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Information on EC 3.2.1.73 - licheninase and Organism(s) Bacillus licheniformis and UniProt Accession P27051

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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:
Bacillus licheniformis
UNIPROT: P27051
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The taxonomic range for the selected organisms is: Bacillus licheniformis
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-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-glucan 4-glucanohydrolase
-
-
-
-
1,3;1,4-beta-glucan endohydrolase
-
-
-
-
beta-(1--> 3), (1--> 4)-D-glucan 4-glucanohydrolase
-
-
-
-
beta-1,3-1,4-glucanase
-
-
endo-beta-1,3-1,4 glucanase
-
-
-
-
laminarinase
-
-
-
-
Lichenase
Mixed linkage beta-glucanase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
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
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
4-methylumbelliferyl 3-O-beta-cellobiosyl-beta-D-glucopyranoside + H2O
4-methylumbelliferone + 3-O-beta-cellobiosyl-beta-D-glucopyranoside
show the reaction diagram
-
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
?
lichenan + 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-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-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
-
-
-
-
?
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
-
-
-
-
?
barley beta-glucan + H2O
3-O-beta-cellobiosyl-D-glucose + 3-O-beta-cellotriosyl-D-glucose
show the reaction diagram
-
-
oligosaccharides, mainly trisaccharide and tetrasaccharide
-
?
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
barley-beta-glucan + H2O
?
show the reaction diagram
-
-
-
-
?
lichenan + H2O
3-O-beta-cellobiosyl-D-glucose + 3-O-beta-cellotriosyl-D-glucose
show the reaction diagram
-
-
oligosaccharides, mainly trisaccharide and tetrasaccharide
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
-
?
lichenan + H2O
cellotriose + cellotetraose + ?
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
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
?
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
Ca2+
necessary for the activity of the enzyme
Cu2+
-
inhibits isozyme EG1 by 35%, but slightly activates isozyme EG2 at 2.5 mM
Mn2+
-
activates at 10 mM
Ni2+
-
1 mM, 114% of initial activity
additional information
-
poor effects on both isozymes by Mg2+ and EDTA at 2.5 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-ethyl-3-(3-dimethylaminopropyl)carbodiimide
-
-
2,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
-
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
-
-
Co2+
-
inhibits isozyme EG1 by 35%, and isozyme EG2 also slightly, at 2.5 mM
EDTA
-
1 mM, 77% residual activity
Fe2+
-
inhibits isozyme EG1 by 50% at 2.5 mM
Fe3+
-
1 mM, 65% residual activity
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
hexadecyltrimethylammonium bromide
-
1 mM, no residual activity
Hg2+
-
complete inhibition of both isozymes at 2.5 mM
Mn2+
-
1 mM, 87% residual activity
N-bromosuccinimide
-
1 mM, no residual activity
sodium perborate
-
isozymes EG1 and EG2 retain 58% and 66.8% of their activities after 1 h of incubation at 40°C in the presence of 0.2% w/v sodium perborate, respectively
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
1 mM, 115% of initial activity
beta-mercaptoethanol
-
0.1%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7
2,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30°C
0.7
3,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30°C
0.37 - 0.6
4-methylumbelliferyl 3-O-beta-cellobiosyl-beta-D-glucoside
1
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30°C
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, 30°C
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, 30°C
1.36
beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
-
pH 7.0, 35°C
0.34
beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
-
pH 7.0, 35°C
0.15
beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
-
pH 7.0, 35°C
additional information
Barley beta-glucan
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.04
beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
-
pH 7.0, 35°C
0.91
beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
-
pH 7.0, 35°C
1.35
beta-D-Glc-(1-4)-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-alpha-D-Glc-fluoride
-
pH 7.0, 35°C
60 - 708.3
lichenan
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.5
2,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30°C
0.9
3,4-dinitrophenyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30°C
6
4-methylumbelliferyl-beta-D-Glc-(1-4)-beta-D-Glc-(1-3)-beta-D-Glc
-
pH 7.2, 30°C
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, 30°C
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, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1280
-
recombinant enzyme, using barley beta-glucan as a substrate, at 50°C and pH 6.0
1335
-
recombinant enzyme, using lichenan as a substrate, at 50°C and pH 6.0
15.6
-
isozyme EG1, pH 5.0, 50°C, substrate lichenan
1906
-
recombinant enzyme, using lichenan as a substrate
2.7
-
purified recombinant linear enzyme and wild-type enzyme, substrate barley-beta-glucan, pH and temperature not specified in the publication
2479
-
recombinant enzyme after 8.74fold purification, using barley beta-glucan as a substrate
283.8
-
recombinant enzyme from crude extract, using barley beta-glucan as a substrate
767
-
isozyme EG2, pH 5.0, 50°C, substrate lichenan
8231
-
pH 6.5, 60°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5
-
isozyme EG1
5.6
-
recombinant enzyme
6
-
recombinant enzyme
7
-
isozyme EG2
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 7
activity range
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40
-
recombinant enzyme
45
-
recombinant enzyme
70
-
isozyme EG1
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
40 - 70
activity range
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
the wild-type enzyme contains a signal peptide
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GUB_BACLI
243
1
27435
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27000
-
1 * 27000, recombinant mature circular enzyme variant LicA-C1 without intein sequences, SDS-PAGE
28000
-
recombinant enzyme with a six-His tag at the N terminus, SDS-PAGE
30000
-
1 * 30000, isozyme EG1, SDS-PAGE, 1 * 50000, isozyme EG2, SDS-PAGE
34000
-
SDS-PAGE
50000
-
1 * 30000, isozyme EG1, SDS-PAGE, 1 * 50000, isozyme EG2, SDS-PAGE
55000
-
isozyme EG2, native PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 25000, SDS-PAGE, x * 24400, calculated
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N207D
mutant displays better thermotolerance than the wild type but also reduced activity
E134A
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
-
retains approximately 80% of original activity after treatment at pH 3.0 for 12 h
677749
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 - 6
-
the recombinant enzyme is stable between pH 4.0 and 6.0, having 85% of the original activity
677749
8
-
retains approximately 80% of original activity after treatment at pH 8.0 for 12 h
677749
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
12 h, 50% activity remaining
40 - 50
-
purified isozymes EG1 and EG2, retaining over 90% activity after 1 h
50 - 70
-
after incubation at 50, 60, and 70°C for 30 min, the residual activity is 95, 60, and 0%, respectively
60
-
purified isozymes EG1 and EG2, half-lives are 55 min and 5 h, respectively
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
70
-
purified isozymes EG1 and EG2, half-lives are 10 min and 52 min, respectively
additional information
-
addition of 1 mM EDTA causes the linear enzyme to denature at 59.8°C, which is lower compared to the melting temperature of 62.6°C in the presence of calcium. At 1 mM EDTA, the circular enzyme variant LicA-C1 shows a melting temperature of 62.8°C, at 1 mM CaCl2 the melting temperature is 66.4°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene bg1, recombinant expression in Escherichia coli and in Pichia pastoris
expressed in Escherichia coli strain BL21 (DE3)
-
expressed in Pichia pastoris strain GS115
-
expression in Escherichia coli
-
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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
Hahn, M.; Pons, J.; Planas, A.; Querol, E.; Heinemann, U.
Crystal structure of Bacillus licheniformis 1,3-1,4-beta-D-glucan 4-glucanohydrolase at 1.8 A resolution
FEBS Lett.
374
221-224
1995
Bacillus licheniformis (P27051), Bacillus licheniformis
Manually annotated by BRENDA team
Abel, M.; Planas, A.; Christensen, U.
Presteady-state kinetics of Bacillus 1,3-1,4-beta-glucanase: binding and hydrolysis of a 4-methylumbelliferyl trisaccharide substrate
Biochem. J.
357
195-202
2001
Bacillus licheniformis
Manually annotated by BRENDA team
Abel, M.; Iversen, K.; Planas, A.; Christensen, U.
Pre-steady-state kinetics of Bacillus licheniformis 1,3-1,4-beta-glucanase: evidence for a regulatory binding site
Biochem. J.
371
997-1003
2003
Bacillus licheniformis
Manually annotated by BRENDA team
Faijes, M.; Perez, X.; Perez, O.; Planas, A.
Glycosynthase activity of Bacillus licheniformis 1,3-1,4-beta-glucanase mutants: specificity, kinetics, and mechanism
Biochemistry
42
13304-13318
2003
Bacillus licheniformis
Manually annotated by BRENDA team
Fairweather, J.K.; Faijes, M.; Driguez, H.; Planas, A.
Specificity studies of Bacillus 1,3-1,4-beta-glucanases and application to glycosynthase-catalyzed transglycosylation
Chembiochem
3
866-873
2002
Bacillus licheniformis
Manually annotated by BRENDA team
Teng, D.; Wang, J.H.; Fan, Y.; Yang, Y.L.; Tian, Z.G.; Luo, J.; Yang, G.P.; Zhang, F.
Cloning of beta-1,3-1,4-glucanase gene from Bacillus licheniformis EGW039 (CGMCC 0635) and its expression in Escherichia coli BL21 (DE3)
Appl. Microbiol. Biotechnol.
72
705-712
2006
Bacillus licheniformis, Bacillus licheniformis EGW039 / CGMCC 0635
Manually annotated by BRENDA team
Teng, D.; Fan, Y.; Yang, Y.L.; Tian, Z.G.; Luo, J.; Wang, J.H.
Codon optimization of Bacillus licheniformis beta-1,3-1,4-glucanase gene and its expression in Pichia pastoris
Appl. Microbiol. Biotechnol.
74
1074-1083
2007
Bacillus licheniformis, Bacillus licheniformis EGW039 / CGMCC 0635
Manually annotated by BRENDA team
Gargallo, R.; Cedano, J.; Mozo-Villarias, A.; Querol, E.; Oliva, B.
Study of the influence of temperature on the dynamics of the catalytic cleft in 1,3-1,4-beta-glucanase by molecular dynamics simulations
J. Mol. Model.
12
835-845
2006
Bacillus licheniformis (P27051), Bacillus licheniformis
Manually annotated by BRENDA team
van Lieshout, J.F.; Perez Gutierrez, O.N.; Vroom, W.; Planas, A.; de Vos, W.M.; van der Oost, J.; Koutsopoulos, S.
Thermal stabilization of an endoglucanase by cyclization
Appl. Biochem. Biotechnol.
167
2039-2053
2012
Bacillus licheniformis
Manually annotated by BRENDA team
Chaari, F.; Bhiri, F.; Blibech, M.; Maktouf, S.; Ellouz-Chaabouni, S.; Ellouz-Ghorbel, R.
Potential application of two thermostable lichenases from a newly isolated Bacillus licheniformis UEB CF: purification and characterization
Process Biochem.
47
509-516
2012
Bacillus licheniformis, Bacillus licheniformis UEB CF
-
Manually annotated by BRENDA team
Gao, Z.
Purification and characterization of a novel lichenase from Bacillus licheniformis GZ-2
Biotechnol. Appl. Biochem.
63
249-256
2016
Bacillus licheniformis, Bacillus licheniformis GZ-2
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