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Information on EC 3.2.1.4 - cellulase and Organism(s) Thermobifida fusca and UniProt Accession P26221
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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: Thermobifida fusca
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
Cel9A-68
Cel9A is secreted as a 90400 Da protein. Limited proteolysis of Cel9A produces Cel9A-68
Cel9A-90
Cel9A is secreted as a 90400 Da protein. Limited proteolysis of Cel9A produces Cel9A-68
9.5 cellulase
-
-
-
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Abscission cellulase
-
-
-
-
alkali cellulase
-
-
-
-
Alkaline cellulase
-
-
-
-
avicelase
-
-
-
-
beta-1,4-endoglucan hydrolase
-
-
-
-
beta-1,4-glucanase
-
-
-
-
Carboxymethyl cellulase
-
-
-
-
Carboxymethyl-cellulase
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-
-
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carboxymethylcellulase
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-
-
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CEL1
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-
-
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cellobiohydrolase
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-
-
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celluase A
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-
-
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celludextrinase
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-
-
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Cellulase
cellulase A 3
-
-
-
-
Cellulase E1
-
-
-
-
Cellulase E2
-
-
-
-
Cellulase E4
-
-
-
-
Cellulase E5
-
-
-
-
Cellulase SS
-
-
-
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Cellulase V1
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-
-
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cellulosin AP
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-
-
-
CMCase
-
-
-
-
CX-cellulase
-
-
-
-
EG1
-
-
-
-
EG2
-
-
-
-
EG3
-
-
-
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EGA
-
-
-
-
EGB
-
-
-
-
EGC
-
-
-
-
EGCCA
-
-
-
-
EGCCC
-
-
-
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EGCCD
-
-
-
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EGCCF
-
-
-
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EGCCG
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-
-
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EGD
-
-
-
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EGE
-
-
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-
EGF
-
-
-
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EGH
-
-
-
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EGI
-
-
-
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EGIV
-
-
-
-
EGM
-
-
-
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EGSS
-
-
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EGX
-
-
-
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EGY
-
-
-
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EGZ
-
-
-
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endo-1,4-beta-D-glucanase
-
-
-
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endo-1,4-beta-glucanase
endo-1,4-beta-glucanase E1
-
-
-
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endo-1,4-beta-glucanase V1
-
-
-
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endocellulase E1
-
-
-
-
endoglucanase
endoglucanase D
-
-
-
-
FI-CMCASE
-
-
-
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pancellase SS
-
-
-
-
Thermoactive cellulase
-
-
-
-
Cellulase
-
-
-
-
endo-1,4-beta-glucanase
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-
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endoglucanase
-
-
-
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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
alpha-chitin + H2O
?
-
due to the binding, it seems chitin would be an inhibitor of Cel6B, Cel9A and Cel48A, but not of Cel6A and Cel5A
-
-
?
cellotetraose + H2O
2 cellobiose
-
effectively hydrolyzed by endoglucanase E1, limited hydrolysis by endoglucanase E2
-
-
?
cellotriose + H2O
D-glucose + cellobiose
-
effectively hydrolyzed by endoglucanase E1, limited hydrolysis by endoglucanase E2
-
-
?
cellotriose + H2O
D-glucose + cellobiose
-
hydrolyzed by endoglucanase E1, no activity with endoglucanase E2
+ glucose, endoglucanase E1
?
cellulose + H2O
?
-
amorphous cellulose
endoglucanase E1 produces mainly cellobiose and a trace of glucose, endoglucanase E2 produces mainly cellotriose and higher oligomers with some cellobiose and a trace of glucose
?
cellulose + H2O
?
-
the catalytic domains of Cel6A, Cel6B, Cel48A, Cel5A, and Cel9A only show very weak binding to bacterial cellulose
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
endoglucanase E1 exhibits higher activity
endoglucanase E2 produces glucose, cellobiose, cellotriose and higher oligosaccharides. The major end product produced by endoglucanase E1 is cellobiose and small amounts of glucose
?
additional information
?
-
-
Cel9A presents both exo- and endo-cellulase activities, reaction mode, existence of an active conformer prior to ligand binding, overview
-
-
?
NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
-
Cel9A presents both exo- and endo-cellulase activities, reaction mode, existence of an active conformer prior to ligand binding, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.197
2,4-dinitrophenyl beta-D-cellobioside
50°C, mutant enzyme E424G
0.29
2,4-dinitrophenyl beta-D-cellobioside
50°C, mutant enzyme E424A
0.697
2,4-dinitrophenyl beta-D-cellobioside
50°C, wild-type enzyme Cel9A-68
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
2,4-dinitrophenyl beta-D-cellobioside
50°C, wild-type enzyme Cel9A-68
0.07
2,4-dinitrophenyl beta-D-cellobioside
50°C, mutant enzyme E424A
0.7
2,4-dinitrophenyl beta-D-cellobioside
50°C, mutant enzyme E424G
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
genes Tfu_1627, Tfu_1074, Tfu_2176, and Tfu_0901, encoding endo-1,4-beta-glucanases, expression analysis during stationary and exponential growth, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the mechanism for enzymatic hydrolysis of cellulose involves synergistic actions by endoglucanase, EC 3.2.1.4, exoglucanase or cellobiohydrolase, EC 3.2.1.91, and beta-glucosidase, EC 3.2.1.21
physiological function
-
model of synergistic cooperation between endocellulase Cel9A and exocellulase Cel48a. Endocellulase Cel9A is most effective on fresh bacterial cellulose with a presumably uniform surface at the molecular level. Its processive activity likely erodes the surface and thus reduces its own activity. Cel48A is able to hydrolyze the Cel9A-modified substrate efficiently and replenish the uniform surface required by Cel9A, creating a feedback mechanism
additional information
-
mechanochemical model simulations and molecular dynamics of Cel9A, overview. Analysis of the electrostatic surface of the enzyme, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
no modification
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor-diffusion method at room temperature. Structure of the complex of the catalytic domain of endoglucanase Cel6A with a nonhydrolyzable substrate analogue that acts as an inhibitor, methylcellobiosyl-4-thio-beta-cellobioside determined at 1.5 A resolution, structure of mutant enzyme Y73S, structure of mutant enzyme Y73S in complex with methylcellobiosyl-4-thio-beta-cellobioside at 1.04 A resolution, structure of mutant enzyme Y73S in complex with cellotetrose at 1.64 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D55A
activity with carboxymethyl cellulose is 0.2% of wild-type activity, activity with phosphoric acid-swollen cellulose is 1.2% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 1.6% of wild-type activity
D55A/D58A
activity with carboxymethyl cellulose is less than 0.1% of wild-type activity, activity with phosphoric acid-swollen cellulose is 0.13% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 0.5% of wild-type activity
D55N
activity with carboxymethyl cellulose is 0.3% of wild-type activity, activity with phosphoric acid-swollen cellulose is 1.6% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 2.2% of wild-type activity
D58A
activity with carboxymethyl cellulose is 0.4% of wild-type activity, activity with phosphoric acid-swollen cellulose is 1.8% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 3.5% of wild-type activity, mutant enzyme loses about 90% of the initial activity after 15 h at 65°C, compared to 10% loss of wild-type activity
D58N
activity with carboxymethyl cellulose is 0.45% of wild-type activity, activity with phosphoric acid-swollen cellulose is 2% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 2.7% of wild-type activity, mutant enzyme loses about 20% of the initial activity after 15 h at 65°C, compared to 10% loss of wild-type activity
DELTAT245-L251/R252K
activity with carboxymethyl cellulose, acid-swollen cellulose or bacterial microcrystalline cellulose from Acetobacter xylinum is nearly identical to wild-type activity
E424A
activity with carboxymethyl cellulose is 0.13% of wild-type activity, activity with phosphoric acid-swollen cellulose is 0.2% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 0.43% of wild-type activity, kcat/Km for 2,4-dinitrophenyl beta-D-cellobioside is 8.5fold higher than the wild-type value
E424G
activity with carboxymethyl cellulose is 0.3% of wild-type activity, activity with phosphoric acid-swollen cellulose is 1.1% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 2.5% of wild-type activity, kcat/Km for 2,4-dinitrophenyl beta-D-cellobioside is 123.8fold higher than the wild-type value
E424Q
activity with carboxymethyl cellulose is less than 0.1% of wild-type activity, activity with phosphoric acid-swollen cellulose is 0.15% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 1.1% of wild-type activity
Y206F
activity with carboxymethyl cellulose is 7% of wild-type activity, activity with phosphoric acid-swollen cellulose is 4.1% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 8.3% of wild-type activity, mutant enzyme loses about 20% of the initial activity after 15 h at 65°C, compared to 10% loss of wild-type activity
Y206S
activity with carboxymethyl cellulose is 0.5% of wild-type activity, activity with phosphoric acid-swollen cellulose is 1.3% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 1.8% of wild-type activity
Y318A
activity with carboxymethyl cellulose is 5fold higher than wild-type activity, activity with phosphoric acid-swollen cellulose is 28% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 14.2% of wild-type activity, mutant enzyme loses about 30% of the initial activity after 15 h at 65°C, compared to 10% loss of wild-type activity
Y318F
activity with carboxymethyl cellulose is 6.7fold higher than wild-type activity, activity with phosphoric acid-swollen cellulose is 75% of wild-type activity, activity with bacterial microcrystalline cellulose from Acetobacter xylinum is 16.6% of wild-type activity
D117A
-
activity with carboxymethyl cellulose is 0.03% of wild-type activity, activity with phosphoric acid-swollen cellulose is 0.02% of wild-type activity
D261A/R378K
-
Cel9A mutant, causes weaker binding to alpha-chitin than wild-type, mutation of residue near the catalytic center. Mutant has weak chitinase activity, but no soluble products are detected
G234S
-
Cel6B mutant, causes weaker binding to alpha-chitin than wild-type, mutation of residue near the catalytic center
R78A
-
activity with phosphoric acid-swollen cellulose is less than 1.3% of the wild-type activity, activity with carboxymethylcellulose is less than 0.9% of the wild-type activity, activity with bacterial microcrystalline cellulose is less than 18.7% of the wild-type activity
R78K
-
activity with phosphoric acid-swollen cellulose is 54% of the wild-type activity, activity with carboxymethylcellulose is 15% of the wild-type activity, activity with bacterial microcrystalline cellulose is 52% of the activity with wild-type enzyme
W329C
-
Cel6B mutant, causes weaker binding to alpha-chitin than wild-type, mutation of residue near the catalytic center
W332A
-
Cel6B mutant, causes weaker binding to alpha-chitin than wild-type, mutation of residue near the catalytic center
Y206F
-
Cel9A mutant, causes weaker binding to alpha-chitin than wild-type, mutation of residue near the catalytic center
Y206S
-
Cel9A mutant, causes weaker binding to alpha-chitin than wild-type, mutation of residue near the catalytic center
Y73F
-
activity with carboxymethyl cellulose is 8.4% of wild-type activity, activity with phosphoric acid-swollen cellulose is 5.7% of wild-type activity
Y73S
-
activity with carboxymethyl cellulose is 0.022% of wild-type activity, activity with phosphoric acid-swollen cellulose is 0.088% of wild-type activity
additional information
additional information
the FnIII-like domain is deleted from Cel19A-90, reducing activity with bacterial microcrystalline cellulose to 43% of the wild-type
additional information
-
the FnIII-like domain is deleted from Cel19A-90, reducing activity with bacterial microcrystalline cellulose to 43% of the wild-type
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
15 h, wild-type enzyme and mutant enzymes Y206F, D58A and Y318A are stable, mutant enzyme D58N loses about 20% of its inital activity
60
15 h, wild-type enzyme is stable, mutant enzyme D58A loses about 20% of initial activity, mutant enzymes Y206F, D58N, D58N and Y318A lose about 10% of the inital activity
65
15 h, wild-type enzyme loses about 10% of initial activity, mutant enzyme D58N and Y206F loses about 20% of maximal activity, mutant enzyme D58A loses about 90% of initial activity, mutant enzyme Y318A loses about 30% of initial activity
70
wild-type enzyme loses about 50% of initial activity, mutant enzyme D58A loses about 20% of initial activity, mutant enymes D58A, Y206F and Y318A nearly completely lose activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
phenyl-Sepharose column, followed by a Q-Sepharose column, assessed by SDS-PAGE
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
12 mutant genes with changes in fice conserved residues of Cel9A-68 are constructed, cloned and expressed in Escherichia coli
Cel6A production in Escherichia coli and the DB-Cel6A fusions are inserted by particle bombardment method into the tobacco (Nicotiana tabacum cv. Samsun) chloroplast genome for protein expression
-
genes Tfu_1627, Tfu_1074, Tfu_2176, and Tfu_0901, encoding endo-1,4-beta-glucanases, expression analysis during stationary and exponential growth, overview
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
Wilson, D.B.
Cellulases of Thermomonospora fusca
Methods Enzymol.
160
314-323
1988
Thermobifida fusca
-
Andre, G.; Kanchanawong, P.; Palma, R.; Cho, H.; Deng, X.; Irwin, D.; Himmel, M.E.; Wilson, D.B.; Brady, J.W.
Computational and experimental studies of the catalytic mechanism of Thermobifida fusca cellulase Cel6A (E2)
Protein Eng.
16
125-134
2003
Thermobifida fusca
Zhou, W.; Irwin, D.C.; Escovar-Kousen, J.; Wilson, D.B.
Kinetic studies of Thermobifida fusca Cel9A active site mutant enzymes
Biochemistry
43
9655-9663
2004
Thermobifida fusca (P26221), Thermobifida fusca, Thermobifida fusca Cel9A (P26221), Thermobifida fusca Cel9A
Larsson, A.M.; Bergfors, T.; Dultz, E.; Irwin, D.C.; Roos, A.; Driguez, H.; Wilson, D.B.; Jones, T.A.
Crystal structure of Thermobifida fusca endoglucanase Cel6A in complex with substrate and inhibitor: the role of tyrosine Y73 in substrate ring distortion
Biochemistry
44
12915-12922
2005
Thermobifida fusca
Rudsander, U.J.; Sandstrom, C.; Piens, K.; Master, E.R.; Wilson, D.B.; Brumer Iii, H.; Kenne, L.; Teeri, T.T.
Comparative NMR analysis of cellooligosaccharide hydrolysis by GH9 bacterial and plant endo-1,4-beta-glucanases
Biochemistry
47
5235-5241
2008
Populus tremula x Populus tremuloides, Thermobifida fusca
Li, Y.; Wilson, D.B.
Chitin binding by Thermobifida fusca cellulase catalytic domains
Biotechnol. Bioeng.
100
644-652
2008
Thermobifida fusca
Gray, B.N.; Ahner, B.A.; Hanson, M.R.
High-level bacterial cellulase accumulation in chloroplast-transformed tobacco mediated by downstream box fusions
Biotechnol. Bioeng.
102
1045-1054
2009
Thermobifida fusca, Thermobifida fusca Cel6A
Deng, Y.; Fong, S.S.
Influence of culture aeration on the cellulase activity of Thermobifida fusca
Appl. Microbiol. Biotechnol.
85
965-974
2010
Thermobifida fusca
Batista, P.R.; Costa, M.G.; Pascutti, P.G.; Bisch, P.M.; de Souza, W.
High temperatures enhance cooperative motions between CBM and catalytic domains of a thermostable cellulase: mechanism insights from essential dynamics
Phys. Chem. Chem. Phys.
13
13709-13720
2011
Thermobifida fusca
EXTERNAL LINKS (specific for EC-Number 3.2.1.4)
Transporter Classification Database (TCDB): 4.D.3.1.6
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