
barley beta-glucan + H2O
cellotriose + cellotetraose + cellobiose + D-glucose
show the reaction diagram
best substrate
oligosaccharides, mainly trisaccharide and tetrasaccharide
?
barley beta-glucan + H2O
cellotriose + cellotetraose + cellobiose + D-glucose
show the reaction diagram
Aspergillus niger US368
-
-
oligosaccharides (mainly trisaccharide and tetrasaccharide) followed by disaccharide (cellobiose) and glucose are formed as the major products of hydrolysis after a prolonged incubation of 4 h
?
barley beta-glucan + H2O
cellotriose + cellotetraose + cellobiose + D-glucose
show the reaction diagram
best substrate
oligosaccharides, mainly trisaccharide and tetrasaccharide
?
barley beta-glucan + H2O
cellotriose + cellotetraose + cellobiose + D-glucose
show the reaction diagram
Penicillium occitanis Pol6
-
best substrate
oligosaccharides, mainly trisaccharide and tetrasaccharide
?
barley-beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
barley-beta-glucan + H2O
?
show the reaction diagram
KM079629
best substrate, azo-barley-glucan as the substrate
-
-
?
beta-(1-3),(1-4)-D-glucan + H2O
beta-D-glucose + ?
show the reaction diagram
-
-
-
?
beta-1,3-1,4-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
beta-1,3-1,4-glucan + H2O
?
show the reaction diagram
-
from Hordeum vulgare, from Hordeum vulgare, best substrate
-
-
?
beta-1,3-1,4-glucan + H2O
?
show the reaction diagram
source of substrate: barley
-
-
?
beta-1,3-1,4-glucan + H2O
?
show the reaction diagram
Ruminiclostridium thermocellum DSM 1237
-
-
-
-
?
beta-1,3-1,4-glucan + H2O
3-O-cellobiosyl-D-glucose + 3-O-cellotriosyl-D-glucose
show the reaction diagram
beta-1,3-1,4-glucanase can hydrolyse only the beta-1,4-glycosidic bond adjacent to beta-1,3-glycosidic bond in the mixed glycosidic linkages of beta-glucan, but cannot hydrolyse the beta-1,4-glycosidic bond in cellulose, from oat and barley
-
?
beta-1,3-1,4-glucan + H2O
3-O-cellobiosyl-D-glucose + 3-O-cellotriosyl-D-glucose
show the reaction diagram
beta-1,3-1,4-glucanase can hydrolyse only the beta-1,4-glycosidic bond adjacent to beta-1,3-glycosidic bond in the mixed glycosidic linkages of beta-glucan, but cannot hydrolyse the beta-1,4-glycosidic bond in cellulose, from oat and barley
-
?
beta-1,3/1,4-glucan + H2O
?
show the reaction diagram
best substrate is 1,3/1,4-beta-glucan from Hordeum vulgare, and almost equally active from Avena sativa
-
-
?
beta-D-glucan + H2O
?
show the reaction diagram
-
the two extremely different folds adopted by GHF16 and GHF17 enzymes, beta-jellyroll and (beta/alpha)8, respectively, accommodate mixed beta-1,3 and beta-1,4 beta-D-glucans or lichenan
-
-
?
beta-D-glucan + H2O
?
show the reaction diagram
source of substrate: oat
-
-
?
beta-D-glucan + H2O
?
show the reaction diagram
source of substrate: oat
-
-
?
beta-D-glucan + H2O
?
show the reaction diagram
Bispora sp.
source: barley, best substrate
hydrolysis products from barley beta-glucan are 6.8 micromol/ml glucose and 16.3 micromol/ml cellobiose
-
?
carboxymethyl cellulose + H2O
?
show the reaction diagram
Bispora sp.
9.8% of the activity with beta-D-glucan
-
-
?
carboxymethyl-cellulose + H2O
?
show the reaction diagram
-
-
-
-
?
carboxymethyl-cellulose + H2O
?
show the reaction diagram
-
-
-
-
?
carboxymethyl-cellulose + H2O
?
show the reaction diagram
-
a negligible amount of hydrolysis of carboxymethyl-cellulose is observed
-
-
?
carboxymethyl-cellulose + H2O
?
show the reaction diagram
Trichoderma koningii ZJU-T
-
-
-
-
?
carboxymethylcellulose + H2O
?
show the reaction diagram
-
-
-
?
carboxymethylcellulose + H2O
?
show the reaction diagram
-
18% of the activity with beta-1,3-1,4-glucan from Hordeum vulgare
-
-
?
cellulose + H2O
?
show the reaction diagram
-
7% of the activity with beta-1,3-1,4-glucan from Hordeum vulgare
-
-
?
cellulose + H2O
?
show the reaction diagram
filter paper
main products are cellobiose and cellotriose
-
?
CM-cellulose + H2O
?
show the reaction diagram
KM079629
low activity
-
-
?
Glcbeta(1-3)Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-4)Glc + H2O
glucose + Glcbeta(1-3)Glcbeta(1-4)Glcbeta(1-4)Glc
show the reaction diagram
-
-
-
?
Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-3)Glcbeta(1-4)Glcbeta(1-4)Glc-OMe + H2O
?
show the reaction diagram
-
-
-
-
?
Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-3)Glc + H2O
?
show the reaction diagram
-
-
-
-
?
Glcbeta(1-4)Glcbeta(1-4)Glcbeta(1-4)Glcbeta-O-4-methylumbeliferone + H2O
?
show the reaction diagram
-
-
-
-
?
Glcbeta3Glcbeta-methylumbelliferone + H2O
?
show the reaction diagram
-
-
-
-
?
glucan tetrasaccharide + H2O
D-glucose + glucan trisaccharide
show the reaction diagram
containing two beta-1,4-linkages separated by one beta-1,3-linkage, i.e. G4G3G4G
containing one beta-1,4-linkage separated by one beta-1,3-linkage, i.e. G4G3G, which is not further degraded
?
hydroxyethylcellulose + H2O
?
show the reaction diagram
-
-
-
?
laminarin + H2O
reducing sugar + ?
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
-
70% of the activity with carboxymethyl-cellulose
-
-
?
laminarin + H2O
?
show the reaction diagram
the wild-type enzyme displays a bent topology adapted to the binding of helical-shaped laminarin
-
-
?
laminarin + H2O
?
show the reaction diagram
Bacillus subtilis A8-8
-
70% of the activity with carboxymethyl-cellulose
-
-
?
laminaritriose + H2O
D-glucose + laminaribiose
show the reaction diagram
the smallest oligosaccharide that can be degraded by the enzyme
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
?
lichenan + H2O
?
show the reaction diagram
KM079629
-
-
-
?
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
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
the enzyme produces glucosyl beta-1,3 glucosyl beta-1,4 glucose as the major end product, glucosyl beta-1,4 glucosyl beta-1,3 glucose is not detected
-
?
lichenan + H2O
?
show the reaction diagram
-
the two extremely different folds adopted by GHF16 and GHF17 enzymes, beta-jellyroll and (beta/alpha)8, respectively, accommodate mixed beta-1,3 and beta-1,4 beta-D-glucans or lichenan
-
-
?
lichenan + H2O
?
show the reaction diagram
-
85% of the activity with beta-1,3-1,4-glucan from Hordeum vulgare
-
-
?
lichenan + H2O
?
show the reaction diagram
a beta-1,3/1,4-glucan from Cetraria islandica, half as active as barley or oat beta-1,3/1,4-glucans
-
-
?
lichenan + H2O
?
show the reaction diagram
a beta-1,3/1,4-glucan from Cetraria islandica, half as active as barley or oat beta-1,3/1,4-glucans
-
-
?
lichenan + H2O
?
show the reaction diagram
-
500% of the activity with carboxymethyl-cellulose
-
-
?
lichenan + H2O
?
show the reaction diagram
68.8% of the activity with barley beta-glucan
-
-
?
lichenan + H2O
?
show the reaction diagram
Bispora sp.
72% of the activity with beta-D-glucan
hydrolysis products from lichenan are 9.1 micromol/ml glucose and 9.9 micromol/ml cellobiose, and 0.45 micromol/ml cellotetraose
-
?
lichenan + H2O
?
show the reaction diagram
Bacillus subtilis 168
-
-
-
?
lichenan + H2O
?
show the reaction diagram
Ruminiclostridium thermocellum DSM 1237
-
-
-
?
lichenan + H2O
?
show the reaction diagram
Paenibacillus polymyxa GS01
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
Bacillus altitudinis YC-9
-
-
-
?
lichenan + H2O
?
show the reaction diagram
Bacillus tequilensis CGX5-1
-
-
-
?
lichenan + H2O
?
show the reaction diagram
Bacillus licheniformis EGW039(CGMCC
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
Aspergillus niger US368
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
Bacillus subtilis A8-8
-
500% of the activity with carboxymethyl-cellulose
-
-
?
lichenan + H2O
?
show the reaction diagram
Bacillus licheniformis EGW039
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
Bacillus subtilis SU40
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
?
lichenan + H2O
?
show the reaction diagram
Malbranchea cinnamomea S168
-
-
-
?
lichenan + H2O
?
show the reaction diagram
Neocallimastix patriciarum J11
-
-
-
?
lichenan + H2O
D-glucose + ?
show the reaction diagram
Thermomonospora sp.
-
-
-
?
lichenan + H2O
reducing sugar + ?
show the reaction diagram
-
-
-
?
lichenan + H2O
reducing sugar + ?
show the reaction diagram
-
-
-
?
lichenan + H2O
reducing sugar + ?
show the reaction diagram
Bacillus subtilis A3
-
-
-
?
lichenan + H2O
reducing sugar + ?
show the reaction diagram
Trichoderma koningii ZJU-T
-
-
-
?
lichenan + H2O
lichenan oligosaccharides
show the reaction diagram
-
-
-
?
lichenan + H2O
3-O-beta-cellobiosyl-D-glucose + 3-O-beta-cellotriosyl-D-glucose
show the reaction diagram
Bacillus licheniformis, Bacillus licheniformis UEB CF
-
-
oligosaccharides, mainly trisaccharide and tetrasaccharide
?
lichenan + H2O
cellotriose
show the reaction diagram
95.2% activity compared to barley beta-glucan
oligosaccharides, mainly trisaccharide
?
lichenin + H2O
?
show the reaction diagram
-
-
-
-
?
lichenin + H2O
?
show the reaction diagram
-
-
-
-
?
lichenin + H2O
?
show the reaction diagram
Aspergillus niger A-25
-
-
-
-
?
oat beta-glucan + H2O
?
show the reaction diagram
-
-
-
?
oat beta-glucan + H2O
?
show the reaction diagram
-
-
-
?
oat beta-glucan + H2O
?
show the reaction diagram
-
-
-
?
oat beta-glucan + H2O
?
show the reaction diagram
Bacillus tequilensis CGX5-1
-
-
-
?
oat beta-glucan + H2O
?
show the reaction diagram
-
-
-
?
oat beta-glucan + H2O
?
show the reaction diagram
Malbranchea cinnamomea S168
-
-
-
?
soluble starch + H2O
?
show the reaction diagram
KM079629
low activity
-
-
?
xylan + H2O
?
show the reaction diagram
-
-
-
?
xylan + H2O
?
show the reaction diagram
KM079629
low activity
-
-
?
xylan + H2O
?
show the reaction diagram
Bacillus subtilis, Bacillus subtilis A8-8
-
500% of the activity with carboxymethyl-cellulose
-
-
?
xylan + H2O
?
show the reaction diagram
Bacillus subtilis SU40
-
-
-
?
xylan + H2O
xylose + ?
show the reaction diagram
Thermomonospora sp.
-
-
-
?
barley beta-glucan + H2O
beta-glucan oligosaccharides
show the reaction diagram
-
-
-
?
barley beta-glucan + H2O
additional information
-
-
-
pentose, triose, tetarose and a high molecular weight polysaccharide with 1,3 linkage, pentose, triose, tetrose and a high molecular weight polysaccharide with 1,3 linkage
?
barley beta-glucan + H2O
additional information
-
Bacillus subtilis GN156
-
-
pentose, triose, tetarose and a high molecular weight polysaccharide with 1,3 linkage, pentose, triose, tetrose and a high molecular weight polysaccharide with 1,3 linkage
?
beta-1,3/1,4-glucan + H2O
?
show the reaction diagram
best substrate is 1,3/1,4-beta-glucan from Hordeum vulgare, and almost equally active from Avena sativa
-
-
?
beta-D-glucan + H2O
additional information
-
-
-
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
-
?
beta-D-glucan + H2O
additional information
-
Orpinomyces sp.
-
beta-D-glucan from barley
main products are triose and tetraose
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from barley
oligosaccharides are formed as the major products, no glucose
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from oat
-
?
beta-D-glucan + H2O
additional information
-
-
beta-D-glucan from oat
oligosaccharides are formed as the major products, no glucose
?
beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
carboxymethyl beta-glucan + H2O
additional information
-
-
carboxymethyl beta-glucan from barley
trisaccharide, 53%, tetrasaccharide, 25%
?
lichenan + H2O
cellotriose + cellotetraose
show the reaction diagram
Penicillium occitanis, Penicillium occitanis Pol6
-
93.5% activity compared to barley beta-glucan
oligosaccharides, mainly trisaccharide and tetrasaccharide
?
lichenin + H2O
additional information
-
-
-
-
?
lichenin + H2O
additional information
-
-
-
-
?
lichenin + H2O
additional information
-
-
-
-
?
lichenin + H2O
additional information
-
-
-
-
?
lichenin + H2O
additional information
-
-
-
-
?
lichenin + H2O
additional information
-
-
-
-
?
lichenin + H2O
additional information
-
-
-
-
?
lichenin + H2O
additional information
-
Orpinomyces sp.
-
-
main products are triose and tetraose
?
lichenin + H2O
additional information
-
-
lichenin from Cetralia islandica and from Usnea barbata
-
?
lichenin + H2O
?
show the reaction diagram
Ruminiclostridium thermocellum ZJL4
-
-
-
-
?
additional information
?
-
-
no hydrolysis of carboxymethylpachyman
-
-
-
additional information
?
-
-
no hydrolysis of carboxymethylpachyman, no hydrolysis of starch, no hydrolysis of xylan
-
-
-
additional information
?
-
Orpinomyces sp.
-
no hydrolysis of xylan
-
-
-
additional information
?
-
-
no hydrolysis of laminarin
-
-
-
additional information
?
-
-
no hydrolysis of laminarin
-
-
-
additional information
?
-
-
no hydrolysis of laminarin
-
-
-
additional information
?
-
Orpinomyces sp.
-
no hydrolysis of laminarin
-
-
-
additional information
?
-
-
no hydrolysis of laminaran
-
-
-
additional information
?
-
-
no hydrolysis of carboxymethylcellulose
-
-
-
additional information
?
-
-
no hydrolysis of carboxymethylcellulose
-
-
-
additional information
?
-
-
no hydrolysis of carboxymethylcellulose
-
-
-
additional information
?
-
-
no hydrolysis of carboxymethylcellulose
-
-
-
additional information
?
-
Orpinomyces sp.
-
no hydrolysis of carboxymethylcellulose
-
-
-
additional information
?
-
-
no hydrolysis of pustulan
-
-
-
additional information
?
-
Orpinomyces sp.
-
no hydrolysis of pustulan
-
-
-
additional information
?
-
-
no activity against beta-1,4- or beta-1,3 homopolymers of gluco- or manno-configured polysaccharides
-
-
-
additional information
?
-
-
activity against 1% carboxymethylcellulose is not observed
-
-
-
additional information
?
-
-
carboxymethylcellulose and arabinoxylan are no substrates
-
-
-
additional information
?
-
-
carboxymethylcellulose and starch are no substrates
-
-
-
additional information
?
-
-
carboxymethylcellulose, arabinoxylan, laminarin, and starch are no substrates
-
-
-
additional information
?
-
-
does not display any activity on crystalline cellulose or laminarin
-
-
-
additional information
?
-
-
does not hydrolyze carboxymethyl-cellulose or avicel cellulose
-
-
-
additional information
?
-
-
no activity on cellulose
-
-
-
additional information
?
-
Thermomonospora sp.
-
no activity towards avicel, laminarin, gum arabic, p-nitrophenyl glucoside, and p-nitrophenyl xylopyranoside
-
-
-
additional information
?
-
-
the enzyme shows only residual activity against 1,3-beta-glucan (laminarin) or no activity at all against 1,4-beta-glucan (cellulose), chitin, xylan, or manan
-
-
-
additional information
?
-
-
the purified enzyme fraction shows no activity on laminarin and xylan
-
-
-
additional information
?
-
-
beta-glucanase does not act toward avicel, carboxymethylcellulose, cellulose, filter paper, beta-1,3-glucan, hydroxyethyl-cellulose, laminarin, starch, pullulan, birchwood xylan, locust bean gum, cellobiose, and xylobiose. No activity for p-nitrophenyl-beta-D-glucopyranoside, p-nitrophenyl-beta-D-xylopyranoside, p-nitrophenyl-beta-D-fucopyranoside, p-nitrophenyl-beta-D-galactopyranoside, and p-nitrophenyl-beta-D-mannopyranoside
-
-
-
additional information
?
-
-
does not hydrolyze laminaripentaose and cellopentaose
-
-
-
additional information
?
-
-
no activity against carboxymethylcellulose, xylan, laminarin, dextrin
-
-
-
additional information
?
-
-
lichenase hydrolyses only beta-1,4-linkages that are adjacent to beta-1,3-linkages in beta-glucans, mainly producing cellobiosyltriose and cellotriosyltetraose
-
-
-
additional information
?
-
-
also active with laminarin, poor activity with Avicel, rice straw, and xylan, no activity with 4-nitrophenyl-beta-D-hexoside derivatives, substrate specificity, overview
-
-
-
additional information
?
-
purified recombinant EGL1 protein hydrolyzes beta-1,3/1,4-glucans, but not beta-1,3/1,6-linked or beta-1,3-linked glucopolysaccharides, e.g. laminarin from Laminaria digitata or Eisenia bicyclis, or curdlan from Alcaligenes faecalis, nor carboxymethylcellulose
-
-
-
additional information
?
-
purified recombinant EGL2 protein hydrolyzes beta-1,3/1,4-glucans, but not beta-1,3/1,6-linked or beta-1,3-linked glucopolysaccharides, e.g. laminarin from Laminaria digitata or Eisenia bicyclis, or curdlan from Alcaligenes faecalis, nor carboxymethylcellulose
-
-
-
additional information
?
-
no substrate: carboxymethyl cellulose, xylan from birch, soluble starch
-
-
-
additional information
?
-
no substrate: carboxymethyl cellulose, xylan from birch, soluble starch
-
-
-
additional information
?
-
-
no substrate: cellobiose
-
-
-
additional information
?
-
Bispora sp.
poor substrates: laminarin, oat spelt xylan. No substrate: avicel
-
-
-
additional information
?
-
strictly specific for beta-1,3-1,4-glucans. No substrates are: Avicel, carboxymethyl-cellulose, cellulose, filter paper, beta-1,3-glucan, laminarin, and birchwood xylan
-
-
-
additional information
?
-
no activitiy using beta-1,3-glucan, laminarin, or Avicel as substrates
-
-
-
additional information
?
-
beta-1,3-1,4-glucanase is an endo-beta-glucanase that cleaves the beta-1,4-linkage in the presence of alphabeta-1,3-linkage in mixed-linkage beta-1,3-1,4-glucans
-
-
-
additional information
?
-
-
beta-1,3-1,4-glucanase strictly cleaves the beta-1,4-D-glucosidic bonds adjacent to beta-1,3-linkages in mixed linked beta-glucans
-
-
-
additional information
?
-
beta-1,3-1,4-glucanase strictly hydrolyzes beta-1,4-glycosidic linkage adjacent to a 3-O-substituted glucose residue in mixed linked beta-glucans but cannot act on beta-1,4-glucans
-
-
-
additional information
?
-
the enzyme catalyzes the specific hydrolysis of internal beta-1,4-glycosidic bonds adjacent to the 3-O-substituted glucose residues in mixed-linked beta-glucans. The Clostridium thermocellum enzyme exhibits a high specific activity towards barley beta-glucan and lichenan, but is not active towards laminarin, curdlan and cellulosic substrates
-
-
-
additional information
?
-
the enzyme hydrolyzes plant cell wall beta-glucans
-
-
-
additional information
?
-
the enzyme specifically catalyzes the hydrolysis of beta-1,4-glycosidic bonds located prior to beta-1,3-glycosidic linkages in 1,3-1,4-beta-glucan, enzyme substrate specificity, overview. No activity with laminarin, carboxymethyl cellulose, xylan and soluble starch
-
-
-
additional information
?
-
native and recombinant enzymes are both inactive on laminarin, cellulose, xylan, or mannan
-
-
-
additional information
?
-
-
no activity with carboxymethyl cellulose and laminarin, isozymes EG1 and EG2 exhibit no activity for pure beta-1,3 bond and for pure beta-1,4 glucan forms
-
-
-
additional information
?
-
-
no activity with carboxymethyl cellulose, laminarin, xylan, scleroglucan, and starch, substrate specificity, overview. The enzyme is inactive toward alpha-1,4, alpha-1,6, beta-1,4 and beta-1,6 linkages
-
-
-
additional information
?
-
no activity with carboxymethyl cellulose, xylan, laminarin, and soluble starch, substrate specificity, overview
-
-
-
additional information
?
-
no activity with pachyman, laminarin, starch, carboxymethyl cellulose, Avicel, and xylan
-
-
-
additional information
?
-
-
the enzyme is a conformation-retaining and is only active toward glucan containing beta-1,3-1,4-linkages. No activity with laminarin and carboxymethyl cellulose
-
-
-
additional information
?
-
the enzyme shows strict substrate specificity for barley beta-glucan, oat beta-glucan and lichenan, but is not active with other tested polysaccharides and synthetic 4-nitrophenyl derivates
-
-
-
additional information
?
-
the enzyme specifically cleaves beta-1,4-linkages next to beta-1,3-linkages and is active on linear 1,3-beta-D-glucans with 3-6 monomers and on a glucan tetrasaccharide containing two beta-1,4-linkages separated by one beta-1,3-linkage. Enzyme-substrate complex structure analysis using wild-type and mutant enzymes with glucan oligomers, binding structure and substrate recognition, overview
-
-
-
additional information
?
-
thin layer chromatography product analysis, overview. Poor activity with laminarin, no activity with birchwood xylan, carboxymethyl cellulose, pullulan, soluble starch, locust bean gum, cellulose, Avicel, beta-1,3-glucan, 4-nitrophenyl-beta-D-glucopyranoside, 4-nitrophenyl-beta-D-xylopyranoside, and 4-nitrophenyl-beta-D-galactopyranoside, substrate specificity, overview
-
-
-
additional information
?
-
thin layer product identification
-
-
-
additional information
?
-
Bacillus subtilis 168
the enzyme hydrolyzes plant cell wall beta-glucans
-
-
-
additional information
?
-
Ruminiclostridium thermocellum DSM 1237
the enzyme catalyzes the specific hydrolysis of internal beta-1,4-glycosidic bonds adjacent to the 3-O-substituted glucose residues in mixed-linked beta-glucans. The Clostridium thermocellum enzyme exhibits a high specific activity towards barley beta-glucan and lichenan, but is not active towards laminarin, curdlan and cellulosic substrates
-
-
-
additional information
?
-
Aspergillus niger A-25
-
does not hydrolyze carboxymethyl-cellulose or avicel cellulose
-
-
-
additional information
?
-
Bacillus altitudinis YC-9
beta-1,3-1,4-glucanase strictly hydrolyzes beta-1,4-glycosidic linkage adjacent to a 3-O-substituted glucose residue in mixed linked beta-glucans but cannot act on beta-1,4-glucans, native and recombinant enzymes are both inactive on laminarin, cellulose, xylan, or mannan
-
-
-
additional information
?
-
Bacillus tequilensis CGX5-1
no activity with carboxymethyl cellulose, xylan, laminarin, and soluble starch, substrate specificity, overview
-
-
-
additional information
?
-
Bacillus licheniformis EGW039(CGMCC
-
no activity on cellulose
-
-
-
additional information
?
-
Aspergillus niger US368
-
the enzyme is a conformation-retaining and is only active toward glucan containing beta-1,3-1,4-linkages. No activity with laminarin and carboxymethyl cellulose
-
-
-
additional information
?
-
Bacillus subtilis A8-8
-
no substrate: cellobiose
-
-
-
additional information
?
-
thin layer chromatography product analysis, overview. Poor activity with laminarin, no activity with birchwood xylan, carboxymethyl cellulose, pullulan, soluble starch, locust bean gum, cellulose, Avicel, beta-1,3-glucan, 4-nitrophenyl-beta-D-glucopyranoside, 4-nitrophenyl-beta-D-xylopyranoside, and 4-nitrophenyl-beta-D-galactopyranoside, substrate specificity, overview
-
-
-
additional information
?
-
Penicillium occitanis Pol6
-
no activity with carboxymethyl cellulose, laminarin, xylan, scleroglucan, and starch, substrate specificity, overview. The enzyme is inactive toward alpha-1,4, alpha-1,6, beta-1,4 and beta-1,6 linkages
-
-
-
additional information
?
-
Ruminiclostridium thermocellum ZJL4
-
lichenase hydrolyses only beta-1,4-linkages that are adjacent to beta-1,3-linkages in beta-glucans, mainly producing cellobiosyltriose and cellotriosyltetraose
-
-
-
additional information
?
-
Bacillus licheniformis EGW039
-
activity against 1% carboxymethylcellulose is not observed
-
-
-
additional information
?
-
Bacillus subtilis GN156
-
no activity against carboxymethylcellulose, xylan, laminarin, dextrin
-
-
-
additional information
?
-
Bacillus licheniformis UEB CF
-
no activity with carboxymethyl cellulose and laminarin, isozymes EG1 and EG2 exhibit no activity for pure beta-1,3 bond and for pure beta-1,4 glucan forms
-
-
-
additional information
?
-
the enzyme specifically catalyzes the hydrolysis of beta-1,4-glycosidic bonds located prior to beta-1,3-glycosidic linkages in 1,3-1,4-beta-glucan, enzyme substrate specificity, overview. No activity with laminarin, carboxymethyl cellulose, xylan and soluble starch
-
-
-
additional information
?
-
beta-1,3-1,4-glucanase is an endo-beta-glucanase that cleaves the beta-1,4-linkage in the presence of alphabeta-1,3-linkage in mixed-linkage beta-1,3-1,4-glucans, thin layer product identification
-
-
-
additional information
?
-
Trichoderma koningii ZJU-T
-
the purified enzyme fraction shows no activity on laminarin and xylan
-
-
-
additional information
?
-
Malbranchea cinnamomea S168
the enzyme shows strict substrate specificity for barley beta-glucan, oat beta-glucan and lichenan, but is not active with other tested polysaccharides and synthetic 4-nitrophenyl derivates
-
-
-
additional information
?
-
Neocallimastix patriciarum J11
no activity with pachyman, laminarin, starch, carboxymethyl cellulose, Avicel, and xylan
-
-
-
additional information
-
-
-
the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan
-
-
-
additional information
-
-
the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan
-
-
-
additional information
-
-
-
the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan. Computer modeling of active-site bound oligosaccharides, overview
-
-
-
additional information
-
-
the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan. Computer modeling of active-site bound oligosaccharides, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
barley beta-glucan + H2O
?
show the reaction diagram
Bacillus tequilensis, Bacillus tequilensis CGX5-1
K0A689
-
-
-
?
barley-beta-glucan + H2O
?
show the reaction diagram
KM079629
-
-
-
?
beta-1,3-1,4-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
beta-1,3-1,4-glucan + H2O
?
show the reaction diagram
-
from Hordeum vulgare
-
-
?
beta-1,3-1,4-glucan + H2O
3-O-cellobiosyl-D-glucose + 3-O-cellotriosyl-D-glucose
show the reaction diagram
I1W007
beta-1,3-1,4-glucanase can hydrolyse only the beta-1,4-glycosidic bond adjacent to beta-1,3-glycosidic bond in the mixed glycosidic linkages of beta-glucan, but cannot hydrolyse the beta-1,4-glycosidic bond in cellulose
-
?
beta-1,3-1,4-glucan + H2O
?
show the reaction diagram
Ruminiclostridium thermocellum DSM 1237
-
-
-
-
?
beta-1,3-1,4-glucan + H2O
3-O-cellobiosyl-D-glucose + 3-O-cellotriosyl-D-glucose
show the reaction diagram
I1W007
beta-1,3-1,4-glucanase can hydrolyse only the beta-1,4-glycosidic bond adjacent to beta-1,3-glycosidic bond in the mixed glycosidic linkages of beta-glucan, but cannot hydrolyse the beta-1,4-glycosidic bond in cellulose
-
?
laminarin + H2O
?
show the reaction diagram
G0L5X4
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
KM079629
-
-
-
?
lichenan + H2O
?
show the reaction diagram
K0A689
-
-
-
?
lichenan + H2O
?
show the reaction diagram
P04957
-
-
-
?
lichenan + H2O
?
show the reaction diagram
K7XFI7
-
-
-
?
lichenan + H2O
?
show the reaction diagram
Bacillus subtilis 168
P04957
-
-
-
?
lichenan + H2O
?
show the reaction diagram
Bacillus altitudinis YC-9
K7XFI7
-
-
-
?
oat beta-glucan + H2O
?
show the reaction diagram
Bacillus tequilensis, Bacillus tequilensis CGX5-1
K0A689
-
-
-
?
lichenan + H2O
?
show the reaction diagram
Bacillus tequilensis CGX5-1
K0A689
-
-
-
?
additional information
?
-
-
lichenase hydrolyses only beta-1,4-linkages that are adjacent to beta-1,3-linkages in beta-glucans, mainly producing cellobiosyltriose and cellotriosyltetraose
-
-
-
additional information
?
-
I1W007
beta-1,3-1,4-glucanase is an endo-beta-glucanase that cleaves the beta-1,4-linkage in the presence of alphabeta-1,3-linkage in mixed-linkage beta-1,3-1,4-glucans
-
-
-
additional information
?
-
-
beta-1,3-1,4-glucanase strictly cleaves the beta-1,4-D-glucosidic bonds adjacent to beta-1,3-linkages in mixed linked beta-glucans
-
-
-
additional information
?
-
K7XFI7
beta-1,3-1,4-glucanase strictly hydrolyzes beta-1,4-glycosidic linkage adjacent to a 3-O-substituted glucose residue in mixed linked beta-glucans but cannot act on beta-1,4-glucans
-
-
-
additional information
?
-
A3DBX3
the enzyme catalyzes the specific hydrolysis of internal beta-1,4-glycosidic bonds adjacent to the 3-O-substituted glucose residues in mixed-linked beta-glucans. The Clostridium thermocellum enzyme exhibits a high specific activity towards barley beta-glucan and lichenan, but is not active towards laminarin, curdlan and cellulosic substrates
-
-
-
additional information
?
-
P04957
the enzyme hydrolyzes plant cell wall beta-glucans
-
-
-
additional information
?
-
M9XGK2
the enzyme specifically catalyzes the hydrolysis of beta-1,4-glycosidic bonds located prior to beta-1,3-glycosidic linkages in 1,3-1,4-beta-glucan
-
-
-
additional information
-
-
-
the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan
-
-
-
additional information
-
-
E0XN39
the enzyme specifically cleaves the beta-1,4-glycosidic bonds adjacent to beta-1,3-linkages in polysaccharides such as beta-D-glucan or lichenan
-
-
-
additional information
?
-
Bacillus subtilis 168
P04957
the enzyme hydrolyzes plant cell wall beta-glucans
-
-
-
additional information
?
-
Ruminiclostridium thermocellum DSM 1237
A3DBX3
the enzyme catalyzes the specific hydrolysis of internal beta-1,4-glycosidic bonds adjacent to the 3-O-substituted glucose residues in mixed-linked beta-glucans. The Clostridium thermocellum enzyme exhibits a high specific activity towards barley beta-glucan and lichenan, but is not active towards laminarin, curdlan and cellulosic substrates
-
-
-
additional information
?
-
Bacillus altitudinis YC-9
K7XFI7
beta-1,3-1,4-glucanase strictly hydrolyzes beta-1,4-glycosidic linkage adjacent to a 3-O-substituted glucose residue in mixed linked beta-glucans but cannot act on beta-1,4-glucans
-
-
-
additional information
?
-
Ruminiclostridium thermocellum ZJL4
-
lichenase hydrolyses only beta-1,4-linkages that are adjacent to beta-1,3-linkages in beta-glucans, mainly producing cellobiosyltriose and cellotriosyltetraose
-
-
-
additional information
?
-
M9XGK2
the enzyme specifically catalyzes the hydrolysis of beta-1,4-glycosidic bonds located prior to beta-1,3-glycosidic linkages in 1,3-1,4-beta-glucan
-
-
-
additional information
?
-
I1W007
beta-1,3-1,4-glucanase is an endo-beta-glucanase that cleaves the beta-1,4-linkage in the presence of alphabeta-1,3-linkage in mixed-linkage beta-1,3-1,4-glucans
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
-
necessary for the activity of the enzyme
Ca2+
-
three Ca2+ binding sites are found in the mutant W203F structure. The primary calcium is coordinated to seven atoms in a pentagonal-bipyramidal arrangement: three backbone carbonyl oxygen atoms (Asn164, Asn189 and Gly222), one Odelta2 atom of Asn164 and three water molecules. The primary calcium binding site present in the mutant W203F structure is similar to that for the wild-type
Ca2+
activates slightly
Ca2+
slight activtion, stabilizes the enzyme at higher temperatures
Ca2+
KM079629
activates slightly
Ca2+
-
enhances the isozyme EG1 and EG2 activities by 32.7% and 12%, respectively, at 2.5 mM. Ca2+ enhances the substrate binding affinity of the enzyme and stabilize the conformation of the catalytic site
Ca2+
-
8% activation at 5 mM
Co2+
-
activates at 10 mM
Co2+
-
9% activation at 1 mM
Co2+
-
5 mM, 160% of initial activity
Co2+
10 mM, activity increased to 154%
Co2+
slight activtion
Co2+
best activating metal ion
Cu2+
-
0.3% residual activity at 12 mM
Cu2+
-
110.11% activity at 1 mM
Cu2+
10 mM, activity decreased to 86%
Cu2+
-
inhibits isozyme EG1 by 35%, but slightly activates isozyme EG2 at 2.5 mM
Fe2+
-
activates at 10 mM
Fe2+
-
20.8% increase of activity at 1 mM
Fe2+
KM079629
activates
Fe2+
-
slightly activates isozyme EG2 at 2.5 mM
Fe2+
-
50% activation at 5 mM
Fe3+
-
89.6% residual activity at 12 mM
K+
-
115.73% activity at 1 mM
K+
activates slightly
K+
-
11% activation at 5 mM
Li+
-
103.25% activity at 1 mM
Mg2+
-
95.2% residual activity at 12 mM
Mg2+
-
5.3% increase of activity at 1 mM
Mg2+
10 mM, activity decreased to 85%
Mg2+
activates by 89% at 1 mM, inhibits 50% at 10 mM
Mg2+
slight activtion
Mg2+
KM079629
activates
Mn2+
-
activates at 10 mM
Mn2+
-
62.3% residual activity at 12 mM
Mn2+
-
5 mM, 152% of initial activity
Na+
-
28% activation at 5 mM
NaCl
1.5fold activation at 0.5 M, the enzyme is acid-, alkali- and salt-tolerant, the purified recombinant His-tagged enzyme retains over 90% activity in 4 M NaCl at 25C for 24 h
Ni2+
-
19% activation at 1 mM
Triton X-100
about 20% activation
Zn2+
-
65% residual activity at 12 mM
Mn2+
KM079629
activates slightly
additional information
-
shows no sensitivity to Ca2+ and Al3+
additional information
-
Ca2+ stabilizes the enzyme at higher temperatures
additional information
no or poor effects by K+, Na+, and Mg2+
additional information
-
no effects by 10 mM of Na+, K+, Ca2+, and Mg2+
additional information
metal ions are required for enzyme activity and also disulfide linkage may be involved in catalytic activity
additional information
metal ions such as Mn2+, Na+, K+, Mg2+ and Zn2+ show little or no effect on the enzyme activity
additional information
the enzyme is halotolerant
additional information
EDTA has little effect on enzymatic activity
additional information
-
poor effects by Mg2+ and Zn2+ at 5 mM
additional information
the enzyme activity is not or poorly affected by EDTA, Tween-80, Triton X-100, H2O2, NaOCl, and diverse washing powders and soaps, overview
additional information
-
poor effects on both isozymes by Mg2+ and EDTA at 2.5 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3,4)-epoxybutyl beta-D-cellobioside
-
identification of Glu105 at the active site
1-ethyl-3-(3-dimethylaminopropyl)carbodiimide
-
-
2,4,6-Trinitrobenzenesulfonic acid
Thermomonospora sp.
-
-
2,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
-
2-mercaptoethanol
-
10 mM, 28% inhibition
2-mercaptoethanol
-
inhibits activity at a concentration of 5%
2-mercaptoethanol
-
3,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
-
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
-
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
-
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
-
5,5'-dithiobis 2-nitrobenzoic acid
Thermomonospora sp.
-
-
Ag+
-
inhibits the enzyme activity at 4 mM by 56.9%
Ag+
Bispora sp.
strong inhibition
Ba2+
-
8% inhibition at 1 mM
beta-mercaptoethanol
-
inhibits the enzyme activity at 4 mM by 82.7%
Ca2+
-
78.65% residual activity at 1 mM
Ca2+
-
90.98% residual activity at 1 mM
Ca2+
-
partially inhibited
Ca2+
-
inhibits the enzyme activity at 4 mM by 55.5%
Ca2+
-
noncompetitive
Ca2+
16% inhibition at 10 mM, 15% at 1 mM
Ca2+
-
11% inhibition at 5 mM
CaCl2
-
10 mM, 33% inhibition
Co2+
-
82.19% residual activity at 1 mM
Co2+
6% inhibition at 10 mM, 16% at 1 mM
Co2+
-
52% inhibition at 5 mM
Co2+
-
inhibits isozyme EG1 by 35%, and isozyme EG2 also slightly, at 2.5 mM
Co2+
-
40% inhibition at 5 mM
compatibility of EG1 and EG2 lichenases with solid laundry detergents
-
-
-
Cu2+
-
91.01% residual activity at 0.5 mM
Cu2+
-
44% residual activity at 1 mM
Cu2+
-
partially inhibited
Cu2+
-
completely inhibits the enzyme activity at 4 mM
Cu2+
-
14% inhibition at 1 mM
Cu2+
-
inhibits 37% at 10 mM
Cu2+
-
complete inhibition at 5 mM
Cu2+
-
inhibits isozyme EG1 by 28%, but slightly activates isozyme EG2 at 2.5 mM
Cu2+
-
40% inhibition at 5 mM
dithiothreitol
-
1 mM, 21% inhibition
DTT
-
inhibits the enzyme activity at 4 mM by 82.3%
EDTA
-
-
EDTA
-
10 mM, 18% inhibition
EDTA
-
47.3% residual activity at 60 mM
EDTA
-
79.64% residual activity at 1 mM
EDTA
-
inhibits the enzyme activity at 4 mM by 43.4%
EDTA
Bispora sp.
strong inhibition
EDTA
-
12% inhibition at 1 mM
EDTA
-
52% inhibition at 5 mM
epoxyalkyl cellobiosides
-
irreversible active-site directed inactivation, stereospecific requirements for inhibition
-
Fe2+
-
84.27% residual activity at 1 mM
Fe2+
-
slightly inhibited
Fe2+
-
inhibits the enzyme activity at 4 mM by 14.9%
Fe2+
-
inhibits 51% at 10 mM
Fe2+
92% inhibition at 10 mM
Fe2+
-
complete inhibition at 5 mM
Fe2+
-
inhibits isozyme EG1 by 50% at 2.5 mM
Fe3+
-
93.26% residual activity at 1 mM
Fe3+
-
inhibits the enzyme activity at 4 mM by 13.5%
Fe3+
-
5 mM, 58% of initial activity
Glc-beta-1,3-isofagomine
-
-
glucono-delta-lactone
-
-
H2O2
-
at 0.5% w/v hydrogen peroxide, isozymes EG1 and EG2 retain 82.8% and 90.28% of their activities, respectively. At 1% w/v hydrogen peroxide, isozyme EG2 retains 60% activity, while isozyme EG1 is completely inhibited
Hg2+
-
complete inhibition at 1 mM
Hg2+
-
completely inhibits the enzyme activity at 4 mM
Hg2+
Bispora sp.
strong inhibition
Hg2+
complete inhibition
Hg2+
-
complete inhibition of both isozymes at 2.5 mM
Hg2+
-
complete inhibition at 5 mM
imidazole
-
competitive
K+
-
95.61% residual activity at 1 mM
Li+
-
66.29% residual activity at 0.5 mM
Li+
48.5% inhibition at 10 mM, 18% at 1 mM
Mg2+
-
78.65% residual activity at 0.5 mM
Mg2+
-
slightly inhibited
Mg2+
-
inhibits the enzyme activity at 4 mM by 52.9%
Mg2+
-
8% inhibition at 1 mM
Mg2+
activates by 89% at 1 mM, inhibits 50% at 10 mM
Mg2+
-
90% inhibition at 5 mM
Mn2+
-
77.53% residual activity at 1 mM
Mn2+
-
37.29% residual activity at 1 mM
Mn2+
-
partially inhibited
Mn2+
-
completely inhibits the enzyme activity at 4 mM
Mn2+
-
67% inhibition at 1 mM
Mn2+
-
inhibits 6.5% at 10 mM
Mn2+
45% inhibition at 10 mM, 20% at 1 mM
Mn2+
-
complete inhibition at 5 mM
Na+
-
inhibits the enzyme activity at 4 mM by 47.3%; inhibits the enzyme activity at 4 mM by 80.3%
Ni2+
-
inhibits the enzyme activity at 4 mM by 11.5%
o-phthaldehyde
Thermomonospora sp.
-
-
Pb2+
-
97.75% residual activity at 0.5 mM
Pb2+
-
79.29% residual activity at 1 mM
PCMB
-
-
SDS
-
100 mM, 28% inhibition
SDS
-
inhibits activity at a concentration of 5%
SDS
-
inhibits the enzyme activity at 4 mM by 88.2%
SDS
about 55% inhibition
SDS
-
the strong anionic surfactant at 0.1% and 0.5% causes a moderate inhibition of 27.5% and 30.7% of isozyme EG2 activity. Isozyme EG1 is highly stable against SDS and retains 100% of its activity in the presence of 0.1% and 0.5% SDS
Sodium dodecyl sulfate
Bispora sp.
strong inhibition
sodium perborate
-
isozymes EG1 and EG2 retain 58% and 66.8% of their activities after 1 h of incubation at 40C in the presence of 0.2% w/v sodium perborate, respectively
-
Sr2+
-
inhibits the enzyme activity at 4 mM by 49%
Tris
-
competitive
Urea
-
14.5% residual activity at 7 mM
Zn2+
-
69.66% residual activity at 0.5 mM
Zn2+
-
88.66% residual activity at 1 mM
Zn2+
-
partially inhibited
Zn2+
-
inhibits the enzyme activity at 4 mM by 11.6%
Zn2+
-
8% inhibition at 1 mM
Zn2+
slightly inhibitory
Zn2+
-
inhibits 15% at 10 mM
Zn2+
52% inhibition at 10 mM, 44% at 1 mM
Zn2+
-
78% inhibition of isozyme EG1, poor inhibition of isozyme EG2
Zn2+
-
complete inhibition at 5 mM
Mn2+
-
complete inhibition at 5 mM
additional information
-
no inhibition up to a concentration of 10% SDS-PAGE
-
additional information
-
resistent to trypsin protease digestion
-
additional information
-
no significant effects are found for Ca2+, Mg2+, glycerol, D-sorbitol, boric acid, and EDTA
-
additional information
-
not inhibited by Li+; not inhibited by Li+, not significantly by Fe2+
-
additional information
-
substrate inhibition for 4-methylumbelliferyl laminaribiose, but not for 4-methylumbelliferyl cellobiose
-
additional information
-
no inhibition by Ca2+ and Fe2+ at 1 mM
-
additional information
-
not inhibitory: EDTA
-
additional information
-
poor inhibition at 10 mM by Co2+ and EDTA
-
additional information
KM079629
poor inhibition by Fe3+
-
additional information
-
the isozymes are highly stable in the presence of non-ionic surfactants such as Tween 80 and Triton X-100
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
slightly activating
Avicel
-
mutants show higher levels of activity compared to wild type
-
beet pulp
-
mutants show higher levels of activity compared to wild type
-
beta-mercaptoethanol
-
0.1%
N-bromosuccinimide
-
-
SDS
activates to 139.72%
SDS
slightly activating
solk floc
-
mutants show higher levels of activity compared to wild type
-
Triton X-100
activates to 221.30%
Tween-20
activates to 159.20%
Tween-80
activates to 267.73%
wheat bran
-
mutants show higher levels of activity compared to wild type
-
additional information
-
Phe205, Gly207, and Asn208 in the type II turn of the connecting loop may play a role in the catalytic function of beta-glucanase
-
additional information
-
the J18 strain produces the maximum level of extracellular beta-glucanase (135.6 U/ml) when grown in a medium containing corncob (5%, w/v) at 50C for 4 days
-
additional information
-
in contrast to barley beta-glucanase, TFs beta-glucanase possesses a unique and compact active site which requires induced-fit substrate binding for enzymatic cleavage
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.7
2,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30C
0.7
3,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30C
0.37
4-methylumbelliferyl 3-O-beta-cellobiosyl-beta-D-glucoside
-
pH 6.9, 30C
0.5
4-methylumbelliferyl 3-O-beta-cellobiosyl-beta-D-glucoside
-
pH 7.2, 30C
0.6
4-methylumbelliferyl 3-O-beta-cellobiosyl-beta-D-glucoside
-
pH 7.8, 30C
0.058
4-methylumbelliferyl cellobiose
-
-
0.19
4-methylumbelliferyl laminaribiose
-
-
1
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30C
0.5
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30C
1.36
beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
-
pH 7.0, 35C
0.34
beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
-
pH 7.0, 35C
5.3
Glcbeta3Glcbeta-methylumbelliferone
-
pH 7.0, 37C, 50 mM sodium phosphate buffer
2.29
Laminarin
-
Y123F, mg/ml
3.82
Laminarin
-
E131Q, mg/ml
3.9
Laminarin
-
Y123A, mg/ml
4.05
Laminarin
-
Y24W, mg/ml
4.42
Laminarin
-
E63Q, mg/ml
5.41
Laminarin
-
H99D, mg/ml
5.61
Laminarin
-
S90A, mg/ml
5.76
Laminarin
-
A98W, mg/ml
5.88
Laminarin
-
Y24A, mg/ml
6.1
Laminarin
-
W192A, mg/ml
6.18
Laminarin
-
R65A, mg/ml
6.73
Laminarin
-
wild type, mg/ml
7.19
Laminarin
-
W184Y, mg/ml
9.1
Laminarin
-
E63D, mg/ml
9.46
Laminarin
-
Y24F, mg/ml
11.1
Laminarin
-
H99R, mg/ml
14.7
Laminarin
-
N26A, mg/ml
0.13
lichenan
-
Y123A, mg/ml
0.14
lichenan
-
Y24W, mg/ml
0.16
lichenan
-
Y123F, mg/ml
0.26
lichenan
-
H99D, mg/ml
0.33
lichenan
-
S90A, mg/ml
0.45
lichenan
-
wild type, mg/ml
0.61
lichenan
-
A98W, mg/ml
0.68
lichenan
-
W184Y, mg/ml
0.89
lichenan
-
H99R, mg/ml
0.98
lichenan
-
pH 6.0, 40C, mutant D58N
1.04
lichenan
-
pH 6.0, 40C, mutant E60D
1.47
lichenan
-
E63Q, mg/ml
1.69
lichenan
-
pH 6.0, 40C, mutant E56D
1.91
lichenan
-
pH 6.0, 40C, wild type
1.95
lichenan
-
R65A, mg/ml
2.1
lichenan
-
pH 6.0, 40C, mutant D58E
2.1
lichenan
pH 6.0, 50C, mutant chimeric enzyme
2.19
lichenan
-
Y24F, mg/ml
2.37
lichenan
-
E131Q, mg/ml
2.5
lichenan
-
wild type
2.83
lichenan
-
expressed in Pichia pastoris
2.89
lichenan
-
expressed in Escherichia coli
3.1
lichenan
-
pH 6.0, 40C, mutant G63A
3.1
lichenan
pH 6.0, 50C, wild-type enzyme
3.13
lichenan
-
W192A, mg/ml
3.85
lichenan
-
Y24A, mg/ml
4.7
lichenan
-
N26A, mg/ml
4.8 - 5
lichenan
-
E63D, mg/ml
0.6
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30C
additional information
Barley beta-glucan
-
1.53 mg/ml; 4.36 mg/ml with substrate barley beta-glucan
0.15
beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
-
pH 7.0, 35C
additional information
carboxymethylcellulose
Km-value: 2.71 g/l at 50C, pH5.0
-
10.3
lichenan
-
pH 6.0, 40C, mutant M39F
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
-
-
-
additional information
additional information
Orpinomyces sp.
-
-
-
additional information
additional information
-
wild-type and mutant enzymes
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
2.25 mg/ml for wild-type enzyme, 2.44 mg/ml for mutant V18Y, 3.67 mg/ml for mutant W203Y, and 3.29 mg/ml for mutant V18Y/W203Y, with lichenan, pH 5.0, 50C, calculated as reducing sugar released from substrate
-
additional information
additional information
KM value for native enzyme, substrate beta-D-glucan, is 1.5 mg/ml, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, is 1.2 mg/ml
-
additional information
additional information
KM value for native enzyme, substrate beta-D-glucan, is 2.7 mg/ml, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, 1.2 mg/ml
-
additional information
additional information
-
KM-value for wild-type, substrate lichenan, 2.88 mg/ml
-
additional information
additional information
-
1.65 mg/ml with beta-1,3-1,4-glucan, at pH 6.0, 70C
-
additional information
additional information
10.0 mg/ml with barley beta-glucan, pH 6.0, 40C, recombinant enzyme
-
additional information
additional information
0.86 mg/ml with barley beta-glucan, recombinant enzyme, pH 6.0, 40C; 0.90 mg/ml barley beta-glucan, recombinant enzyme, pH 6.0, 40C; 0.94 mg/ml with barley beta-glucan, at recombinant enzyme, pH 6.0, 40C; 1.19 mg/ml with barley beta-glucan, recombinant enzyme, pH 6.0, 40C
-
additional information
additional information
-
7.9 mg/ml for recombinant wild-type enzyme, 7.2 mg/ml for recombinant optimally-modified enzyme, with AZO blue beta-glucan at pH 6.5, 40C
-
additional information
additional information
3.7 mg/ml at pH 6.2, 55C with barley beta-glucan, recombinant enzyme
-
additional information
additional information
-
Michaelis-Menten kinetics, 0.62 mg/ml with barley beta-glucan at pH 5.0, 60C,and 0.38 mg/ml with lichenan at pH 5.0, 60C
-
additional information
additional information
2.0 mg/ml with barley beta-glucan and 1.4 mg/ml with lichenan at pH 5.5, 60C
-
additional information
additional information
-
3.69 mg/ml for the wild-type enzyme and 3.30 mg/ml for mutant D56G/D221G/C263S, with barley beta-glucan at pH 5.0, 70C
-
additional information
additional information
0.69 mg/ml with barley beta-glucan, 1.11 mg/ml with oat beta-glucan, and 0.63 with lichenan, pH 10.0, 55C
-
additional information
additional information
KM079629
0.45 mg/ml with lichenan at pH 6.0, 50C
-
additional information
additional information
-
2.1 mg/ml for isozyme EG1 and 1.8 mg/ml for isozyme EG2 with lichenan at pH 5.0, 50C
-
additional information
additional information
-
5.96 mg/ml with lichenan at pH 5.5, 50C
-
additional information
additional information
-
5.3 mg/ml for mutant TFsW203F with lichenan, pH 6.0-7.0, 45C. Kinetic properties of parental TFsW203F and mutant hybrid glucanases, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.25
1,3-1,4-beta-D-glucan
Fibrobacter succinogenes
-
wild-type, expressed in Escherichia coli, pH 5.0, 50C
-
2.44
1,3-1,4-beta-D-glucan
Fibrobacter succinogenes
-
mutant V18Y, expressed in Escherichia coli, pH 5.0, 50C
-
3.29
1,3-1,4-beta-D-glucan
Fibrobacter succinogenes
-
mutant V18Y/W203Y, expressed in Escherichia coli, pH 5.0, 50C
-
3.67
1,3-1,4-beta-D-glucan
Fibrobacter succinogenes
-
mutant W203Y, expressed in Escherichia coli, pH 5.0, 50C
-
1.35
4-methylumbelliferyl cellobiose
Synechocystis sp. PCC 6803
-
-
0.327
4-methylumbelliferyl laminaribiose
Synechocystis sp. PCC 6803
-
-
109
AZO blue beta-glucan
Bacillus amyloliquefaciens
-
recombinant wild-type enzyme, pH 6.5, 40C
-
267
AZO blue beta-glucan
Bacillus amyloliquefaciens
-
recombinant optimally-modified enzyme, pH 6.5, 40C
-
0.016
Barley beta-glucan
Malbranchea cinnamomea
S6DXG7
pH 10.0, 55C
0.074
Barley beta-glucan
Bacillus subtilis
-
-
0.091
Barley beta-glucan
Bacillus subtilis
-
-
8.4
Barley beta-glucan
Synechocystis sp. PCC 6803
-
-
19.11
Barley beta-glucan
Aspergillus niger
-
pH 5.0, 60C
63.06
Barley beta-glucan
Neocallimastix patriciarum
I3W8N0, I3W8N1, I3W8N2, I3W8N3
recombinant enzyme, pH 6.0, 40C
68.19
Barley beta-glucan
Neocallimastix patriciarum
I3W8N0, I3W8N1, I3W8N2, I3W8N3
recombinant enzyme, pH 6.0, 40C
81.6
Barley beta-glucan
Paecilomyces sp.
-
calculated as D-glucose units released from beta-glucan
83.89
Barley beta-glucan
Neocallimastix patriciarum
I3W8N0, I3W8N1, I3W8N2, I3W8N3
recombinant enzyme, pH 6.0, 40C
102
Barley beta-glucan
Paecilomyces sp. J18
-
pH 5.0, 70C, wild-type enzyme
133.3
Barley beta-glucan
Neocallimastix patriciarum
I3W8N0, I3W8N1, I3W8N2, I3W8N3
recombinant enzyme, pH 6.0, 40C
143
Barley beta-glucan
Paecilomyces sp. J18
-
pH 5.0, 70C, mutant D56G/D221G/C263S
13.5
beta-1,3-1,4-glucan
Laetiporus sulphureus
-
pH 4.0, 75C, substrate from Hordeum vulgare
0.04
beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
Bacillus licheniformis
-
pH 7.0, 35C
0.91
beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
Bacillus licheniformis
-
pH 7.0, 35C
1.35
beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
Bacillus licheniformis
-
pH 7.0, 35C
2.3
Beta-D-glucan
Ruminiclostridium thermocellum
Q84C00
native enzyme, pH 6.0, 70C
9.2
Beta-D-glucan
Bacillus amyloliquefaciens
Q84F88
native enzyme, pH 6.0, 50C
20.3
Beta-D-glucan
Bacillus amyloliquefaciens
Q84F88
fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, pH 6.0, 70C
20.3
Beta-D-glucan
Ruminiclostridium thermocellum
Q84C00
fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, pH 6.0, 70C
5.3
carboxymethylcellulose
Laetiporus sulphureus
-
pH 4.0, 75C, substrate from Hordeum vulgare
-
0.0039
Laminarin
Bacillus sp.
-
E63Q
0.0097
Laminarin
Bacillus sp.
-
E63D
0.021
Laminarin
Bacillus sp.
-
W192A; Y123A
0.045
Laminarin
Bacillus sp.
-
N26A
0.056
Laminarin
Bacillus sp.
-
S90A
0.07
Laminarin
Bacillus sp.
-
Y24A
0.09
Laminarin
Bacillus sp.
-
R65A
0.095
Laminarin
Bacillus sp.
-
W184Y
0.1711
Laminarin
Bacillus sp.
-
Y24F
0.178
Laminarin
Bacillus sp.
-
H99R
0.198
Laminarin
Bacillus sp.
-
H99D
0.217
Laminarin
Bacillus sp.
-
E131Q
0.263
Laminarin
Bacillus sp.
-
wild type
0.375
Laminarin
Bacillus sp.
-
A98W
0.5
Laminarin
Bacillus sp.
-
Y24W
0.65
Laminarin
Bacillus sp.
-
Y123F
0.007
lichenan
Malbranchea cinnamomea
S6DXG7
pH 10.0, 55C
0.047
lichenan
Bacillus sp.
-
E131Q
0.2
lichenan
Paenibacillus macerans
-
mutant enzyme E107D
0.55
lichenan
Paenibacillus macerans
-
mutant enzyme E103D
0.7
lichenan
Paenibacillus macerans
-
mutant enzyme E107H
1.7
lichenan
Paenibacillus macerans
-
mutant enzyme W101Y
1.707
lichenan
Penicillium occitanis
-
pH 5.5, 50C
2.9
lichenan
Paenibacillus macerans
-
mutant enzyme W101F
3.1
lichenan
Paenibacillus macerans
-
mutant enzyme D105N
3.71
lichenan
Synechocystis sp. PCC 6803
-
calculated as D-glucose units released from lichenan
5.8
lichenan
Fibrobacter succinogenes
-
mutant E11L, 45C, pH 5.0
8.08
lichenan
Bacillus sp.
-
E63Q
13.32
lichenan
Aspergillus niger
-
pH 5.0, 60C
27
lichenan
Bacillus sp.
-
E63D
40.4
lichenan
Bacillus sp.
-
Y123A
40.5
lichenan
Bacillus sp.
-
W192A
44
lichenan
Fibrobacter succinogenes
-
mutant W203R, calculated as D-glucose units released from lichenan
60
lichenan
Bacillus licheniformis
-
isozyme EG1, pH 5.0, 50C
109
lichenan
Fibrobacter succinogenes
-
mutant Q70I, calculated as D-glucose units released from lichenan
112.6
lichenan
Bacillus sp.
-
E63D
131
lichenan
Fibrobacter succinogenes
-
mutant F40I, 45C, pH not specified in the publication
147.1
lichenan
Bacillus sp.
-
H99R
154
lichenan
Fibrobacter succinogenes
-
mutant R137Q, 40C, pH not specified in the publication
163.8
lichenan
Bacillus sp.
-
W184Y
166.4
lichenan
Paecilomyces sp.
-
calculated as D-glucose units released from lichenan
244
lichenan
Fibrobacter succinogenes
-
mutant Q70A, calculated as D-glucose units released from lichenan
262
lichenan
Bacillus sp.
-
N26A
276
lichenan
Bacillus sp.
-
H99D
302.4
lichenan
Bacillus sp.
-
E131Q
322
lichenan
Fibrobacter succinogenes
-
mutant Y42L, 45C, pH not specified in the publication
324
lichenan
Bacillus sp.
-
S90A
325
lichenan
Bacillus sp.
-
Y24A
349
lichenan
Fibrobacter succinogenes
-
mutant R137M, 40C, pH not specified in the publication
371
lichenan
Fibrobacter succinogenes
-
mutant Q70N, calculated as D-glucose units released from lichenan
401
lichenan
Fibrobacter succinogenes
-
mutant L62G, 45C, pH not specified in the publication
481
lichenan
Bacillus sp.
-
Y24F
504
lichenan
Fibrobacter succinogenes
-
mutant N72Q, calculated as D-glucose units released from lichenan
608
lichenan
Fibrobacter succinogenes
-
mutant G207-, calculated as D-glucose units released from lichenan
627
lichenan
Bacillus sp.
-
Y123F
639
lichenan
Fibrobacter succinogenes
-
mutant Q70D, calculated as D-glucose units released from lichenan
641
lichenan
Fibrobacter succinogenes
-
mutant Q70E, calculated as D-glucose units released from lichenan
699
lichenan
Fibrobacter succinogenes
-
mutant D206R, calculated as D-glucose units released from lichenan
708.3
lichenan
Bacillus licheniformis
-
isozyme EG1, pH 5.0, 50C
756
lichenan
Fibrobacter succinogenes
-
mutant N139A, 45C, pH not specified in the publication
785
lichenan
Fibrobacter succinogenes
-
mutant E85I, calculated as D-glucose units released from lichenan
787
lichenan
Bacillus sp.
-
Y24W
811
lichenan
Bacillus sp.
-
R65A
820
lichenan
Fibrobacter succinogenes
-
mutant N72A, calculated as D-glucose units released from lichenan
865
lichenan
Fibrobacter succinogenes
-
mutant F205L, calculated as D-glucose units released from lichenan
883
lichenan
Fibrobacter succinogenes
-
mutant D202L, calculated as D-glucose units released from lichenan
908
lichenan
Bacillus sp.
-
A98W
911
lichenan
Fibrobacter succinogenes
-
mutant K200M, calculated as D-glucose units released from lichenan
942
lichenan
Fibrobacter succinogenes
-
mutant N208G, calculated as D-glucose units released from lichenan
992
lichenan
Fibrobacter succinogenes
-
mutant E47I, 45C, pH not specified in the publication
1020
lichenan
Paenibacillus macerans
-
wild-type enzyme
1037
lichenan
Fibrobacter succinogenes
-
mutant R209M, calculated as D-glucose units released from lichenan
1120
lichenan
Bacillus subtilis
P04957
pH 6.0, 50C, mutant chimeric enzyme
1141
lichenan
Fibrobacter succinogenes
-
mutant K200F, calculated as D-glucose units released from lichenan
1191
lichenan
Bacillus sp.
-
wild type
1220
lichenan
Bacillus subtilis
P04957
pH 6.0, 50C, wild-type enzyme
1277
lichenan
Fibrobacter succinogenes
-
mutant T204F, calculated as D-glucose units released from lichenan
1296
lichenan
Fibrobacter succinogenes
-
wild-type, calculated as D-glucose units released from lichenan
1353
lichenan
Fibrobacter succinogenes
-
mutant G201S, calculated as D-glucose units released from lichenan
1422
lichenan
Fibrobacter succinogenes
-
mutant E85D, calculated as D-glucose units released from lichenan
1435
lichenan
Fibrobacter succinogenes
-
mutant Q70R, calculated as D-glucose units released from lichenan
1788
lichenan
Fibrobacter succinogenes
-
mutant K64A, 50C, pH not specified in the publication
1833
lichenan
Fibrobacter succinogenes
-
mutant K64M, 50C, pH not specified in the publication
1860
lichenan
Fibrobacter succinogenes
-
mutant D206N, calculated as D-glucose units released from lichenan
1955
lichenan
Fibrobacter succinogenes
-
mutant G207N, calculated as D-glucose units released from lichenan
2060
lichenan
Fibrobacter succinogenes
-
mutant D206M, calculated as D-glucose units released from lichenan
2170
lichenan
Fibrobacter succinogenes
-
mutant N44L, 55C, pH not specified in the publication
2562
lichenan
Fibrobacter succinogenes
-
mutant D202N, calculated as D-glucose units released from lichenan
2663
lichenan
Fibrobacter succinogenes
-
mutant Q81N, calculated as D-glucose units released from lichenan
2924
lichenan
Fibrobacter succinogenes
-
pH 5.0, 50C, wild-type enzyme, calculated as reducing sugar released from substrate
3026
lichenan
Fibrobacter succinogenes
-
mutant N44Q, 55C, pH not specified in the publication
3224
lichenan
Fibrobacter succinogenes
-
pH 5.0, 50C, mutant V18Y, calculated as reducing sugar released from substrate
3641
lichenan
Fibrobacter succinogenes
-
mutant Q81I, calculated as D-glucose units released from lichenan
3911
lichenan
Fibrobacter succinogenes
-
wild-type, 50C, pH 5.0
3920
lichenan
Fibrobacter succinogenes
-
truncated enzyme, calculated as D-glucose units released from lichenan
5003
lichenan
Fibrobacter succinogenes
-
pH 5.0, 50C, mutant W203Y, calculated as reducing sugar released from substrate
5090
lichenan
Fibrobacter succinogenes
-
pH 5.0, 50C, mutant V18Y/W203Y, calculated as reducing sugar released from substrate
5476
lichenan
Fibrobacter succinogenes
-
mutant W203F, calculated as D-glucose units released from lichenan
10100
lichenan
Fibrobacter succinogenes
-
pH 6.0-7.0, 45C, mutant TFsW203F
0.022
Oat beta-glucan
Malbranchea cinnamomea
S6DXG7
pH 10.0, 55C
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
394
lichenan
Bacillus subtilis
P04957
pH 6.0, 50C, wild-type enzyme
581
534
lichenan
Bacillus subtilis
P04957
pH 6.0, 50C, mutant chimeric enzyme
581
additional information
additional information
Bacillus amyloliquefaciens
Q84F88
Kcat/KM value for native enzyme, substrate beta-D-glucan, is 369 mg/ml/min, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, is 1014 mg/ml/min
2
additional information
additional information
Ruminiclostridium thermocellum
Q84C00
kcat/KM value for native enzyme, substrate beta-D-glucan, is 51 ml/mg/min, for fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, 1014 ml/mg/min
2
additional information
additional information
Fibrobacter succinogenes
-
kcat/KM-value for wild-type, substrate lichenan, 1358 ml/mg/s
2
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3.5
2,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30C
0.9
3,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30C
6
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30C
2.5
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30C
1.4
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30C
20.7
Ca2+
-
mutant W203F, pH 6.0, temperature not specified in the publication
23.9
Ca2+
-
wild-type, pH 6.0, temperature not specified in the publication
98.7
imidazole
-
wild-type, pH 6.0, temperature not specified in the publication
117
imidazole
-
mutant W203F, pH 6.0, temperature not specified in the publication
100.7
Tris
-
mutant W203F, pH 6.0, temperature not specified in the publication
255.4
Tris
-
wild-type, pH 6.0, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.197
-
concentrated crude extract, at 50C, pH 5
1.01
-
recombinant enzyme at 37C
1.57
-
pH 6.0, 40C, mutant D58E
2.43
-
pH 6.0, 40C, mutant D58N
2.57
-
pH 6.0, 40C, mutant E60D
2.7
-
purified recombinant linear enzyme and wild-type enzyme, substrate barley-beta-glucan, pH and temperature not specified in the publication
5.75
-
pH 6.0, 40C, mutant E56D
10.4
-
hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens
11.6
-
mutant E11L, 45C, pH 5.0
12.6
-
after 55.53fold purification, at 50C, pH 5
14.5
-
37C, pH 5.0
15 - 19
-
pH 6.0, mutant W105H
15 - 25
-
mutant N139A, 45C, pH not specified in the publication
15.6
-
isozyme EG1, pH 5.0, 50C, substrate lichenan
18.89
Thermomonospora sp.
-
enzyme from culture filtrate, using xylan as a substrate, at 50C, pH 7.0
23
purified enzyme without addition of agents and metal ions, with lichenan as the substrate, pH 10.0, 55C
24.83
KM079629
substrate lichenan, pH 6.0, 50C
25
Thermomonospora sp.
-
enzyme from culture filtrate, using lichenan as a substrate, at 50C, pH 7.0
29
-
pH 6.0, mutant W54F
29
-
purified native enzyme, substrate is Hordeum vulgare beta-1,3-1,4-glucan
37
-
pH 6.0, mutant W54Y
41.66
-
purified native enzyme, pH 5.5, 50C, substrate lichenan
43 - 46
-
mutant N44L, 55C, pH not specified in the publication
43.2
purified enzyme without addition of agents and metal ions, with oat beta-D-glucan as the substrate, pH 10.0, 55C
50.9
-
crude culture supernatant
52.7
purified enzyme without addition of agents and metal ions, with barley beta-D-glucan as the substrate, pH 10.0, 55C
54.3
carboxymethylcellulose as substrate, pH 5.0, 50C
58.6
hydroxyethylcellulose as substrate, pH 5.0, 50C
60 - 61
-
mutant N44Q, 55C, pH not specified in the publication
69
-
pH 6.0, mutant W141H
70
-
pH 6.0, mutant W203R
70
-
mutant W203R
77.7
purified enzyme with addition of Co2+, with barley beta-D-glucan as the substrate, pH 10.0, 55C
192
native enzyme, substrate lichenan, pH 6.0, 70C
234
-
mutant enzyme D317A, at 50C
236
-
mutant Q70I
240
-
mutant enzyme D220A, at 50C
241
-
mutant enzyme E323A, at 50C
245
-
mutant enzyme E242A, at 50C
258
-
mutant enzyme D106A, at 50C
262
-
mutant F40I, 45C, pH not specified in the publication
266
-
mutant enzyme D258A, at 50C
271
-
mutant enzyme E262A, at 50C
273
-
mutant enzyme D100A, at 50C
274
-
mutant enzyme D195A, at 50C
275
native enzyme, substrate beta-D-glucan, pH 6.0, 70C
283.8
-
recombinant enzyme from crude extract, using barley beta-glucan as a substrate
296
-
mutant enzyme D196A, at 50C
308
-
mutant R137Q, 40C, pH not specified in the publication
419
-
pH 6.0, mutant W141F
480
-
pH 6.0, mutant W148F
502
-
pH 6.0, 40C, mutant G63A
527
-
mutant Q70A
545
-
pH 6.0, 40C, mutant M39F
555.1
-
purified enzyme
598.6
Thermomonospora sp.
-
after 31.6fold purification, using xylan as a substrate, at 50C, pH 7.0
626
-
substrate lichenan, pH 6.0-7.0, 45C, mutant TFsW203F
644
-
mutant Y42L, 45C, pH not specified in the publication
699
-
mutant R137M, 40C, pH not specified in the publication
748
-
mutant enzyme D314A, at 50C
754
-
wild type enzyme, at 50C
767
-
isozyme EG2, pH 5.0, 50C, substrate lichenan
792.2
Thermomonospora sp.
-
after 31.6fold purification, using lichenan as a substrate, at 50C, pH 7.0
802
-
mutant Q70N
803
-
mutant L62G, 45C, pH not specified in the publication
851
native enzyme, substrate lichenan, pH 6.0, 50C
916
-
pH 6.0, mutant W112F
969
-
mutant G207-
1089
-
mutant N72Q
1106
native enzyme, substrate beta-D-glucan, pH 6.0, 50C
1114
-
mutant D206R
1280
-
recombinant enzyme, using barley beta-glucan as a substrate, at 50C and pH 6.0
1329
-
-
1335
-
recombinant enzyme, using lichenan as a substrate, at 50C and pH 6.0
1377
-
mutant F205L
1381
-
mutant Q70D
1385
-
mutant Q70E
1388
-
pH 6.0, 40C, wild type
1406
-
mutant D202L
1452
-
mutant K200M
1501
-
mutant N208G
1572
-
pH 6.0, mutant W165H
1621
-
pH 6.0, mutant W105F
1652
-
mutant R209M
1699
-
mutant E85I
1746
fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate lichenan, pH 6.0, 70C
1746
fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate lichenan, pH 6.0, 70C
1755
-
pH 6.0, mutant W198F
1774
-
mutant N72A
1791
-
pH 6.0, mutant W165F
1817
-
mutant K200F
1906
-
recombinant enzyme, using lichenan as a substrate
1986
-
mutant E47I, 45C, pH not specified in the publication
2034
-
mutant T204F
2065
-
pH 6.0, wild type
2065
-
wild type, sodium citrate buffer, pH 6.0, 50C, 10 min
2065
-
wild-type
2155
-
mutant G201S
2373
purified native enzyme, pH 6.0, 65C
2434
fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, pH 6.0, 70C
2434
fusion protein encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, substrate beta-D-glucan, pH 6.0, 70C
2479
-
recombinant enzyme after 8.74fold purification, using barley beta-glucan as a substrate
2717
-
recombinant wild-type enzyme, pH 6.5, 40C, substrate AZO blue beta-glucan
2740
Bispora sp.
substrate lichenan, pH 5.0, 60C
2941
-
pH 6.0, mutant W186F
2962
-
mutant D206N
3076
-
mutant E85D
3104
-
mutant Q70R
3115
-
mutant G207N
3282
-
mutant D206M
3370
-
recombinant optimally-modified enzyme, pH 6.5, 40C, substrate AZO blue beta-glucan
3581
-
mutant K64A, 50C, pH not specified in the publication
3659
Orpinomyces sp.
-
-
3671
-
mutant K64M, 50C, pH not specified in the publication
3722
-
hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase
4040
Bispora sp.
substrtae beta-D-glucan, pH 5.0, 60C
4081
-
mutant D202N
5393
purified recombinant enzyme, pH 6.0, 65C
5694
-
wild-type, expressed in Escherichia coli, pH 5.0, 50C
5758
-
mutant Q81N
6242
-
122.5fold purified enzyme
6520
-
mutant V18Y, expressed in Escherichia coli, pH 5.0, 50C
7055
purified recombinant His-tagged enzyme, substrate barley beta-glucan, pH 6.2, 55C
7500
purified recombinant enzyme, substrate barley beta-glucan, pH 6.0, 40C
7833
-
wild-type, 50C, pH 5.0
7873
-
mutant Q81I
7980
-
expressed in Escherichia coli, sodium citrate buffer, pH 6.0, 50C, 10 min
8208
substrate lichenan, pH 7.0, 70C
8478
-
truncated enzyme
8726
-
pH 6.0, mutant W203F
8726
-
mutant W203F
9263
-
mutant W203Y, expressed in Escherichia coli, pH 5.0, 50C
9967
-
mutant V18Y/W203Y, expressed in Escherichia coli, pH 5.0, 50C
10800
-
expressed in Pichia pastoris X-33, sodium citrate buffer, pH 6.0, 50C, 10 min
11940
substrate barley beta-glucan, pH 7.0, 70C
26530
purified recombinant enzyme, pH 6.0, 40C, substrate barley beta-glucan
28820 - 33480
purified native enzyme, substrate barley beta-glucan, pH 5.5, 60C
32100
purified recombinant enzyme, pH 6.0, 40C, substrate barley beta-glucan
39520
purified recombinant enzyme, pH 6.0, 40C, substrate barley beta-glucan
41210
purified recombinant enzyme, pH 6.0, 40C, substrate barley beta-glucan
additional information
-
-
additional information
-
-
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.5
Bispora sp.
three activity peaks at pH 1.5, 3.5, and 5.0. At pH 1.5, 61% of the activity at pH 5.0
3.5
Bispora sp.
three activity peaks at pH 1.5, 3.5, and 5.0. At pH 3.5, 91% of the activity at pH 5.0
3.6 - 5.6
-
-
4
-
two optima at pH 4 and 6.5
4
-
two optima at pH 4.0 and 6.3
4
-
two optima at pH 4 and 6.5
4.5
-
wild type, mutant H300P
5
Bispora sp.
three activity peaks at pH 1.5, 3.5, and 5.0. Maximum activity at pH 5.0
5
-
wild-type and mutant E11L
5
-
mutant D56G/D221G/C263S
5
-
isozyme EG1
5.5
-
mutant C263S
5.6
-
recombinant enzyme
5.6 - 6.6
-
hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase
5.8 - 6.2
Orpinomyces sp.
-
-
6
-
recombinant enzyme
6
recombinant enzyme
6
-
mutant D56G
6
recombinant mutant chimeric laccase/beta-1,3-1,4-glucanase enzyme, substrate lichenan
6 - 7
-
-
6 - 7
-
recombinant proteins
6 - 7
-
assay at
6 - 8
-
wild type
6.3
-
two optima at pH 4.0 and 6.3
6.5
-
two optima at pH 4 and 6.5
6.5 - 7.5
-
-
7
Thermomonospora sp.
-
-
7
-
wild-type enzyme and mutant D221G
7
-
isozyme EG2
7 - 8
-
hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens
7 - 8
-
hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens
additional information
-
amino acid residues at positions 56 and 263 are important in determining optimal pH activity
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 10
-
activity range, wild-type and mutant enzymes, profile overview
3 - 11
over 50% of maximal activity within this range, profile overview
3 - 5.5
-
79% and 73% of the maximum activity, respectively, at pH 3.5 and pH 4.5
3 - 6
-
pH 3.0: about 50% of maximal activity, pH 6.0: about 40% of maximal activity
3 - 6.5
-
activity range, profile overview
3.5 - 10
recombinant His-tagged enzyme, activity range, profile, overview
3.5 - 7.5
activity range, profile overview
4 - 10
-
isozyme EG1, more than 80% of maximal activity within pH range pH 4.0-7.0, 50% at pH 10.0. Isozyme Eg2 shows over 70% of maximal activity at pH 4.0-10.0
4 - 11
-
activity range, recombinant enzyme, profile overview
4 - 11
pH profile overview
4 - 8
KM079629
activity range, no activity below or above
4.5 - 8
activity range, over 80% activity within the range of pH 5.0-7.5, recombinant enzyme
4.5 - 8
-
activity range, wild-type and optimally-modified enzymes, overview
5 - 12
50% of maximal activity within this range
5 - 12.5
-
half-maximal activity at pH 5.0 and at pH 12.5
5.2 - 8
-
50% of maximal activity at pH 5.2 and pH 8.0
5.4 - 7
Orpinomyces sp.
-
about 80% of maximal activity at pH 5.4 and at pH 7.0
5.5 - 6
-
mutant enzyme E107H
5.5 - 7
-
more than 80% of maximal activity at pH 5.5 and pH 7.0
5.9 - 6.5
-
more than 80% of maximal activity at pH 5.9 and pH 6.5
5.9 - 8.5
-
more than 80% of maximal activity at pH 5.9 and pH 8.5
6 - 11
-
pH 6.0: about 55% of maximal activity, pH 11.0: about 45% of maximal activity
6 - 7
-
wild-type enzyme and mutant enzymes W101F, W101Y, E103D, D105N and E107D
6 - 9
-
with 50% of the activity remaining at pH 9
40 - 80
activity profile, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
recombinant enzyme
40
-
mutants R137M and R137Q
40
recombinant enzyme
45
Orpinomyces sp.
-
-
45
-
recombinant enzyme
45
-
mutants E11L, F40I, Y42L, E47I, L62G, and N139A
50
-
lichenin or oat beta-D-glucan as substrate
50
Thermomonospora sp.
-
-
50
-
wild-type, mutants K64A and K64M
50
recombinant mutant chimeric laccase/beta-1,3-1,4-glucanase enzyme, substrate lichenan
50 - 60
-
-
55
-
mutants N44L and N44Q
60
Bispora sp.
-
60
-
isozyme EG2
65
native and recombinant enzyme
70
-
recombinant enzyme
70
-
isozyme EG1
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 90
over 50% of maximal activity within this range, profile overview. The enzyme shows 75, 88, 90 and 80% activity at 20, 40, 60 and 80C, respectively
20 - 70
-
30 min with about 50% of activity remaining at 50C; the remaining activity decreased to 20% at 20-40C and is completely destroyed at 50-70C
20 - 70
KM079629
activity range, profile overview
30 - 60
-
30C, about 30% of maximal activity with oat beta-D-glucan, about 45% of maximal activity with lichenin, 60C: about 20% of maximal activity with lichenin and oat beta-D-glucan as substrate
30 - 70
recombinant His-tagged enzyme, activity range, profile, overview
30 - 80
temperature profile overview
35 - 65
-
activity range, wild-type and optimally-modified enzymes, overview
37 - 65
-
more than 80% of maximal activity at 37C and at 65C
40 - 55
-
about 60% of maximal activity at 40C and at 55C
40 - 60
-
40C: about 60% of maximal activity, 60C: about 20% of maximal activity
40 - 65
-
40C: about 60% of maximal activity, 65C: about 50% of maximal activity
40 - 65
-
about 40% of maximal activity at 40C and at 65C
40 - 65
-
40C: about 80% of maximal activity, 65C: about 60% of maximal activity
40 - 65
high activity within this range, recombinant enzyme
40 - 65
activity range, profile overview
40 - 80
-
40C: about 40% of maximal activity, 80C: about 30% of maximal activity
40 - 80
-
activity range, recombinant enzyme
40 - 80
-
activity range, profile overview
40 - 90
-
activity range, wild-type and mutant enzymes, profile overview
45 - 65
-
45C: about 80% of maximal activity, 65C: about 90% of maximal activity
45 - 90
-
at temperatures of 60C and 85C, the enzyme activity is 85% and 80% of maximal activity, respectively
55 - 75
-
more than 80% of maximal activity at 55C and at 75C
55 - 90
-
55C: about 50% of maximal activity, 90C: about 30% of maximal activity
60 - 80
-
-
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5
-
isoelectric focusing
3.6
-
isoelectricfocusing
3.9
sequence calculation
4.2
-
isoelectric focusing
4.27
Thermomonospora sp.
-
isoelectric focusing
6.76
sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
isoenzyme II is synthesized exclusively in the aleurone layer, isoenzyme III is detected in scutellum and aleurone layer
Manually annotated by BRENDA team
Orpinomyces sp.
-
recombinant enzyme expressed in E. coli
Manually annotated by BRENDA team
Bacillus subtilis GN156
-
-
-
Manually annotated by BRENDA team
-
enzyme level increases with leaf development and decreases with leaf aging, depletion of sugars results in increase of enzyme protein and activity, elevated carbohydrate contents causes a rapid decrease in enzyme abundance
Manually annotated by BRENDA team
-
second leaf, enzyme protein increases upon incubation in the dark and disappears upon illumination or feeding with sucrose
Manually annotated by BRENDA team
gene OsEGL1 is expressed in seedling, and young and adult plant roots
Manually annotated by BRENDA team
-
isoenzyme I is synthesized predominantly in the scutellum, isoenzyme III is detected in scutellum and aleurone layer
Manually annotated by BRENDA team
-
transfer from antural light/dark cycle into darkness induces eisozyme EI
Manually annotated by BRENDA team
additional information
-
the optimum temperature for the fungal growth is 28C, the fungus does not grow above 42C
Manually annotated by BRENDA team
additional information
isolated from rumen from a yak rumen metagenomic library, chinese yak, Bos grunniens
Manually annotated by BRENDA team
additional information
-
optimization of production of beta-glucanase with barley flour as the sole carbon source
Manually annotated by BRENDA team
additional information
high-level extracellular enzyme production of 6230 U/mL on oat flour at 3% w/v as a carbon source at 50 C
Manually annotated by BRENDA team
additional information
-
strain Pol6 produces high level of extracellular lichenase when grown in a medium containing oat flour (2%, w/v) at 30C for 7 days. Highest lichenases activity is obtained on the cellulose (50 U/ml) and oat flour (45 U/ml) as a carbon sources
Manually annotated by BRENDA team
additional information
Aspergillus niger US368
-
optimization of production of beta-glucanase with barley flour as the sole carbon source
-
Manually annotated by BRENDA team
additional information
Penicillium occitanis Pol6
-
strain Pol6 produces high level of extracellular lichenase when grown in a medium containing oat flour (2%, w/v) at 30C for 7 days. Highest lichenases activity is obtained on the cellulose (50 U/ml) and oat flour (45 U/ml) as a carbon sources
-
Manually annotated by BRENDA team
additional information
-
high-level extracellular enzyme production of 6230 U/mL on oat flour at 3% w/v as a carbon source at 50 C
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Orpinomyces sp.
-
recombinant enzyme expressed in Escherichia coli
-
Manually annotated by BRENDA team
Orpinomyces sp.
-
-
Manually annotated by BRENDA team
Aspergillus niger US368, Bacillus sp. SJ-10, Bacillus subtilis GN156, Penicillium occitanis Pol6, Rhizomucor miehei CAU432
-
-
-
-
Manually annotated by BRENDA team
additional information
-
the wild-type enzyme contains a signal peptide
-
Manually annotated by BRENDA team
additional information
KM079629
the enzyme contains a signal peptide
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)
Fibrobacter succinogenes (strain ATCC 19169 / S85)
Fibrobacter succinogenes (strain ATCC 19169 / S85)
Fibrobacter succinogenes (strain ATCC 19169 / S85)
Fibrobacter succinogenes (strain ATCC 19169 / S85)
Fibrobacter succinogenes (strain ATCC 19169 / S85)
Fibrobacter succinogenes (strain ATCC 19169 / S85)
Fibrobacter succinogenes (strain ATCC 19169 / S85)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
12000
-
discrepancy between molecular weight determined by gel filtration and low speed equilibrium sedimentation is probably due to a moderate interaction between the enzyme and the Sephadex polmer, gel filtration
171536
25000
-
SDS-PAGE
695667
25300
-
SDS-PAGE
679391
27000
-
discrepancy between molecular weight determined by gel filtration and low speed equilibrium sedimentation is probably due to a moderate interaction between the enzyme and the Sephadex polmer, low speed sedimentation without reaching equilibrium
171536
27700
-
enzyme I, ultracentrifugation
171532
27900
-
SDS-PAGE
681336
28000
-
recombinant enzyme with a six-His tag at the N terminus, SDS-PAGE
677726
29000
-
SDS-PAGE
677775
31000
-
SDS-PAGE
680529
31690
-
mass spectrometry
698410
32000
-
gel filtration
171539
33700
gel filtration
729865
33730
-
mass spectrometry
678923
33800
-
enzyme II, ultracentrifugation
171532
34000
-
SDS-PAGE
677749
34600
-
gel filtration
698410
36500
-
SDS-PAGE
678923
37200
-
gel filtration
171528
46900
gel filtration
730139
52000
-
gel filtration
709502
55000
-
SDS-PAGE
680529
55000
-
isozyme EG2, native PAGE
730844
60000
-
SDS-PAGE
680529
60600
calculated mass
717134
63000
-
SDS-PAGE
680529
64120
Thermomonospora sp.
-
gel filtration
678492
64240
Thermomonospora sp.
-
calculated from amino acid sequence
678492
64500
Thermomonospora sp.
-
SDS-PAGE
678492
66730
Thermomonospora sp.
-
MALDI-TOF mass spectrometry
678492
90000
-
SDS-PAGE, J2 is composed of three protein subunits of 40, 32 and 18 kDa
695667
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 27500, enzyme inactivated by epoxyalkyl beta-D-oligoglucosides
?
-
x * 24000, SDS-PAGE
?
-
x * 30000, SDS-PAGE
?
-
x * 26000, SDS-PAGE
?
Orpinomyces sp.
-
x * 27000, recombinant enzyme, SDS-PAGE; x * 27929, calculation from nucleotide sequence
?
-
x * 32085, calculation from nucleotide sequence
?
-
x * 30000, SDS-PAGE
?
-
x * 29000, SDS-PAGE
?
-
x * 35000, recombinant enzyme, SDS-PAGE
?
-
x * 33500, SDS-PAGE, recombinant enzyme with His-tag
?
Bispora sp.
x * 45170, calculated, x * 60000-80000, SDS-PAGE of recombinant enzyme, x * 48000, SDS-PAGE after Endo H treatment
?
x * 38500, SDS-PAGE, x * 31923, calculated
?
-
x * 55000, SDS-PAGE
?
x * 28000, about, recombinant catalytic domain, SDS-PAGE
?
x * 27470, sequence calculation. x * 45000, recombinant tagged enzyme, SDS-PAGE
?
x * 26900, about, sequence calculation, x * 24000, recombinant enzyme, SDS-PAGE
?
x * 24000, recombinant enzyme, SDS-PAGE
?
x * 26800, about, sequence calculation
?
x * 239000, about, sequence calculation, x * 25000, recombinant His-tagged enzyme, SDS-PAGE
?
-
x *32000, SDS-PAGE
?
KM079629
x * 45133, sequence calculation, x * 41694, recombinant enzyme without signal peptide, SDS-PAGE
?
-
x * 20000, SDS-PAGE
?
x * 28000, recombinant enzyme, SDS-PAGE, x * 96000, recombinant CotA-BglS chimeric mutant enzyme, SDS-PAGE
?
Aspergillus niger US368
-
x *32000, SDS-PAGE
-
?
Bacillus altitudinis YC-9
-
x * 27470, sequence calculation. x * 45000, recombinant tagged enzyme, SDS-PAGE
-
?
-
x * 26800, about, sequence calculation
-
?
Bacillus subtilis 168
-
x * 28000, recombinant enzyme, SDS-PAGE, x * 96000, recombinant CotA-BglS chimeric mutant enzyme, SDS-PAGE
-
?
Bacillus subtilis A8-8
-
x * 55000, SDS-PAGE
-
?
Bacillus subtilis SU40
-
x * 24000, recombinant enzyme, SDS-PAGE
-
?
Bacillus tequilensis CGX5-1
-
x * 26900, about, sequence calculation, x * 24000, recombinant enzyme, SDS-PAGE
-
?
-
x * 239000, about, sequence calculation, x * 25000, recombinant His-tagged enzyme, SDS-PAGE
-
?
Penicillium occitanis Pol6
-
x * 20000, SDS-PAGE
-
?
Ruminiclostridium thermocellum DSM 1237
-
x * 28000, about, recombinant catalytic domain, SDS-PAGE
-
dimer
-
2 * 26000, SDS-PAGE
monomer
-
1 * 35200, SDS-PAGE
monomer
-
1 * 28000, enzyme II, SDS-PAGE; 1 * 28000, enzyme I, SDS-PAGE
monomer
-
1 * 31000, SDS-PAGE
monomer
-
1 * 38600, SDS-PAGE
monomer
-
1 * 27000, recombinant mature circular enzyme variant LicA-C1 without intein sequences, SDS-PAGE
monomer
1 * 35400, SDS-PAGE, 1 * 31564, sequence calculation
monomer
1 * 44700, SDS-PAGE
monomer
-
1 * 30000, isozyme EG1, SDS-PAGE, 1 * 50000, isozyme EG2, SDS-PAGE
monomer
Bacillus licheniformis UEB CF
-
1 * 30000, isozyme EG1, SDS-PAGE, 1 * 50000, isozyme EG2, SDS-PAGE
-
monomer
Malbranchea cinnamomea S168
-
1 * 44700, SDS-PAGE
-
monomer
-
1 * 35400, SDS-PAGE, 1 * 31564, sequence calculation
-
additional information
-
four protein bands of approximately 40, 32, 25 and 18 kDa are resolved from pJ2
additional information
-
the Thr-Pro box has a positive effect while the dockerin domain has a negative impact on the properties of LicMB. The N-terminal residues 10-25 and C-terminal residues 1-9 of LicMB-CD are necessary to retain high thermostability, while the N-terminal residues 1-7 and C-terminal residues 1-3 are not necessary to maintain enzymatic activity
additional information
peptide mapping of native enzyme
additional information
-
molecular structure modeling and analysis
additional information
Bacillus subtilis GN156
-
four protein bands of approximately 40, 32, 25 and 18 kDa are resolved from pJ2
-
additional information
-
peptide mapping of native enzyme
-
additional information
Ruminiclostridium thermocellum ZJL4
-
the Thr-Pro box has a positive effect while the dockerin domain has a negative impact on the properties of LicMB. The N-terminal residues 10-25 and C-terminal residues 1-9 of LicMB-CD are necessary to retain high thermostability, while the N-terminal residues 1-7 and C-terminal residues 1-3 are not necessary to maintain enzymatic activity
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
no glycoprotein
Bispora sp.
five potential N-glycosylation site Asn-Xaa-Thr/Ser-Zaa, where Zaa is not Pro, are found. Endo H treatment decreases molecular mass from 60000-80000 to 48000, SDS-PAGE
proteolytic modification
Bispora sp.
presence of an N-terminal signal peptide at residues 1-9
glycoprotein
-
expressed in Pichia pastoris
glycoprotein
-
enzyme I contains 0.7% carbohydrate of which three residues are probably N-acetylglucosamine, enzyme II contains 3.6% carbohydrate
proteolytic modification
Orpinomyces sp.
-
a N-terminal signal peptide of 29 amino residues is cleaved from the enzyme secreted from Orpinomyces whereas 21 amino acid residues of the signal peptide are removed when the enzyme is produced by E. coli
no glycoprotein
no N-glycosylation sites present in the protein, Endo H treatment does not result in a protein band shift
glycoprotein
the enzyme contains two possible N-glycosylation sites at 72 (NKT) and 275 (NPT), respectively
glycoprotein
-
the enzyme contains two possible N-glycosylation sites at 72 (NKT) and 275 (NPT), respectively
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
enzyme-substrate complex, experiments by car-Parinello molecular dynamics simulations combined with force field molecular dynamics QM/MM CPMD, substrate 4-methylumbelliferyl tetrasaccharide
-
H(A16-M) in complex with beta-glucan tetrasaccharide, resolution range from 34.5 A to 1.64 A, hanging-drop vapour diffusion, room temperature
-
hybrid enzyme
-
the crystal structure of the enzyme is used for structure modelling, PDB ID 3O5S
apo-form and substrate complex structures of mutant V18Y/W203Y, to 1.53 A resolution; purified recombinant mutant V18Y/W203Y alone and in complex with product cellotetraose , from 0.1 M TrisHCl, pH 7.5, 0.3 M calcium acetate, and 29% PEG 5000 MME for the free mutant, and 0.15 M Tris, pH 8.5, 0.4 M calcium acetate and 33% PEG 5000 MME plus soaking in mother liquor with 5 mM cellotetraose for 1 h for the complexed mutant, X-ray diffraction structure determination and analysis at 1.53 A resolution, molecular replacement method
-
mutant E85I, at 2.2 A resolution, by hanging-drop vapour-diffusion method at room temperature. The mutant crystallizes in space group P3121 with one molecule in the asymmetric unit, Ca2+ ion-binding site is maintained
-
mutant F40I, to 1.7 A resolution. Overall globular structures in the wild-type and mutant F40I enzymes do not differ
-
mutant W203F of truncated beta-glucanase catalytic domain, residues 1-243, to 1.4 A resolution. Residue W203 is stacked with the glucose product of cellotriose. Two extra calcium ions and a Tris molecule bind to the mutant structure. A Tris molecule, bound to the catalytic residues of E56 and E60, is found at the position normally taken by substrate binding at the -1 subsite. A second Ca2+ ion is found near the residues F152 and E154 on the protein's surface, and a third one near the active site residue D202
-
truncated form of enzyme containing the catalytic domain from amino acid 1-258, seleno-methionine labeled protein
-
purified wild-type PtLic16A and inactive mutant E113A in ligand-free form and in complex with the ligands cellobiose, cellotetraose and glucotriose, X-ray diffraction structure determination and analysis at 1.80-2.25 A resolution. Native PtLic16A crystals belong to the space group C2221 and contain four polypeptide chains in an asymmetric unit. The E113A mutant crystals belong to a different space group of C2 and have two protein molecules in an asymmetric unit. The third E113A crystal belongs to space group P21, with four molecules in an asymmetric unit
purified wild-type PtLic16A and inactive mutant E113A in ligand-free form and in complex with the ligands cellobiose, cellotetraose and glucotriose, X-ray diffraction structure determination and analysis at 1.80-2.25 A resolution. Native PtLic16A crystals belong to the space group C2221 and contain four polypeptide chains in an asymmetric unit. The E113A mutant crystals belong to a different space group of C2 and have two protein molecules in an asymmetric unit. The third E113A crystal belongs to space group P21, with four molecules in an asymmetric unit
-
1.5 A resolution, native enzyme, 1.6 A resolution, enzyme-inhibitor Glc-beta-1,3-isofagomine-complex, hanging drop vapor diffusion method for the enzyme, sitting drop vapor diffusion method for the complex
-
purified recombinant catalytic domain, sitting drop vapour diffusion method, mixing of 0.002 ml of 30 mg/ml protein in 25 mM Tris pH 7.5, 150 mM NaCl, and 0.002 ml reservori solution containing 0.04 M citric acid, 0.06 M Bis-Tris propane, pH 6.4, 18% w/v PEG 3350, 25C, 7 days, optimized method, X-ray diffraction structure determination and analysis at 1.95 A resolution, molecular replacement method
purified recombinant His-tagged wild-type and mutant enzymes, hanging drop vapour diffusion method, mixing of 0.002 ml of 10 mg/ml protein with 0.002 ml reservoir solution containing 24% PEG 3350 and 100 mM sodium citrate, pH 5.2, 4C, crystals of enzyme mutant E269S in complex with laminarin oligosaccharides are obtained from 0.002 ml of 13.3 mg/ml protein and 5 mM of purified hexasaccharides,with 0.001 ml of reservoir solution containing 100 mM sodium malonate, imidazole, and boric acid (MIB-buffer), pH 4.0, and 19% of PEG 1500 in hanging drops at 20C. Single crystals of mutant E269S in complex with MLG trisaccharides are obtained from mixing 0.002 ml 11.7 mg/ml of protein, 0.04% w/v of MLG degradation products with 0.001 ml of reservoir solution containing 100 mM MIB buffer, pH 4.0, 17% of PEG 1500, and 10% of glycerol in hanging drops at 12C, X-ray diffraction structure determination and analysis at 1.13-1.45 A resolution, molecular replacement method
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1 - 2
purified enzyme, 37C, 30 min, inactivation
730139
1 - 8
Bispora sp.
37C, 1 h, more than 85% of maximum activity
707242
2.5 - 9
-
4C or 20C, stable for 20 h
171529
3
-
retains approximately 80% of original activity after treatment at pH 3.0 for 12 h
677749
3 - 10
-
purified enzyme, 37C, 1 h, completely stable
729532
3 - 11
purified recombinant His-tagged enzyme, 50C, 30 min, completely stable
729409
3.4 - 9.8
Orpinomyces sp.
-
4C, stable for at least 24 h
171538
3.5 - 12
the enzyme is acid-, alkali- and salt-tolerant, the purified recombinant His-tagged enzyme retains more than 80% activity after incubation for 4 h
729476
3.5 - 7
-
hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase, stable
171537
3.6 - 10.6
-
-
681336
4
-
optimum condition for the beta-glucanase stability
681159
4 - 10
-
-
698410
4 - 10
purified enzyme, stable at
730139
4 - 10
-
purified isozymes EG1 and EG2, retaining over 90% activity after 48 h, after 72 h isozyme EG1 loses 30% and isozyme EG2 15% activity
730844
4 - 5
-
25C, 72-96 h, stable
171531
4 - 6
-
the recombinant enzyme is stable between pH 4.0 and 6.0, having 85% of the original activity
677749
4 - 7
-
increase in stability from pH 4 to pH 7
657085
4 - 8
Thermomonospora sp.
-
-
678492
4.1
-
65C, 1 h, 95% loss of activity; 65C, 1 h, hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase, 85%-95% of the initial activity is retained
171544
4.1
-
65C, 1 h, complete inactivation; 65C, 1 h, hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase, 85%-95% of the initial activity is retained
171544
4.8 - 6
-
stable
171537
4.8 - 6.4
-
stable
171537
5 - 6
-
60C, 10 min, stable
171533
5 - 7
-
10 min, stable
171536
5 - 7.5
purified native enzyme, retains 90% of its activity at 60C for 30 min
729865
5.6 - 6
-
hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens, stable
171537
6
-
no enzyme activity is detected at pH higher than 6
678923
6 - 9
-
with 50% of the activity remaining at pH 9
695667
6 - 9
-
stable within
715156
8
-
retains approximately 80% of original activity after treatment at pH 8.0 for 12 h
677749
11
purified enzyme, 37C, 30 min, loss of 50% activity
730139
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
-4
GLU-3 retains 14%-35% activity at -4C
682405
20 - 40
-
the remaining activity decreased to 20% at 20-40C and is completely destroyed at 50-70C
695667
20 - 50
-
30 min with about 50% of activity remaining at 50C
695667
22
-
11 days, complete inactivation of wild-type, 70% residual activity of mutant D70V
655016
25 - 35
-
decrease in stability from 25C to 35C
657085
25 - 40
purified recombinant enzyme, pH 6.0, 70 min, completely stable
729016
30 - 60
-
99.1, 87.8, 56.6, and 34.2% residual activity after 30 min preincubation at 30, 40, 50, and 60C, respectively
680529
30 - 60
-
104.5, 101.2, 67.9, and 21.2% residual activity after 30 min preincubation at 30, 40, 50, and 60C, respectively
680529
30 - 60
-
102, 91.2, 60.7, and 4.3% residual activity after 30 min preincubation at 30, 40, 50, and 60C, respectively
680529
30 - 60
-
98, 74.3, 2.4, and 0% residual activity after 30 min preincubation at 30, 40, 50, and 60C, respectively
680529
30 - 90
-
temperature effects on mutant W203F and on W203F mutant bifunctional hybrid enzymes, the latter is more resistant to heat treatment than the parental TFsW203F, overview
730863
40
-
pH 5.5, 10 min, stable
171531
40
Orpinomyces sp.
-
recombinant enzyme, pH 6.0, 24 h, stable
171538
40
-
10 min, stable
171539
40
-
purified native enzyme, 75% activity remaining after 120 min
730848
40 - 50
-
purified isozymes EG1 and EG2, retaining over 90% activity after 1 h
730844
44.5
-
15 min, 50% of activity, mutant G44R
657219
45
Orpinomyces sp.
-
recombinant enzyme, pH 6.0, 24 h, 28% loss of activity
171538
45
-
the wild-type maintains more than 85% of the original activity for 10 min
696479
45
purified enzyme, pH 10.0, 30 min, completely stable up to
730139
46
-
15 min, 50% of activity, mutant K23R
657219
46.1
-
15 min, 50% of activity, mutant A79P
657219
46.2
-
15 min, 50% of activity, mutant F85Y
657219
47.5
-
15 min, 50% of activity, wild type
657219
47.9
-
15 min, 50% of activity, mutant M298K, mutant T17D
657219
48.2
-
15 min, 50% of activity, mutant N290H
657219
50
Orpinomyces sp.
-
recombinant enzyme, pH 6.0, 24 h, 41% loss of activity
171538
50
-
10 min, about 25% loss of activity
171539
50
-
unstable above
654660
50
30 min, more than 90% of maximum activity
713885
50
purified recombinant His-tagged enzyme, pH 6.0, 30 min, completely stable
729409
50
purified recombinant His-tagged enzyme retaining more than 70% activity at up to 50C for 2 h
729476
50
-
purified enzyme, pH 5.0, half-life is 150 min
729532
50
-
purified native enzyme, 60% activity remaining after 120 min
730848
50 - 60
-
sharp decrease in activity up to 60C, but very stable below 50C
681336
50 - 70
-
after incubation at 50, 60, and 70C for 30 min, the residual activity is 95, 60, and 0%, respectively
677749
50 - 70
-
after 2 h incubation at 50C and 60C, the residual activity remaines 100% and 50%, respectively, while the enzymatic activity is abolished after 3 min incubation at 70C
678923
51.2
-
15 min, 50% of activity, mutant H300P
657219
52
-
10 min, 50% inactivation, wild-type
655016
55
Orpinomyces sp.
-
recombinant enzyme, pH 6.0, 24 h, 70% loss of activity
171538
55
purified recombinant His-tagged enzyme, half-life is about 50 min, 10% activity remaining after 2 h
729476
55
purified enzyme, pH 10.0, 30 min, loss of 50% activity
730139
57
-
Tm of wild-type enzyme
713931
59
-
Tm of mutant V18Y
713931
60
-
10 min, 50% loss of activity, crude enzyme extract
171528
60
-
15 min, pH 6.5, stable
171529
60
-
pH 5.5, 10 min, complete loss of activity
171531
60
-
pH 5.0-6.0, 10 min, stable. pH 6, in presence of 10 mM CaCl2 and serum albumin, stable for 120 min
171533
60
-
10 min, about 35% loss of activity
171536
60
-
10 min, complete inactivation
171539
60
-
4 min, 50% inactivation, wild-type, 11 min, 50% inactivation, mutant D70V
655016
60
Bispora sp.
stable for at least 1 h
707242
60
purified recombinant enzyme, retains more than 90% activity after 2 h
728997
60
purified recombinant His-tagged enzyme, inactivation within 10 min, in presence of 5 mM CaCl2 the enzyme retains over 80% activity after 2 h
729476
60
-
purified enzyme, pH 5.0, half-life is 135 min
729532
60
purified native enzyme, no loss in activity at pH 5.5 for 30 min, half-life is 225 min
729865
60
-
purified isozymes EG1 and EG2, half-lives are 55 min and 5 h, respectively
730844
60
-
purified native enzyme, half-life is 80 min
730848
60 - 70
-
purified recombinant enzyme, the wild-type enzymes activity decline rapidly above 60C, while the optimally-modified enzyme is more stable and shows activity up to 70C
729474
64
GLU-3 is irreversibly denatured above 64C
682405
65
-
half-life: 25 min; hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase is stable for more than 1 h at pH 5.5. The 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase. Hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens irreversible thermoinactivated within 20-25 min
171537
65
-
hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase is stable for more than 1 h at pH 5.5. The 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase. Hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens irreversible thermoinactivated within 20-25 min
171537
65
-
for 30 min
698410
65
-
purified native enzyme, half-life is over 68 days
709502
65
-
the linear enzyme form loses 50% activity within 3 min, whereas the two circular variants have 6fold (LicA-C1) and 16fold (LicA-C2) increased half-life time of inactivation
728986
65
purified recombinant His-tagged enzyme, pH 6.0, 30 min, loss of 50% activity
729409
65
purified recombinant His-tagged enzyme, in presence of 5 mM CaCl2 the enzyme retains 40% activity after 10 min, and 20% after 20 min, inactivation after 1 h
729476
65
-
purified enzyme, pH 5.0, half-life is 90 min
729532
66
-
10 min, 50% inactivation, mutant D70V
655016
70
-
1 h, 15% loss of activity
171543
70
-
pH 6.0, 1 h, hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase exhibit 90% of the initial activity, the parental enzymes retain 5% or less of the initial activity
171544
70
Bispora sp.
5 min, 48% residual activity, 60 min, 30% residual activity
707242
70
-
purified native enzyme, half-life is 125 h
709502
70
30 min, 65% of maximum activity
713885
70
purified recombinant enzyme, retains more 75% activity after 10 min
728997
70
-
purified recombinant enzyme, pH 7.0, 40% activity remaining after 6 h
729015
70
purified recombinant His-tagged enzyme, pH 6.0, 30 min, inactivation
729409
70
-
purified enzyme, pH 5.0, half-life is 30 min
729532
70
purified native enzyme, pH 5.5, half-life is 101 min
729865
70
-
purified isozymes EG1 and EG2, half-lives are 10 min and 52 min, respectively
730844
70
-
purified native enzyme, half-life is 21 min
730848
70 - 80
purified enzyme, pH 10.0, 30 min, loss of 80% activity
730139
75
-
1 h, 25% loss of activity
171543
75
-
purified recombinant wild-type enzyme, 10 min, 51% remaining activity in absence of Ca2+, 86% in presence of 1 mM Ca2+
707827
75
-
purified native enzyme, half-life is 22 h
709502
75
purified native enzyme, pH 5.5, half-life is 64 min
729865
80
Thermomonospora sp.
-
half-life of 5 min at 80C
678492
80
-
optimum condition for the beta-glucanase stability
681159
80
-
purified recombinant wild-type enzyme, 5 min, 54% remaining activity in absence of Ca2+, 73% in presence of 1 mM Ca2+
707827
80
-
purified native enzyme, half-life is 1 h
709502
80
purified recombinant enzyme, retains more 44% activity after 10 min
728997
80
-
purified recombinant enzyme, pH 7.0, no activity remaining after 1 h
729015
80
purified recombinant enzyme, retains 54% activity at 80C after incubation for 60 min
729343
80
purified native enzyme, pH 5.5, half-life is 53 min, 80% activity remaining after 30 min
729865
85
-
purified native enzyme, half-life is about 5 min
709502
85
purified native enzyme, pH 5.5, half-life is 27 min, inactivation after 120 min
729865
90
-
80% activity after 10 min
667689
90
-
the residual activity of mHG at 90C for 10 min is 83.45% of its maximum activity
679391
90
-
purified native enzyme, half-life is 80 s
709502
90
purified native enzyme, pH 5.5, 60% activity remaining after 30 min
729865
100
-
even when subjected to 100C for 3 h, beta-glucanase activity does not show significant reduction
681159
100
purified native enzyme, pH 5.5, 40% activity remaining after 30 min
729865
additional information
-
particularly thermostable in presence of Ca2+
171533
additional information
-
Ca2+ stabilizes hybrid enzymes and parental enzymes against thermal inactivation
171537
additional information
-
Ca2+ stabilizes the enzyme at higher temperatures, thermal stability of recombinant wild-type enzyme and mutants in presence and absence of Ca2+, overview
707827
additional information
-
thermal inactivation follow first-order kinetics, overview
709502
additional information
-
addition of 1 mM EDTA causes the linear enzyme to denature at 59.8C, which is lower compared to the melting temperature of 62.6C in the presence of calcium. At 1 mM EDTA, the circular enzyme variant LicA-C1 shows a melting temperature of 62.8C, at 1 mM CaCl2 the melting temperature is 66.4C
728986
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Ca2+ stabilizes hybrid enzymes and parental enzymes against thermal inactivation
-
particularly thermostable in presence of Ca2+
-
stable to repeated freeze-thaw cycles
-
enzyme is highly resistant to both pepsin and trypsin
Bispora sp.
Ca2+ stabilizes hybrid enzymes and parental enzymes against thermal inactivation
-
the purified recombinant His-tagged enzyme retains over 90% activity in 4 M NaCl at 25C for 24 h
Ca2+ stabilizes the enzyme at higher temperatures
-
in strong acid solution (HCl), beta-glucanase loses activity under conditions of pH 2.0, 1.0, and 0 indicating no tolerance to HCl
-
enzyme is rather unstable, stability increases from pH 4 to pH 7 and decreases from 25C to 35C, o-phenanthroline lowers stability of enzyme
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ethanol
-
stable up to concentrations up to 10% w/v
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, stable for 12 months
-
4C, 50 mM sodium phosphate, pH 7.8, 300 mM sodium chloride, stable for several weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-Sepharose CL-6B column chromatography
-
native extracellular enzyme 14.24fold from culture supernatant by ultrafiltration and gel filtration to homogeneity
-
native enzyme 37fold from strain YC-9 by ammonium sulfate precipitation, anion exchange chromatography, and gel filtration, recombinant enzyme from Escherichia coli strain BL21 (DE3) cell culture supernatant by ammonium sulfate precipitation, anion exchange chromatography, and gel filtration
parental enzymes and hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase
-
parental enzymes, hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase and hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
-
native extracellular isozymes EG1 and EG2 0.24fold and 11.6fold, respectively, from cell-free culture supernatant by dialysis and concentration with PEG 400, followed by anion exchange chromatography and gel filtration, both isozymes to homogeneity
-
Ni-NTA His Bind resin column chromatography
-
recombinant N-terminally His-tagged linear and circular enzymes from Escherichia coli strains BL21(DE3) or JM109(DE3) by nickel affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21 by nickel affinity chromatography to homogeneity
affinity chromatography of epoxy-activated sepharose 6B and ultrafiltration technique
-
Ni-NTA agarose column chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to homogeneity
recombinant mutant chimeric laccase/beta-1,3-1,4-glucanase enzyme from Escherichia coli by nickel affinity chromatography and ultrafiltration
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by dialysis, ultrafiltration, and nickel affinity chromatography
mutants purified on Ni-NTA affinity column, more than 95% purity
-
on Ni-NTA affinity column
-
Q-Sepharose FF column twice, Ni-NTA affinity column for the Escherichia coli protein, Q-Sepharose FF column for the Pichia pastoris protein
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, tag cleavage and again nickel affinity chromatography, recombinant extracellular wild-type and mutants V18Y, W203Y, and V18Y/W203Y enzymes from Pichia pastoris cell culture supernatant by dialysis and anion exchange chromatography
-
native enzyme by 16fold ammonium sulfate fractionation, combined cation and anion exchange chromatography, and another anion exchange chromatography
-
3.1fold to homogeneity by ammonium sulfate fractionation, dialysis and anion exchange chromatography, followed by hydrophobic interaction chromatography
recombinant enzyme from Escherichia coli; recombinant enzyme from Escherichia coli; recombinant enzyme from Escherichia coli; recombinant enzyme from Escherichia coli
recombinant enzyme
Orpinomyces sp.
-
recombinant GST-tagged EGL2 from Escherichia coli by glutathione affinity chromatography, the tag is cleaved off by thrombin, followed by benzamidine resin chromatography
recombinant GST-tagged EGL1 from Escherichia coli by glutathione affinity chromatography, the tag is cleaved off by thrombin, followed by benzamidine resin chromatography
by ammonium sulfate precipitation and two steps of ion-exchange chromatographies. Purified 122.5fold with an apparent homogeneity and a recovery yield of 8.9%
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)
-
parental enzymes and hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase
-
parental enzymes, hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase and hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens
-
wild type and mutant enzymes W101F, W101Y, E103D, E103Q, D105N, D105K, E107D, E107Q, and E107H
-
recombinant His-tagged enzyme 2.5fold from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
native extracellular enzyme 0.63fold from cell-free culture supernatant by heat treatment at 50C for 10 min, anion exchange chromatography, lyophilization, and gel filtration to homogeneity
-
native enzyme 6.8fold by ammonium sulfate fractionation and two different steps of anion exchange chromatography, to homogeneity
SP-Sepharose column chromatography and Sephacryl S-100 gel filtration
-
immobilized metal ion affinity chromatography, gel filtration, anion exchange chromatography
-
recombinant His-tagged isolated catalytic domain of the enzyme from Escherichia coli strain BL21trxB(DE3) by nickel affinity chromatography and dialysis, tag cleavage by factor Xa digestion, and removal of the tag by another step of nickel affinity chromatography
GSTrap FF column chromatography and HiTrap Benzamidine FF column chromatography
by gel filtration and ultrafiltration
-
DEAE Sephadex A50 column chromatography and Sephacryl S-200 gel filtration
Thermomonospora sp.
-
Sephadex G-100 gel filtration
-
recombinant enzyme from Escherichia coli strain C43(DE3), the signal peptide is cleaved
KM079629
the cloned protein from the recombinant strain BL21/pET21a-RuCelA is purified using Ni-NTA resin
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons, and phylogenetic analysis. Recombinant expression of the enzyme fused to the Trx-tag/His-tag/S-tag sequences in Escherichia coli strain BL21 (DE3), the enzyme is located in the cell lysate and the cell culture supernatant
expression in Escherichia coli
hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase and hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens, expression in Escherichia coli
-
hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase, expression in Escherichia coli
-
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
expressed in Escherichia coli strain BL21 (DE3)
-
expressed in Pichia pastoris strain GS115
-
expression of the N-terminally His-tagged enzyme with or without inteins, constructs for linear and circular enzymes, in Escherichia coli strains BL21(DE3) or JM109(DE3). The inteins are spliced out
-
gene bg1314, DNA and amino acid sequence determination and analysis, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21
hybrid from Bacillus macerans and Bacillus amyloliquefaciens
-
hybrid from Bacillus macerans and Bacillus amyloliquefaciens, H(A16-M)
-
expression as GST-fusion protein
-
gene bglS, expression of mutant chimeric laccase/beta-1,3-1,4-glucanase enzyme in Escherichia coli
gene SU40-glu, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene bgl5-1, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain JM109
expression in Pichia pastoris
Bispora sp.
expression in Escherichia coli
-
C-terminally truncated (10 kDa), overexpression in Escherichia coli BL21 (DE3) and Pichia pastoris X-33, mutants with increased catalytic efficiency and thermotolerance
-
expressed in Lactobacillus reuteri strain Pg4
-
expression in Escherichia coli
-
expression in Escherichia coli and Pichia pastoris; expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), heterologous expression of extracellular wild-type and mutant enzymes in Pichia pastoris
-
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
plasmid carrying the truncated 1,3-1,4-beta-D-glucanase gene in the pET26b(+) vector, transformed into Escherichia coli XL1-Blue. Overexpression of the truncated form and mutants in Escherichia coli BL21 (DE3) cells
-
wild-type and mutants cloned into vector pET26b(+) and expressed in Escherichia coli BL21 (DE3)
-
expression in Escherichia coli
-
expression in Escherichia coli, isolation and characterization of the gene
-
transgenic barley expressing a protein-engineered, thermostable (1,3-1,4)-beta-glucanase during germination
-
gene bglA13, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli; gene bglA16, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli; gene bglA51, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli; gene bglM2, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli
expression in Escherichia coli
Orpinomyces sp.
-
gene OsEGL2, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, functional expression of GST-tagged EGL2 in Escherichia coli
gene OsEGL1, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic analysis, functional expression od GST-tagged EGL1 in Escherichia coli
expression in Pichia pastoris
gene PtLic16A, DNA and amino acid sequence determination and analysis, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase and hybrid enzyme H2 which consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens, expression in Escherichia coli
-
hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase, expression in Escherichia coli
-
gene plicA, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenetic tree, subcloning in Escherichia coli strain DH5alpha, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
gene RmLic16A, DNA and amino acid sequence determination and analysis, sequence comparisons
expressed in Nicotiana benthamina as fusion protein
-
expression in Escherichia coli
expression of the His-tagged isolated catalytic domain of the enzyme, residues 31-251, in Escherichia coli strain BL21trxB(DE3) with an extra linker AGAGA at its N-terminus
expression of wild-type enzyme and mutant circular enzyme constructs in Escherichia coli strain XL1-Blue
-
gene LicB, expression of mature enzyme and isolated catalytic domain, as well as of the enzyme truncation mutants in Escherichia coli strain BL21
-
overexpression in Escherichia coli XL1-blue and BL21 with His-tag
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recombinant expression and secretion from Bacillus subtilis strain WB800 using vector pP43JM2
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recombinant expression in transgenic Nicotiana tabacum plants
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expressed in Escherichia coli
into pET3a vector and expressed in Escherichia coli strain BL21(DE3)pLysS
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expressed in Escherichia coli
-
expressed in Escherichia coli BL21/pET21a
gene mt-lic, genomic library screening, DNA and amino acid sequence determination and analysis, phylogenetic tree and sequence comparisons, recombinant expression in Escherichia coli strain C43(DE3)
KM079629
gene Zobellia_2431, DNA and amino acid sequence determination and analysis, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the expression of endo-(1,3;1,4)-beta-glucanase is upregulated in response to wounding, methyl jasmonate, abscisic acid and ethephon in rice seedlings
the expression of endo-(1,3;1,4)-beta-glucanase is upregulated in response to wounding, methyl jasmonate, abscisic acid and ethephon in rice seedlings. The increase in the leaf elongation rate of rice seedlings treated under mechanical wounding is concomitant with an increase in OsEGL1 expression levels in seedling leaves, overview
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E134A
-
inactive mutant, analysis of substrate binding
E134A
-
mutant devoid of hydrolase activity but efficiently catalyzing transglycosylation
E134A
-
catalyzes condensation reaction with alpha-fluorido-substrates
N207D
-
mutant displays better thermotolerance than the wild type but also reduced activity
A98W
-
active-site variant
E105Q/E109Q
-
catalytically impaired
E131Q
-
active-site variant
E63D
-
active-site variant
E63Q
-
active-site variant
N26A
-
active-site variant
R65A
-
active-site variant
S90A
-
active-site variant
W184Y
-
active-site variant
W192A
-
active-site variant
Y123A
-
active-site variant
Y123F
-
active-site variant
Y24A
-
active-site variant
Y24F
-
active-site variant
233Stop
-
28.4% of wild-type activity
D202L
-
shows a 1.2fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
D202N
-
exhibits a 1.8fold increase in catalytic efficiency (kcat/KM) compared to the wild-type
D206M
-
shows a 1.1fold increase in catalytic efficiency (kcat/KM) compared to the wild-type
D206N
-
exhibits a 1.5fold increase in catalytic efficiency (kcat/KM) compared to the wild-type
D206R
-
exhibits the highest relative activity at 50C over 10 min, shows a 1.2fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
D58A
-
no enzymatic activity
D58E
-
dramatic decrease in kcat, substrate affinity similar to wild type
D58N
-
dramatic decrease in kcat, substrate affinity similar to wild type
E11L
-
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 10fold decrease in specific activity, more than 2fold increase in KM-value, significant decrease in catalytic efficiency
E47I
-
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 2fold increase in KM-value
E56A
-
no enzymatic activity
E56D
-
dramatic decrease in kcat, substrate affinity similar to wild type
E56Q
-
no enzymatic activity
E60A
-
no enzymatic activity
E60D
-
dramatic decrease in kcat, substrate affinity similar to wild type
E60Q
-
no enzymatic activity
E85D
-
has 5fold lower kcat/Km ratios than the wild-type
E85I
-
has 5fold lower kcat/Km ratios than the wild-type
F205L
-
shows a 3.8fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
F40I
-
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 10fold decrease in specific activity, significant decrease in catalytic efficiency
G201S
-
shows a 1.5fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
G207N
-
shows a fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
G63A
-
decrease in thermostability
K200F
-
is the most heat-sensitive enzyme, retains 72% of activity at 45C for 10 min, shows a 1.2fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
K200M
-
shows a 1.1fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
K64A
-
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure
K64M
-
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 2fold increase in KM-value
L62G
-
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure
M27D/M39R
-
0.1% of wild-type activity; site-directed mutagenesis, almost inactive mutant
M27R/M39D
-
0.2% of wild-type activity; site-directed mutagenesis, almost inactive mutant
M39F
-
5-fold increase in km value
N139A
-
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 2fold increase in KM-value, significant decrease in catalytic efficiency
N208G
-
shows a fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
N44L
-
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure
N44Q
-
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 2fold increase in KM-value
N72A
-
has 11fold lower kcat/Km ratios than the wild-type
N72Q
-
has 17fold lower kcat/Km ratios than the wild-type
Q70A
-
has 299fold lower kcat/Km ratios than the wild-type
Q70D
-
has 62fold lower kcat/Km ratios than the wild-type
Q70E
-
has 106fold lower kcat/Km ratios than the wild-type
Q70I
-
has 499fold lower kcat/Km ratios than the wild-type
Q70N
-
has 63fold lower kcat/Km ratios than the wild-type
Q70R
-
has 35fold lower kcat/Km ratios than the wild-type
Q81I
-
has 2fold lower kcat/Km ratios than the wild-type
Q81N
-
has 2.5fold lower kcat/Km ratios than the wild-type
R137M
-
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 10fold decrease in specific activity, more than 2fold increase in KM-value, significant decrease in catalytic efficiency
R137Q
-
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 10fold decrease in specific activity, more than 2fold increase in KM-value, significant decrease in catalytic efficiency
R209M
-
shows a 1.1fold increase, in catalytic efficiency (kcat/KM) compared to the wild-type
S71F
-
loss of activity; site-directed mutagenesis, inactive mutant
S84D
-
80.9% of wild-type activity; site-directed mutagenesis, 19% reduced activity compared to wild-type
T204F
-
shows a 2.2fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
V18Y
-
104% of wild-type activity. Increase in thermostability by 2 degrees; site-directed mutagenesis, 4% reduced activity compared to wild-type
V18Y/W203Y
-
134.3% of wild-type activity; site-directed mutagenesis, 34% increased activity compared to wild-type
V61F
-
20.9% of wild-type activity; site-directed mutagenesis, 79% reduced activity compared to wild-type
W105F
-
significant decrease in thermostability
W105H
-
significant decrease in thermostability
W141F
-
5-7-fold increase in KM-value for lichenan compared to wild type, decrease in kcat-value, no significant change in thermal stability
W141H
-
5-7-fold increase in KM-value for lichenan compared to wild type, decrease in kcat-value, no significant change in thermal stability
W148F
-
decrease in kcat-value, no significant change in thermal stability
W165F
-
after incubation at pH 3.0, 1 h, 3-7-fold higher activity than wild type
W165H
-
significant decrease in thermostability
W186F
-
increase in kcat-value, no significant change in thermal stability
W198F
-
significant decrease in thermostability
W203F
-
increase in kcat-value, no significant change in thermal stability
W203F
-
exhibits a 2.4fold increase in catalytic efficiency (kcat/KM) compared to the wild-type
W203F
-
87.6% of wild-type activity; site-directed mutagenesis, 13% reduced activity compared to wild-type
W203F
-
mutant of truncated beta-glucanase catalytic domain, residues 1-243. mutant has increased hydrolytic activity. Residue W203 is stacked with the glucose product of cellotriose. Two extra calcium ions and a Tris molecule bind to the mutant structure. A Tris molecule, bound to the catalytic residues of E56 and E60, is found at the position normally taken by substrate binding at the -1 subsite. A second Ca2+ ion is found near the residues F152 and E154 on the protein's surface, and a third one near the active site residue D202
W203F
-
site-directed mutagenesis, truncated and mutated 1,31,4-beta-D-glucanase, no activity with laminarin
W203R
-
5-7-fold increase in KM-value for lichenan compared to wild type, decrease in kcat-value, after incubation at pH 3.0, 1 h, 3-7-fold higher activity than wild type, no significant change in thermal stability
W203R
-
exhibits a 207fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
W203Y
-
130.2% of wild-type activity; site-directed mutagenesis, 30% increased activity compared to wild-type
W54F
-
decrease in kcat-value, no significant change in thermal stability
W54Y
-
decrease in kcat-value, no significant change in thermal stability
Y42L
-
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 10fold decrease in specific activity
A79P
-
decrease in thermal stability
F85Y
-
decrease in thermal stability
G44R
-
decrease in thermal stability
H300P
-
increase in thermal stability
K23R
-
decrease in thermal stability
N290H
-
slight increase in thermal stability
D70V
-
thermostable mutant, similar katalytic efficiency as wild type
E113A
inactive mutant. In the structure of E113A/1,3-1,4-beta-glucotriose complex, the sugar bound to the -1 subsite adopts an intermediate-like (alpha-anomeric) configuration
W108A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W108F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W108Y
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W253A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W253F
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W253Y
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
C263S
-
random mutagenesis, the mutant shows an acidic shift in the pH optimum and altered substrate specificity compared to the wild-type enzyme
D221G2
-
random mutagenesis, the mutant shows unaltered properties compared to the wild-type enzyme
D56G
-
random mutagenesis, the mutant shows an acidic shift in the pH optimum and altered substrate specificity compared to the wild-type enzyme
D56G/D221G/C263S
-
random mutagenesis, mutant PtLic16AM2 shows an acidic shift in the pH optimum and altered substrate specificity compared to the wild-type enzyme. Mutation D221G alone does not lead to altered enzyme properties
W108A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W108F
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W108Y
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W253A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W253F
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
W253Y
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D105K
-
activity is reduced to less than 1%
D105N
-
activity is reduced to less than 1%
E103D
-
activity is reduced to less than 1%
E103Q
-
activity is reduced to less than 1%
E107D
-
activity is reduced to less than 1%
E107H
-
activity is reduced to less than 1%
W101F
-
activity is reduced to less than 1%
W101Y
-
activity is reduced to less than 1%
D100A
-
36% relative activity compared to the wild type enzyme
D106A
-
34% relative activity compared to the wild type enzyme
D195A
-
36% relative activity compared to the wild type enzyme
D220A
-
32% relative activity compared to the wild type enzyme
D258A
-
35% relative activity compared to the wild type enzyme
D314A
-
99% relative activity compared to the wild type enzyme
D317A
-
31% relative activity compared to the wild type enzyme
E196A
-
39% relative activity compared to the wild type enzyme
E222A
-
no activity
E242A
-
32% relative activity compared to the wild type enzyme
E262A
-
36% relative activity compared to the wild type enzyme
E323A
-
32% relative activity compared to the wild type enzyme
E91A
-
no activity
D195A
Paenibacillus polymyxa GS01
-
36% relative activity compared to the wild type enzyme
-
D258A
Paenibacillus polymyxa GS01
-
35% relative activity compared to the wild type enzyme
-
D314A
Paenibacillus polymyxa GS01
-
99% relative activity compared to the wild type enzyme
-
E222A
Paenibacillus polymyxa GS01
-
no activity
-
E269S
site-directed mutagenesis, nucleophile replacement, inactive mutant
E269S
Zobellia galactanivorans DSM 12802
-
site-directed mutagenesis, nucleophile replacement, inactive mutant
-
additional information
-
construction of hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase. Hybrid enzyme H2 consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens. Hybrid enzyme H1 exhibits increased thermostability especially in an acidic environment compared to both parental enzymes. Hybrid enzyme H2 is more thermolabile than the naturally occuring beta-glucanases
additional information
-
hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase, expression in Escherichia coli
additional information
construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30%
additional information
-
modifying five (out of 12) epsilon-amino groups in lysine residues with nitrous acid improves thermostablility and enzymatic activity of the enzyme, optimizing the condition of chemical modification, overview. Compared to the wild-type enzyme, the optimally-modified enzyme has higher specific activity and T50 value, which are 3370 U/mg and 70C, respectively. Its half-life values at 50 and 60C are extended and reach 58.5 and 49.5 min, respectively
E134A/E138A
-
no enzymic activity, but reaction occurs in presence of sodium azide, E138 is the general acid-base catalyst
additional information
-
covalent linkage between the N- and C-termini of a polypeptide chain to create circular variants of the enzyme by an intein-driven protein splicing approach, method, overview. Two circular variants, LicAC1 and LicA-C2, which have connecting loops of 20 and 14 amino acids, respectively, show catalytic activities that are approximately two and three times higher, respectively, compared to that of the linear LicA, LicA-L1. Also the thermal stability of the circular variants is significantly increased compared to the linear form. The circular proteins contain a thrombin recognition site and can be linearized by cleavage with thrombin
H99D
-
active-site variant
additional information
-
subsite +1 mutants, kinetic analysis
Y24W
-
active-site variant
additional information
-
the truncated gene product, devoid of cellulose-binding domain, shows 60% of activity and binds to avicel
additional information
construction of a chimeric bifunctional laccase/beta-1,3-1,4-glucanase mutant enzyme by insertion fusion of the bglS and cotA genes, protein CotA, UniProt ID P07788, the approximation of the two catalytic domains in the chimeric enzyme, and the formation of an inter-domain interface increase catalytic activities,molecular dynamics simulations, overview. The laccase efficiency with substrate 2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonic acid) is higher in the chimera, while the glucanase activity with lichenan shows a Kcat/KM value increased by 26%, a lower Km anf kcat. The beta-1,3-1,4-glucanase hydrolyzes plant cell wall beta-glucans, and the copper-dependent oxidase laccase catalyzes the oxidation of aromatic compounds with simultaneous reduction of oxygen to water. The mutant chimeric enzyme shows synergistic sugar release from milled sugarcane bagasse
additional information
Bacillus subtilis 168
-
construction of a chimeric bifunctional laccase/beta-1,3-1,4-glucanase mutant enzyme by insertion fusion of the bglS and cotA genes, protein CotA, UniProt ID P07788, the approximation of the two catalytic domains in the chimeric enzyme, and the formation of an inter-domain interface increase catalytic activities,molecular dynamics simulations, overview. The laccase efficiency with substrate 2,2'-azinobis (3-ethylbenzthiazoline-6-sulfonic acid) is higher in the chimera, while the glucanase activity with lichenan shows a Kcat/KM value increased by 26%, a lower Km anf kcat. The beta-1,3-1,4-glucanase hydrolyzes plant cell wall beta-glucans, and the copper-dependent oxidase laccase catalyzes the oxidation of aromatic compounds with simultaneous reduction of oxygen to water. The mutant chimeric enzyme shows synergistic sugar release from milled sugarcane bagasse
-
additional information
Bacillus subtilis A8-8
-
the truncated gene product, devoid of cellulose-binding domain, shows 60% of activity and binds to avicel
-
M39F
-
92.8% of wild-type activity; site-directed mutagenesis, 7% reduced activity compared to wild-type
additional information
-
truncated form of enzyme containing the catalytic domain from amino acid 1-258, higher thermal stability and enzymatic activity than wild type protein, crystal structure
additional information
-
construction of mutants based on catalytic domain, residues 1-243, with higher thermostability and specific activity; kinetic and thermostability analysis of the mutant enzymes, overview
additional information
-
engineering of dual-functional hybrid glucanases from a truncated and mutated 1,3-1,4-beta-D-glucanase gene TFsW203F from Fibrobacter succinogenes, and a 1,3-beta-D-glucanase gene TmLam from hyperthermophilic Thermotoga maritima used as target enzymes, by ligating substrate-binding domains (TmB1 and TmB2) and the catalytic domain (TmLamCD) of TmLam to the N- or C-terminus of TFsW203F to create four hybrid enzymes, TmB1-TFsW203F, TFsW203F-TmB2, TmB1-TFsW203F-TmB2 and TFsW203F-TmLamCD, creation of desirable hybrid enzymes with economic benefits for industrial applications. Improved thermal tolerance of the hybrid enzyme TFsW203FTmLamCD, fluorescence and circular dichroism spectrometric analyses, overview. Kinetic properties of parental TFsW203F and mutant hybrid glucanases
M298K
-
thermal stabiltiy similar to wild type
additional information
-
protein-engineered, thermostable (1,3-1,4)-beta-glucanase: the codons for hybrid H(A12-M)DELTAY13 are modified to match those of the gene encoding barley (1,3-1,4)-beta-glucanase isoenzyme EII
E113A
-
inactive mutant. In the structure of E113A/1,3-1,4-beta-glucotriose complex, the sugar bound to the -1 subsite adopts an intermediate-like (alpha-anomeric) configuration
additional information
-
screening of the random mutant library, mutations D56G, D221G, and C263S have only minor effects on specific activity and pH stability
E107Q
-
activity is reduced to less than 1%
additional information
-
construction of hybrid beta-glucanase enzyme H1 which contains the 107 amino-terminal residues of mature Bacillus amyloliquefaciens beta-glucanase and the 107 carboxyl-terminal amino acid residues of Bacillus beta-glucanase. Hybrid enzyme H2 consists of the 105 amino-terminal residues from the Bacillus macerans enzyme and the carboxyl-terminal 107 amino acids from Bacillus amyloliquefaciens. Hybrid enzyme H1 exhibits increased thermostability especially in an acidic environment compared to both parental enzymes. Hybrid enzyme H2 is more thermolabile than the naturally occuring beta-glucanases
additional information
-
hybrid enzymes containing 16, 36, 78, or 152 amino acid N-terminal sequence derived from Bacillus amyloliquefaciens 1,3-1,4-beta-D-glucan glucanohydrolase followed by a C-terminal segment derived from Bacillus macerans 1,3-1,4-beta-D-glucan glucanohydrolase, expression in Escherichia coli
E323A
Paenibacillus polymyxa GS01
-
32% relative activity compared to the wild type enzyme
-
additional information
-
UV irradiation leads to mutants TC2 and TC5 with increased activity against barley beta-glucan during growth on solka floc
additional information
-
construction of diverse enzyme truncation mutants for domain functional analysis, overview
additional information
-
generation of transgenic Nicotiana tabacum plants expressing LicB from Clostridium thermocellum, no altered phenotype, overview. Expression of bacterial beta-1,3-1,4-glucanase gene exerts no significant influence on tobacco plant metabolism, while the expression of bacterial beta-1,3-glucanase affects plant metabolism only at early stages of growth and development. By contrast, the expression of bacterial beta-1,4-glucanase has a significant effect on transgenic tobacco plant metabolism
additional information
construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30%
additional information
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construction of hybrid genes encoding circularly permutated lichenase variants with integrated small peptides, i.e. NC-L-53, NC-L-99, NC-L-53-99, and NC-L-140, method overview. Generation of a thermostable lichenase gene variant encoding only the enzyme's catalytic domain LicBM3. Thermostabilities of the mutant constructs, overview
additional information
Ruminiclostridium thermocellum ZJL4
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construction of diverse enzyme truncation mutants for domain functional analysis, overview
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
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the enzyme is considered as a candidate for application particularly in the animal feed industry
food industry
Aspergillus niger US368
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the enzyme is considered as a candidate for application particularly in the animal feed industry
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synthesis
construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30%
analysis
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the enzyme is used for oligosaccharide profiling of mixed-linkage glucan, beta-1,3-1,4-glucan, a characteristic hemicellulose in primary cell walls of grasses, that adsorps onto microcrystalline cellulose in a slow, irreversible, and temperature-dependent manner. The binding of the oligomer is reduced if the cellulose samples are first treated with certain cell wall polysaccharides, such as xyloglucan and glucuronoarabinoxylan
food industry
the thermostable enzyme can be useful in mashing at 72C of brewing processes
food industry
Bacillus tequilensis CGX5-1
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the thermostable enzyme can be useful in mashing at 72C of brewing processes
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synthesis
Bispora sp.
over-expression in Pichia pastoris, with a yield of about 1000 U/ml in a 3.7 l fermentor
industry
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properties make the enzyme highly suitable for industrial applications
synthesis
upon expression in Pichia pastoirs as active extracellular beta-1,3-1,4-glucanase, the recombinant protein is secreted predominantly into the medium and comprises up to 85% of the total extracellular proteins and reaches a protein concentration of 9.1 g/l with an activity of 55,300 U/ml in 5-l fermentor culture
food industry
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the enzyme is a good candidate in the malting and brewing industry reducing the filtration time and viscosity of mash from barley grains, overview
food industry
Penicillium occitanis Pol6
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the enzyme is a good candidate in the malting and brewing industry reducing the filtration time and viscosity of mash from barley grains, overview
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nutrition
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the enzyme is able to reduce both the viscosity of the brewer mash and the filtration time, indicating its potential value for the brewing industry
food industry
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the secretively produced beta-1,3-1,4-glucanase shows excellent thermostability up to 80C and a wide pH range from pH 4 to pH 11 and has a potential in the food and animal feed applications
synthesis
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the unusually resistance against inactivation by heat, ethanol or ionic detergents makes the enzyme highly suitable for industrial application in the mashing process of beer brewing
synthesis
construction of a fusion gene, encoding beta-1,3-1,4-glucanase both from Bacillus amyloliquefaciens and Clostridium thermocellum, via end-to-end fusion and expression in Escherichia coli. The catalytic efficiency of the fusion enzyme for oat beta-glucan is 2.7- and 20fold higher than that of the parental Bacillus amyloliquefaciens and Clostridium thermocellum enzymes, respectively, and the fusion enzyme can retain more than 50% of activity following incubation at 80C for 30 min, whereas the residual activities of Bacillus amyloliquefaciens and Clostridium thermocellum enzymes are both less than 30%
food industry
Ruminiclostridium thermocellum DSM 1237
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the secretively produced beta-1,3-1,4-glucanase shows excellent thermostability up to 80C and a wide pH range from pH 4 to pH 11 and has a potential in the food and animal feed applications
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biofuel production
RuCelA can produce xylo-oligosaccharides and cell-oligosaccharides in the continuous saccharification of pretreated rice straw, which can be further degraded into fermentable sugars. Therefor, the bifunctional RuCelA distinguishes itself as an ideal candidate for industrial application
agriculture
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1,3-1,4-beta-D-glucanase are widely used as a feed additive to help non-ruminant animals digest plant fibers, with potential in increasing nutrition turnover rate and reducing sanitary problems
additional information
the alkaline beta-1,3-1,4-glucanase may have potential in industrial applications, such as detergent, paper and pulp industries
additional information
Malbranchea cinnamomea S168
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the alkaline beta-1,3-1,4-glucanase may have potential in industrial applications, such as detergent, paper and pulp industries
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