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Information on EC 3.2.1.4 - cellulase and Organism(s) Acetivibrio thermocellus and UniProt Accession P10477
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3.2.1.4 cellulaseIUBMB Comments
Will also hydrolyse 1,4-linkages in beta-D-glucans also containing 1,3-linkages.
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Word Map
- 3.2.1.4
- cellulose
- trichoderma
- biomass
- reesei
- xylanase
-
cellulolytic
-
saccharification
-
lignocellulosic
- cellobiose
- straw
- lignin
- polysaccharide
- aspergillus
- glycoside
- beta-glucosidase
- corn
-
biofuels
- pectinase
- xylan
- hemicellulose
- bagasse
- penicillium
- endoglucanases
-
bioethanol
- xylose
- amylase
- polygalacturonase
- sugarcane
-
carbohydrate-binding
-
feedstock
- viride
- glucans
- thermocellum
- bran
- carboxymethylcellulose
-
microcrystalline
- exoglucanase
-
cellulose-binding
- laccase
-
biorefinery
- rumen
- biotechnology
- analysis
-
novozyme
-
silage
- endoxylanase
-
compost
- industry
- textile industry
- food industry
- biofuel production
- agriculture
-
deconstruct
- xylobiose
- diagnostics
- harzianum
- degradation
- chrysosporium
- synthesis
- detergent
- environmental protection
- xyloglucans
The taxonomic range for the selected organisms is: Acetivibrio thermocellus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
cellulase, cel7a, cellobiohydrolase i, cel5a, cel6a, avicelase, endocellulase, celluclast, cel7b, cbhii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
9.5 cellulase
-
-
-
-
Abscission cellulase
-
-
-
-
alkali cellulase
-
-
-
-
Alkaline cellulase
-
-
-
-
avicelase
-
-
-
-
beta-1,4-endoglucan hydrolase
-
-
-
-
beta-1,4-glucanase
-
-
-
-
Carboxymethyl cellulase
-
-
-
-
Carboxymethyl-cellulase
-
-
-
-
carboxymethylcellulase
-
-
-
-
CEL1
-
-
-
-
cellobiohydrolase
-
-
-
-
celluase A
-
-
-
-
celludextrinase
-
-
-
-
Cellulase
-
-
-
-
cellulase A 3
-
-
-
-
Cellulase E1
-
-
-
-
Cellulase E2
-
-
-
-
Cellulase E4
-
-
-
-
Cellulase E5
-
-
-
-
Cellulase SS
-
-
-
-
Cellulase V1
-
-
-
-
cellulosin AP
-
-
-
-
CMCase
-
-
-
-
CX-cellulase
-
-
-
-
EG1
-
-
-
-
EG2
-
-
-
-
EG3
-
-
-
-
EGA
-
-
-
-
EGB
-
-
-
-
EGC
-
-
-
-
EGCCA
-
-
-
-
EGCCC
-
-
-
-
EGCCD
-
-
-
-
EGCCF
-
-
-
-
EGCCG
-
-
-
-
EGD
-
-
-
-
EGE
-
-
-
-
EGF
-
-
-
-
EGH
-
-
-
-
EGI
-
-
-
-
EGIV
-
-
-
-
EGM
-
-
-
-
EGSS
-
-
-
-
EGX
-
-
-
-
EGY
-
-
-
-
EGZ
-
-
-
-
endo-1,4-beta-D-glucanase
-
-
-
-
endo-1,4-beta-glucanase
-
-
-
-
endo-1,4-beta-glucanase E1
-
-
-
-
endo-1,4-beta-glucanase V1
-
-
-
-
endocellulase E1
-
-
-
-
endoglucanase
endoglucanase D
-
-
-
-
FI-CMCASE
-
-
-
-
pancellase SS
-
-
-
-
Thermoactive cellulase
-
-
-
-
endoglucanase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
4-beta-D-glucan 4-glucanohydrolase
Will also hydrolyse 1,4-linkages in beta-D-glucans also containing 1,3-linkages.
CAS REGISTRY NUMBER
COMMENTARY
9012-54-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
carboxymethyl cellulose + H2O
cellobiose + cellooligosaccharides
-
-
-
-
?
carboxymethylcellulose + H2O
?
-
the smallest product is a disaccharide
-
-
?
cellulose + H2O
?
-
endoglucanase I shows very low activity with acid-swollen cellulose
-
-
?
cellulose + H2O
?
-
Walseth cellulose shows 1.1% of the activity with carboxymethylcellulose
-
-
?
cellulose + H2O
?
-
little ability to hydrolyze ordered cellulose
-
-
?
lichenan + H2O
?
-
6% of the activity with carboxymethylcellulose
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
endoglucanase 1b: cellotriose, 45%, cellotetraose, 31%, cellobiose, 17%, and cellopentaose, 8%. Endoglucanase 2: cellotriose, 50%, and cellotetraose, 30%
?
cellopentaose + H2O
additional information
-
-
enzyme form EGB and EGC
-
-
?
additional information
?
-
-
no activity with p-nitrophenyl-beta-D-glucoside
-
-
?
additional information
?
-
-
modular enzyme that contains a family 30 carbohydrate-binding modules, CBM, and a family 9 catalytic module at its N-terminal moiety. The CBM is extremely important not only because it mediates the binding of the enzyme to the substrate but also because it participates in the catalytic function of the enzyme or contributes to maintain the correct tertiary structure of the family 9 catalytic module for expressing enzyme activity
-
-
?
additional information
?
-
-
substrates are acid swollen cellulose, lichenan, beta-glucan, carboxymethyl cellulose, galactomannans, oat spelt xylan, avicel, and steam exploded bagasse, no activity glucomannan and laminarin
-
-
?
additional information
?
-
-
final hydrolysed product produced from carboxymethyl cellulose by chimera 1 is glucose confirming both beta-1,4-endoglucanase and beta-1,4-glucosidase activities, while the products of CtGH5-F194A point mutant are cellobiose and cello-oligosaccharides. Product indentification by thin layer chromatography. Enzymatic hydrolysis of 1% w/v Sorghum stalk pretreated by 1% NaOH by mutant CtGH5-F194A with or without wild-type enzyme CtGH1, which exhibits beta-glucosidase activity. No activity of the wild-type enzyme and mutant F194A with 4-nitrophenyl beta-D-glucoside, which is a substrate of the beta-glucosidase activity of chimeric mutant CtGH1-CtGH5-F194A
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Mg2+
Na+
-
activates the truncated enzyme mutant CtLic26A-Cel5 about 2fold
Ni2+
-
activates the truncated enzyme mutant CtLic26A-Cel5 about 2fold
additional information
Ca2+
-
activates the truncated enzyme mutant CtLic26A-Cel5 about 2fold
Ca2+
two endogenous calcium ions are observed in the calcium-binding sites of all CtCel9QDELTAc structures, enzyme mutant structure analysis, overview
Mg2+
-
activates the truncated enzyme mutant CtLic26A-Cel5 about 2fold
additional information
the enzyme contains an unusual metal-ion site, which is originally modelled as a Ca2+ site (PDB ID 2xqo) but features aspartic acid, asparagine and two histidine imidazoles as coordinating residues, which are more consistent with a transition-metal binding environment. This metal-ion site can accommodate a range of transition metals, i.e. Fe2+, Cu2+, Mn2+ and Ni2+, but not Ca2+, whilst the three-dimensional structure and mass spectrometry show that one of the histidines is partially covalently modified and is present as a 2-oxohistidine residue, a feature that is rarely observed but that is believed to be involved in an off-switch to transition-metal binding. Atomic resolution complexes define the metal-ion site and also reveal the binding of an unusual fructosylated oligosaccharide, which is presumably present as a contaminant in the cellohexaose used for crystallization
additional information
-
the enzyme contains an unusual metal-ion site, which is originally modelled as a Ca2+ site (PDB ID 2xqo) but features aspartic acid, asparagine and two histidine imidazoles as coordinating residues, which are more consistent with a transition-metal binding environment. This metal-ion site can accommodate a range of transition metals, i.e. Fe2+, Cu2+, Mn2+ and Ni2+, but not Ca2+, whilst the three-dimensional structure and mass spectrometry show that one of the histidines is partially covalently modified and is present as a 2-oxohistidine residue, a feature that is rarely observed but that is believed to be involved in an off-switch to transition-metal binding. Atomic resolution complexes define the metal-ion site and also reveal the binding of an unusual fructosylated oligosaccharide, which is presumably present as a contaminant in the cellohexaose used for crystallization
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
lactose
-
51000 Da subunit from the multicomponent cellulase complexes
Tris
Tris almost completely suppresses CtCel9Q hydrolase activity, a Tris molecule is bound to three catalytic residues of CtCel9Q and occupies subsite -1 of the CtCel9Q active-site cleft, enzyme mutant crystal structure analysis, overview
cellobiose
-
51000 Da subunit from the multicomponent cellulase complexes
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.045
beta-Glucan
-
pH 4.2, 60°C, recombinant mutant CtGH1-CtGH5-F194A
0.006
carboxymethyl cellulose
-
pH 4.2, 60°C, recombinant wild-type enzyme CtGH5
-
0.026
carboxymethyl cellulose
-
pH 4.2, 60°C, recombinant mutant CtGH5-F194A
-
0.115
carboxymethyl cellulose
-
pH 4.2, 60°C, recombinant mutant CtGH1-CtGH5-F194A
-
0.053
lichenan
-
pH 4.2, 60°C, recombinant chimeric mutant CtGH1-CtGH5-F194A
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
315
-
recombinant enzyme from cytoplasmic supernatant of Escherichia coli
428
-
recombinant enzyme from granules produced by Escherichia coli
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 7.5
over 50% of maximal activity within this range, profile overview
4.8 - 8.2
-
more than 50% of maximal activity at pH 4.8 and at pH 8.2
5 - 7.7
-
pH 5.0: about 65% of maximal activity, pH 7.7. about 65% of maximal activity, deletion variants CelEM1, CelEM2 and CelEM3
5 - 8
5 - 8
-
pH 5.0: about 35% of maximal activity, pH 8.0: about 30% of maximal activity
5 - 8
-
pH 5.0: about 50% of maximal activity, pH 8.0: about 45% of maximal activity, endoglucanase 1b
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
60
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35 - 75
over 50% of maximal activity within this range, profile overview
50 - 80
-
50°C: about 40% of maximal activity, 80°C: about 30% of maximal activity, deletion variants CelEM1, CelEM2 and CelEM3
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
the enzyme belongs to the glycoside hydrolase family 5,GH5
additional information
additional information
modelling of the metal-ion sites in the protein three-dimensional structure, overview
additional information
-
modelling of the metal-ion sites in the protein three-dimensional structure, overview
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
64000
65000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
modular enzyme that contains a family 30 carbohydrate-binding modules, CBM, and a family 9 catalytic module at its N-terminal moiety. The CBM is extremely important not only because it mediates the binding of the enzyme to the substrate but also because it participates in the catalytic function of the enzyme or contributes to maintain the correct tertiary structure of the family 9 catalytic module for expressing enzyme activity
additional information
the precursor form of CtCel9Q comprises a signal peptide, a glycoside hydrolase family 9 catalytic domain, a type 3c carbohydrate-binding module (CBM), and a type I dockerin domain
additional information
-
the precursor form of CtCel9Q comprises a signal peptide, a glycoside hydrolase family 9 catalytic domain, a type 3c carbohydrate-binding module (CBM), and a type I dockerin domain
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
no modification
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of recombinant native enzyme diffract to 2.1 A, crystals of seleno-L-methionine-containing protein diffract to 2.8 A, hanging-drop vapour-diffusion method, crystals belong to space group P4(3)2(1)2
-
hanging drop vapor diffusion method at 20°C, crystal structure of Cel44A is solved at a resolution of 0.96 A.The crystal structures of E186Q mutant complexed with cellopentaose and cellohexaose are solved at 2.0 and 1.8 A resolution, respectively
-
purified recombinant C-terminally truncated mutant enzyme CtCel9QDELTAc complexed with Tris, Tris + cellobiose, cellobiose + cellotriose, cellotriose, and cellotetraose, sitting drop vapor diffusion method, a drop consists of 0.0013 ml of protein solution and 0.0013 ml of reservoir solution containing 9-12% w/v PEG 3350, 15-20% v/v PEG 550MME, 30 mM NaBr, 30 mM NaF, and 30 mM NaI, and 0.1 M Tris, pH 8.5, with or without 10 mM cellooligosaccharides, equilibration against 0.2 ml reservoir solution, 22°C, X-ray diffraction structure determination analysis at resolutions 1.50, 1.70, 2.05, 2.05, and 1.75 A, respectively. In both the oligosaccharide-free and cellobiose-bound CtCel9QDELTAc structures, a Tris molecule is observed in the active site
purified recombinant detagged enzyme in complex with G3 or G5f, sitting drop vapour diffuson method, mixing of 0.027 ml of 40 mg/ml protein in 20 mM Tris, pH 7.5, and 6.7 mM G3 or G5f, with 0.027 ml of reservoir solution containing 12% Tacsimate, pH 5.0, 18% or 20% PEG 3350, 2 mM manganese(II) acetate, respectively, and equilibration against 0.4 ml of reservoir solution, 20°C, 3 days, X-ray diffraction structure determination and analysis at 1.04 and 0.99 A resolution, respectively, modelling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F194A
-
site-directed mutagenesis, the mutant shows 2fold increased activity compared to wild-type enzyme
additional information
additional information
-
construction of a His6-tagged truncated enzyme mutant CtLic26A-Cel5
additional information
-
replacement of carbohydrate-binding module either with a family 3 microcrystalline cellulose-directed carbohydrate-binding module from Clostridium josui scaffoldin, or a family 6 xylan-directed carbohydrate-binding module from Clostridium stercorarium xylanase 11A. Chimeric endoglucanases show enhanced activity that is affected by carbohydrate-binding module binding specificity. The chimeric enzymes can efficiently degrade milled lignocellulosic materials, such as corn hulls
additional information
construction of a C-terminally truncated enzyme, CtCel9QDELTAc
additional information
-
construction of a C-terminally truncated enzyme, CtCel9QDELTAc
additional information
-
enzyme mutant CtGH5-F194A is fused with a beta-1,4-glucosidase, CtGH1 from Clostridium thermocellum to develop a chimeric enzyme. Improved structural integrity, thermostability and enhanced bifunctional enzyme activities of the chimeric mutant compared to the single point mutant
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
65
75
-
about 20% loss of activity after 30 min, about 50% loss of activity after 2 h, 51000 Da subunit from the multicomponent cellulase complexes
additional information
additional information
enzyme melting transition occurs at 72°C in presence of EDTA, Ca2+ does not affect the melting temperature
additional information
-
enzyme melting transition occurs at 72°C in presence of EDTA, Ca2+ does not affect the melting temperature
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)pLysS, cleavage of the His-tag by 3C protease
recombinant His6-tagged truncated mutant cellulase CtLic26A-Cel5 from Escherichia coli strain BL21 by metal affinity chromatography
-
the enzyme is the 51000 Da subunit from the multicomponent cellulase complexes
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His6-tagged wild-type and truncated mutant cellulase in Escherichia coli strain BL21
-
gene celQ, sequence comparisons, recombinant expression of truncated and point mutant enzymes in Escherichia coli strain BL21(DE3)
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)pLysS
recombinant expression of soluble enzyme chimeric mutant CtGH1-L1-CtGH5-F194A in Escherichia coli strain BL21
-
wild-type enzyme and mutant enzymes E186Q and E359Q, expression in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
degradation
cellulase complex containing cellulolytic enzymes,endoglucanase CelE, EC 3.2.1.4, and beta-glucosidase BglA, EC 3.2.1.21, to completely degrade cellulose to glucose. The cellulases are displayed on the cell surface of Corynebacterium glutamicum by using themechanosensitive channel to anchor enzymes in the cytoplasmic membrane. The displayed cellulases complexes have a synergic effect on the direct conversion of biomass to reducing sugars leading to 3.1- to 6.0fold increase compared to the conversion by the secreted cellulases complexes. The displayed cellulases complexes increase the residual activities of cCelEand cBglA at 70°C from 28.3% and 24.3% in the secreted form to 65.1% and 82.8%, respectively
degradation
-
replacement of carbohydrate-binding module by modules from enzymes with different specificities leads to enhanced activity that is affected by carbohydrate-binding module binding specificity, e.g. on ball-milled cellulose or avicel. The chimeric enzymes can efficiently degrade milled lignocellulosic materials, such as corn hulls
food industry
-
the capacity of Cel8A to cleave 1,3-1,4-beta-glucans is significantly affected by the presence of the barley-based feed for broilers. Exogenous 1,3-1,4-beta-glucanases (EC 3.2.1.73) but not 1,4-beta-glucanases are obligatory enzymes to improve the nutritive value of barley-based diets for broilers. Enzyme is completely resistant to proteolytic inactivation after a 30 min incubation with pancreatic proteases
synthesis
synthesis
heterologous expression in Bacillus subtilis combined with customized signal peptides for secretion from a random libraries with 173 different signal peptides originating from the Bacillus subtilis genome. The customized signal peptide does not affect enzyme performance when assayed on carboxymethyl cellulose, phosphoric acid swollen cellulose, and microcrystalline cellulose
synthesis
-
enhanced production of enzyme in Escherichia coli. High-cell-density and optimal CenC expression are obtained in ZYBM9 medium induced either with 0.5 mM IPTG/150 mM lactose, after 6 h induction at 37°C. Before induction, bacterial cells are given heat shock (42°C) for 1 h when culture density (OD600 nm) reached at 0.6. Intracellular enzyme activity is enhanced by 6.67- and 3.20fold in ZYBM9 (yeast extract 0.5% (w/v), NaCl 0.5% (w/v), tryptone 1.0% (w/v), NH4Cl 0.1% (w/v), KH2PO4 0.3% (w/v), Na2HPO4 0.6% (w/v), MgSO4.7H2O 1 mM, and Glucose 0.4% (w/v)) and 3×ZYBM9 medium, respectively, under optimal conditions
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mori, Y.
Purification and characterization of an endoglucanase from the cellulosomes (multicomponent cellulase complexes) of Clostridium thermocellum
Biosci. Biotechnol. Biochem.
56
1198-1203
1992
Acetivibrio thermocellus
Halliwell, G.; Halliwell, N.
Cellulolytic enzyme components of the cellulase complex of Clostridium thermocellum
Biochim. Biophys. Acta
992
223-229
1989
Acetivibrio thermocellus
-
Robson, L.M.; Chambliss, G.H.
Cellulases of bacterial origin
Enzyme Microb. Technol.
11
626-644
1989
Acetivibrio cellulolyticus, Bacillus subtilis, Bacillus sp. (in: Bacteria), Cellulomonas fimi, Acetivibrio thermocellus, Dickeya chrysanthemi, Ruminococcus albus, Thermobifida fusca, Thermomonospora curvata, Bacillus sp. (in: Bacteria) No. 1139, Bacillus sp. (in: Bacteria) N-4, Ruminococcus albus F40
-
Beguin, P.; Joliff, G.; Juy, M.; Amit, A.G.; Millet, J.; Poljak, R.J.; Aubert, J.P.
Crystalline endoglucanase D from Clostridium thermocellum overproduced in Escherichia coli
Methods Enzymol.
160
355-362
1988
Acetivibrio thermocellus
-
Ng, T.K.; Zeikus, J.G.
Endoglucanase from Clostridium thermocellum
Methods Enzymol.
160
351-355
1988
Acetivibrio thermocellus
-
Joliff, G.; Beguin, P.; Juy, M.; Millet, J.; Ryter, A.; Poljak, R.; Aubert, J.P.
Isolation, crystallization and properties of a new cellulase of Clostridium thermocellum overproduced in Escherichia coli
Bio/Technology
4
896-900
1986
Acetivibrio thermocellus
-
Romaniec, M.P.M.; Fauth, U.; Kobayashi, T.; Huskisson, N.S.; Barker, P.J.; Demain, A.L.
Purification and characterization of a new endoglucanase from Clostridium thermocellum
Biochem. J.
283
69-73
1992
Acetivibrio thermocellus
-
Abdeev, R.M.; Goldenkova, I.V.; Musiychuk, K.A.; Piruzian, E.S.
Exploring the properties of thermostable Clostridium thermocellum cellulase CelE for the purpose of its expression in plants
Biochemistry
66
808-813
2001
Acetivibrio thermocellus
Arai, T.; Araki, R.; Tanaka, A.; Karita, S.; Kimura, T.; Sakka, K.; Ohmiya, K.
Characterization of a cellulase containing a family 30 carbohydrate-binding module (CBM) derived from Clostridium thermocellum CelJ: importance of the CBM to cellulose hydrolysis
J. Bacteriol.
185
504-512
2003
Acetivibrio thermocellus, Acetivibrio thermocellus CelJ
Najmudin, S.; Guerreiro, C.I.; Ferreira, L.M.; Romao, M.J.; Fontes, C.M.; Prates, J.A.
Overexpression, purification and crystallization of the two C-terminal domains of the bifunctional cellulase ctCel9D-Cel44A from Clostridium thermocellum
Acta Crystallogr. Sect. F
61
1043-1045
2005
Acetivibrio thermocellus
Kitago, Y.; Karita, S.; Watanabe, N.; Kamiya, M.; Aizawa, T.; Sakka, K.; Tanaka, I.
Crystal structure of Cel44A, a glycoside hydrolase family 44 endoglucanase from Clostridium thermocellum
J. Biol. Chem.
282
35703-35711
2007
Acetivibrio thermocellus
Ahmed, S.; Deka, D.; Jawed, M.; Goyal, D.; Fontes, C.; Goyal, A.
Biochemical characterization of a recombinant derivative (CtLic26A-Cel5) of a cellulosomal cellulase from Clostridium thermocellum
Curr. Trends Biotechnol. Pharm.
3
56-63
2009
Acetivibrio thermocellus
-
Kim, S.J.; Hyeon, J.E.; Jeon, S.D.; Choi, G.W.; Han, S.O.
Bi-functional cellulases complexes displayed on the cell surface of Corynebacterium glutamicum increase hydrolysis of lignocelluloses at elevated temperature
Enzyme Microb. Technol.
66
67-73
2014
Acetivibrio thermocellus (P10477), Acetivibrio thermocellus DSM 1237 (P10477)
Lan Thanh Bien, T.; Tsuji, S.; Tanaka, K.; Takenaka, S.; Yoshida, K.
Secretion of heterologous thermostable cellulases in Bacillus subtilis
J. Gen. Appl. Microbiol.
60
175-182
2014
Acetivibrio thermocellus (A3DC29), Acetivibrio thermocellus (P04956), Acetivibrio thermocellus DSM 1237 (A3DC29), Acetivibrio thermocellus DSM 1237 (P04956)
Fernandes, V.; Costa, M.; Ribeiro, T.; Serrano, L.; Cardoso, V.; Santos, H.; Lordelo, M.; Ferreira, L.; Fontes, C.
1,3-1,4-beta-Glucanases and not 1,4-beta-glucanases improve the nutritive value of barley-based diets for broilers
Anim. Feed Sci. Technol.
211
153-163
2016
Acetivibrio thermocellus
-
Haq, I.U.; Akram, F.
Enhanced production of a recombinant multidomain thermostable GH9 processive endo-1,4-beta-glucanase (CenC) from Ruminiclostridium thermocellum in a mesophilic host through various cultivation and induction strategies
Appl. Biochem. Biotechnol.
183
171-188
2017
Acetivibrio thermocellus, Acetivibrio thermocellus ATCC 27405
Ichikawa, S.; Yoshida, M.; Karita, S.; Kondo, M.; Goto, M.
Carbohydrate-binding modules influence substrate specificity of an endoglucanase from Clostridium thermocellum
Biosci. Biotechnol. Biochem.
80
188-192
2016
Acetivibrio thermocellus, Acetivibrio thermocellus 132
Urresti, S.; Cartmell, A.; Liu, F.; Walton, P.H.; Davies, G.J.
Structural studies of the unusual metal-ion site of the GH124 endoglucanase from Ruminiclostridium thermocellum
Acta Crystallogr. Sect. F
74
496-505
2018
Acetivibrio thermocellus (A3DCJ4), Acetivibrio thermocellus, Acetivibrio thermocellus DSM 1237 (A3DCJ4), Acetivibrio thermocellus NBRC 103400 (A3DCJ4), Acetivibrio thermocellus ATCC 27405 (A3DCJ4), Acetivibrio thermocellus VPI 7372 (A3DCJ4), Acetivibrio thermocellus NCIMB 10682 (A3DCJ4), Acetivibrio thermocellus NRRL B-4536 (A3DCJ4)
Nath, P.; Dhillon, A.; Kumar, K.; Sharma, K.; Jamaldheen, S.B.; Moholkar, V.S.; Goyal, A.
Development of bi-functional chimeric enzyme (CtGH1-L1-CtGH5-F194A) from endoglucanase (CtGH5) mutant F194A and ?-1,4-glucosidase (CtGH1) from Clostridium thermocellum with enhanced activity and structural integrity
Biores. Technol.
282
494-501
2019
Acetivibrio thermocellus
Jeng, W.Y.; Liu, C.I.; Lu, T.J.; Lin, H.J.; Wang, N.C.; Wang, A.H.
Crystal structures of the C-terminally truncated endoglucanase Cel9Q from Clostridium thermocellum complexed with cellodextrins and Tris
ChemBioChem
20
295-307
2019
Acetivibrio thermocellus (Q9AJF8), Acetivibrio thermocellus
EXTERNAL LINKS (specific for EC-Number 3.2.1.4)
Transporter Classification Database (TCDB): 4.D.3.1.6
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