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Information on EC 3.2.1.73 - licheninase and Organism(s) Fibrobacter succinogenes and UniProt Accession P17989

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EC Tree
     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.73 licheninase
IUBMB Comments
Acts on lichenin and cereal beta-D-glucans, but not on beta-D-glucans containing only 1,3- or 1,4-bonds.
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This record set is specific for:
Fibrobacter succinogenes
UNIPROT: P17989
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The taxonomic range for the selected organisms is: Fibrobacter succinogenes
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
endoglucanase, plica, glu-1, glu-3, endo-beta-glucanase, 1,3-1,4-beta-glucanase, 1,3-1,4-beta-d-glucanase, bglc8h, af-egl7, xyniii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,3-1,4-beta-D-glucan 4-glucanohydrolase
-
1,3-1,4-beta-D-glucanase
-
beta-1,3-1,4-glucanase
-
(1->3,1->4)-beta-glucanase isoenzyme EII
-
-
-
-
1,3-1,4-beta-D-glucan 4-glucanohydrolase
-
-
-
-
1,3-1,4-beta-D-glucan glucanohydrolase
-
-
-
-
1,3-1,4-beta-D-glucanase
-
-
1,3;1,4-beta-glucan 4-glucanohydrolase
-
-
-
-
1,3;1,4-beta-glucan endohydrolase
-
-
-
-
beta-(1--> 3), (1--> 4)-D-glucan 4-glucanohydrolase
-
-
-
-
beta-glucanase
-
-
endo-beta-1,3-1,4 glucanase
-
-
-
-
Fsbeta-glucanase
-
-
GHF16 TFsbeta-glucanase
-
-
GHF17 barley 1,3-1,4-beta-D-glucanase
-
-
laminarinase
-
-
-
-
Lichenase
Mixed linkage beta-glucanase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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.
CAS REGISTRY NUMBER
COMMENTARY hide
37288-51-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,3-1,4-beta-D-glucan + H2O
?
show the reaction diagram
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
?
lichenan + H2O
?
show the reaction diagram
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
-
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
lichenan + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
noncompetitive
imidazole
competitive
additional information
-
resistent to trypsin protease digestion
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.98 - 10.3
lichenan
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.25 - 3.67
1,3-1,4-beta-D-glucan
-
5.8 - 5476
lichenan
10100
lichenan
-
pH 6.0-7.0, 45°C, mutant TFsW203F
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20.7 - 23.9
Ca2+
98.7 - 117
imidazole
100.7 - 255.4
Tris
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1.01
recombinant enzyme at 37°C
11.6
mutant E11L, 45°C, pH 5.0
15 - 25
mutant N139A, 45°C, pH not specified in the publication
1986
mutant E47I, 45°C, pH not specified in the publication
262
mutant F40I, 45°C, pH not specified in the publication
308
mutant R137Q, 40°C, pH not specified in the publication
3581
mutant K64A, 50°C, pH not specified in the publication
3671
mutant K64M, 50°C, pH not specified in the publication
43 - 46
mutant N44L, 55°C, pH not specified in the publication
5694
wild-type, expressed in Escherichia coli, pH 5.0, 50°C
60 - 61
mutant N44Q, 55°C, pH not specified in the publication
644
mutant Y42L, 45°C, pH not specified in the publication
6520
mutant V18Y, expressed in Escherichia coli, pH 5.0, 50°C
699
mutant R137M, 40°C, pH not specified in the publication
7833
wild-type, 50°C, pH 5.0
803
mutant L62G, 45°C, pH not specified in the publication
8478
truncated enzyme
9263
mutant W203Y, expressed in Escherichia coli, pH 5.0, 50°C
9967
mutant V18Y/W203Y, expressed in Escherichia coli, pH 5.0, 50°C
1.57
-
pH 6.0, 40°C, mutant D58E
10800
-
expressed in Pichia pastoris X-33, sodium citrate buffer, pH 6.0, 50°C, 10 min
1388
-
pH 6.0, 40°C, wild type
15 - 19
-
pH 6.0, mutant W105H
1572
-
pH 6.0, mutant W165H
1621
-
pH 6.0, mutant W105F
1755
-
pH 6.0, mutant W198F
1791
-
pH 6.0, mutant W165F
2.43
-
pH 6.0, 40°C, mutant D58N
2.57
-
pH 6.0, 40°C, mutant E60D
29
-
pH 6.0, mutant W54F
2941
-
pH 6.0, mutant W186F
37
-
pH 6.0, mutant W54Y
419
-
pH 6.0, mutant W141F
480
-
pH 6.0, mutant W148F
5.75
-
pH 6.0, 40°C, mutant E56D
502
-
pH 6.0, 40°C, mutant G63A
545
-
pH 6.0, 40°C, mutant M39F
626
-
substrate lichenan, pH 6.0-7.0, 45°C, mutant TFsW203F
69
-
pH 6.0, mutant W141H
70
-
pH 6.0, mutant W203R
7980
-
expressed in Escherichia coli, sodium citrate buffer, pH 6.0, 50°C, 10 min
8726
-
pH 6.0, mutant W203F
916
-
pH 6.0, mutant W112F
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7
6 - 8
-
wild type
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 10
activity range
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
mutants R137M and R137Q
45
mutants E11L, F40I, Y42L, E47I, L62G, and N139A
55
mutants N44L and N44Q
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 60
-
30°C, about 30% of maximal activity with oat beta-D-glucan, about 45% of maximal activity with lichenin, 60°C: about 20% of maximal activity with lichenin and oat beta-D-glucan as substrate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35200
-
1 * 35200, SDS-PAGE
37200
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 35200, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
expressed in Pichia pastoris
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo-form and substrate complex structures of mutant V18Y/W203Y, to 1.53 A resolution
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
purified recombinant mutant V18Y/W203Y alone and in complex with product cellotetraose , from 0.1 M Tris–HCl, 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
truncated form of enzyme containing the catalytic domain from amino acid 1-258, seleno-methionine labeled protein
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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 50°C over 10 min, shows a 1.2fold decrease in catalytic efficiency (kcat/KM) compared to the 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
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
K200F
is the most heat-sensitive enzyme, retains 72% of activity at 45°C 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
M27R/M39D
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
T204F
shows a 2.2fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
V18Y/W203Y
W203F
W203R
exhibits a 207fold decrease in catalytic efficiency (kcat/KM) compared to the wild-type
W203Y
Y42L
mutant of truncated beta-glucanase catalytic domain, residues 1-243. No discernible changes in secondary structure, more than 10fold decrease in specific activity
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
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
G63A
-
decrease in thermostability
M39F
-
5-fold increase in km value
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
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
W54F
-
decrease in kcat-value, no significant change in thermal stability
W54Y
-
decrease in kcat-value, no significant change in thermal stability
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
the wild-type maintains more than 85% of the original activity for 10 min
57
Tm of wild-type enzyme
59
Tm of mutant V18Y
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
50
-
unstable above
60
-
10 min, 50% loss of activity, crude enzyme extract
90
-
80% activity after 10 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutants purified on Ni-NTA affinity column, more than 95% purity
on Ni-NTA affinity column
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
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
gene FSU_0226, recombinant expression in Escherichia coli and in Pichia pastoris
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)
C-terminally truncated (10 kDa), overexpression in Escherichia coli BL21 (DE3) and Pichia pastoris X-33, mutants with increased catalytic efficiency and thermotolerance
-
expression in Escherichia coli
-
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
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
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Irvin, J.E.; Teather, R.M.
Cloning and expression of a Bacteroides succinogenes mixed-linkage beta-glucanase (1,3-1,4-beta-D-glucan 4-glucanohydrolase) gene in Escherichia coli
Appl. Environ. Microbiol.
54
2672-2676
1988
Fibrobacter succinogenes
Manually annotated by BRENDA team
Erfle, J.D.; Teather, R.M.; Wood, P.J.; Irvin, J.E.
Purification and properties of a 1,3-1,4-beta-D-glucanase (lichenase, 1,3-1,4-beta-D-glucan 4-glucanohydrolase, EC 3.2.1.73) from Bacteroides succinogenes cloned in Escherichia coli
Biochem. J.
255
833-841
1988
Fibrobacter succinogenes
Manually annotated by BRENDA team
Cheng, H.L.; Tsai, L.C.; Lin, S.S.; Yuan, H.S.; Yang, N.S.; Lee, S.H.; Shyur, L.F.
Mutagenesis of Trp(54) and Trp(203) residues on Fibrobacter succinogenes 1,3-1,4-beta-D-glucanase significantly affects catalytic activities of the enzyme
Biochemistry
41
8759-8766
2002
Fibrobacter succinogenes
Manually annotated by BRENDA team
Chen, J.L.; Tsai, L.C.; Wen, T.N.; Tang, J.B.; Yuan, H.S.; Shyur, L.F.
Directed mutagenesis of specific active site residues on Fibrobacter succinogenes 1,3-1,4-beta-D-glucanase significantly affects catalysis and enzyme structural stability
J. Biol. Chem.
276
17895-17901
2001
Fibrobacter succinogenes
Manually annotated by BRENDA team
Tsai, L.C.; Shyur, L.F.; Lee, S.H.; Lin, S.S.; Yuan, H.S.
Crystal structure of a natural circularly permuted jellyroll protein: 1,3-1,4-beta-D-glucanase from Fibrobacter succinogenes
J. Mol. Biol.
330
607-620
2003
Fibrobacter succinogenes
Manually annotated by BRENDA team
Wen, T.N.; Chen, J.L.; Lee, S.H.; Yang, N.S.; Shyur, L.F.
A truncated Fibrobacter succinogenes 1,3-1,4-beta-D-glucanase with improved enzymatic activity and thermotolerance
Biochemistry
44
9197-9205
2005
Fibrobacter succinogenes
Manually annotated by BRENDA team
Liu, J.R.; Yu, B.; Zhao, X.; Cheng, K.J.
Coexpression of rumen microbial beta-glucanase and xylanase genes in Lactobacillus reuteri
Appl. Microbiol. Biotechnol.
77
117-124
2007
Fibrobacter succinogenes (P17989)
Manually annotated by BRENDA team
Tsai, L.C.; Huang, H.C.; Hsiao, C.H.; Chiang, Y.N.; Shyur, L.F.; Lin, Y.S.; Lee, S.H.
Mutational and structural studies of the active-site residues in truncated Fibrobacter succinogenes1,3-1,4-beta-D-glucanase
Acta Crystallogr. Sect. D
64
1259-1266
2008
Fibrobacter succinogenes (P17989), Fibrobacter succinogenes
Manually annotated by BRENDA team
Lin, Y.S.; Tsai, L.C.; Lee, S.H.; Yuan, H.S.; Shyur, L.F.
Structural and catalytic roles of residues located in beta13 strand and the following beta - turn loop in Fibrobacter succinogenes 1,3-1,4-beta-D-glucanase
Biochim. Biophys. Acta
1790
231-239
2009
Fibrobacter succinogenes (P17989), Fibrobacter succinogenes
Manually annotated by BRENDA team
Tsai, L.C.; Chen, Y.N.; Shyur, L.F.
Structural modeling of glucanase-substrate complexes suggests a conserved tyrosine is involved in carbohydrate recognition in plant 1,3-1,4-beta-D-glucanases
J. Comput. Aided Mol. Des.
22
915-923
2008
Fibrobacter succinogenes
Manually annotated by BRENDA team
Huang, J.W.; Cheng, Y.S.; Ko, T.P.; Lin, C.Y.; Lai, H.L.; Chen, C.C.; Ma, Y.; Zheng, Y.; Huang, C.H.; Zou, P.; Liu, J.R.; Guo, R.T.
Rational design to improve thermostability and specific activity of the truncated Fibrobacter succinogenes 1,3-1,4-beta-D-glucanase
Appl. Microbiol. Biotechnol.
94
111-121
2012
Fibrobacter succinogenes (P17989)
Manually annotated by BRENDA team
Tsai, L.C.; Hsiao, C.H.; Liu, W.Y.; Yin, L.M.; Shyur, L.F.
Structural basis for the inhibition of 1,3-1,4-beta-D-glucanase by noncompetitive calcium ion and competitive Tris inhibitors
Biochem. Biophys. Res. Commun.
407
593-598
2011
Fibrobacter succinogenes (P17989)
Manually annotated by BRENDA team
Chen, J.; Tsai, L.; Huang, H.; Shyur, L.
Structural and catalytic roles of amino acid residues located at substrate-binding pocket in Fibrobacter succinogenes 1,3-1,4-beta-D-glucanase
Proteins Struct. Funct. Bioinform.
78
2820-2830
2010
Fibrobacter succinogenes (P17989), Fibrobacter succinogenes
Manually annotated by BRENDA team
Liu, W.; Lin, Y.; Jeng, W.; Chen, J.; Wang, A.; Shyur, L.
Engineering of dual-functional hybrid glucanases
Protein Eng. Des. Sel.
25
771-780
2012
Fibrobacter succinogenes
Manually annotated by BRENDA team
Goldenkova-Pavlova, I.V.; Tyurin, A.A.; Mustafaev, O.N.
The features that distinguish lichenases from other polysaccharide-hydrolyzing enzymes and the relevance of lichenases for biotechnological applications
Appl. Microbiol. Biotechnol.
102
3951-3965
2018
Bacillus amyloliquefaciens, Bacillus amyloliquefaciens (P07980), Bacillus altitudinis, Paenibacillus barcinonensis (A0A097QQT4), Bacillus pumilus (A0A0F6QU36), Paenibacillus barengoltzii (A0A0K1P4J7), Bacillus velezensis (A0A0M4NIK2), Acetivibrio thermocellus (A3DBX3), Acetivibrio thermocellus (Q84C00), Bacillus subtilis (A8CGP1), Bacillus subtilis (G0YW23), Bacillus subtilis (P04957), Bacillus subtilis (Q45691), Paenibacillus polymyxa (A9Z0X6), Ruminococcus albus (E9SCT3), Bacillus sp. SJ-10 (I1W007), Bacillus tequilensis (K0A689), Fibrobacter succinogenes (P17989), Niallia circulans (P19254), Bacillus licheniformis (P27051), Brevibacillus brevis (P37073), Rhodothermus marinus (P45798), Bacillus sp. N137 (Q45648), Bacillus sp. A3 (Q6YAT3), Paenibacillus macerans (Q846Q0), Bacillus subtilis MA139 (A8CGP1), Bacillus tequilensis CGX5-1 (K0A689), Acetivibrio thermocellus DSM 1237 (A3DBX3), Bacillus subtilis 168 (P04957), Ruminococcus albus 8 (E9SCT3), Acetivibrio thermocellus NBRC 103400 (A3DBX3), Brevibacillus brevis ALK36 (P37073), Bacillus velezensis S2 (A0A0M4NIK2), Bacillus altitudinis YC-9, Bacillus subtilis NCIB 8565 (Q45691), Paenibacillus polymyxa CP7 (A9Z0X6), Niallia circulans ATCC 21367 (P19254), Rhodothermus marinus ITI378 (P45798), Bacillus amyloliquefaciens ATCC 23350, Bacillus amyloliquefaciens ATCC 15841 (P07980), Acetivibrio thermocellus ATCC 27405 (A3DBX3), Fibrobacter succinogenes S85 (P17989), Acetivibrio thermocellus VPI 7372 (A3DBX3), Bacillus pumilus US570 (A0A0F6QU36), Bacillus subtilis SU40 (G0YW23), Paenibacillus barcinonensis BP-23 (A0A097QQT4), Acetivibrio thermocellus F7 (Q84C00), Acetivibrio thermocellus NCIMB 10682 (A3DBX3), Acetivibrio thermocellus NRRL B-4536 (A3DBX3)
Manually annotated by BRENDA team