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Information on EC 3.2.1.91 - cellulose 1,4-beta-cellobiosidase (non-reducing end) and Organism(s) Acetivibrio thermocellus and UniProt Accession A3DCH1
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3.2.1.91 cellulose 1,4-beta-cellobiosidase (non-reducing end)Specify your search results
Word Map
- 3.2.1.91
- trichoderma
- reesei
- chitinase
- cellulases
- glucans
- xylanase
- cellobiohydrolases
-
cellulolytic
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biocontrol
-
pathogenesis-related
- laminarin
-
cellulose-binding
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lignocellulosic
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saccharification
- chrysosporium
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cellulosic
-
microcrystalline
- pectinase
- beta-1,3-glucans
- cbhii
- beta-glucans
- mannanase
- cellulomonas
- cellotriose
- phanerochaete
- hypocrea
- succinogenes
- humicola
- harzianum
- cellotetraose
- galactanase
- thermocellum
- lichenan
-
mycoparasite
-
fibrobacter
-
thaumatin-like
- cellulosomal
- stover
- insolens
- biotechnology
- synthesis
- textile production
- paper production
- industry
- detergent
- degradation
- analysis
- biofuel production
The taxonomic range for the selected organisms is: Acetivibrio thermocellus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
glucanase, cbh i, cbh ii, cellobiohydrolase ii, celluclast 1.5, cellobiosidase, cellobiohydrolase 1, cel7d, avicelase ii, cbh9a, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,4-beta-cellobiohydrolase
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-
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1,4-beta-D-glucan cellobiohydrolase
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-
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1,4-beta-glucan cellobiohydrolase
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-
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1,4-beta-glucan cellobiosidase
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-
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avicelase
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-
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avicelase II
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-
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beta-1,4-glucan cellobiohydrolase
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-
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beta-1,4-glucan cellobiosylhydrolase
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-
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Beta-1,4-glycanase CEX
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-
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Beta-glucancellobiohydrolase
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-
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C1 cellulase
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-
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CBH 1
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-
-
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CBH II
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-
-
-
CbhA
CBHI
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-
-
-
CBHII
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-
-
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CBP120
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-
-
-
CBP95
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-
-
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Cel6A
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-
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cellobiohydrolase
cellobiohydrolase A
cellobiohydrolase I
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-
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cellobiohydrolase II
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-
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cellobiohydrolase, exo-
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cellobiosidase
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cellobiosidase, 1,4-beta-glucan
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cellulase, C1
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exo-beta-1,4-glucan cellobiohydrolase
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-
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exo-cellobiohydrolase
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-
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exocellobiohydrolase
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-
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exoglucanase
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-
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cellobiohydrolase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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-
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SYSTEMATIC NAME
IUBMB Comments
4-beta-D-glucan cellobiohydrolase (non-reducing end)
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CAS REGISTRY NUMBER
COMMENTARY
37329-65-0
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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
4-methylumbelliferyl-beta-D-oligoglucosides + H2O
?
-
enzyme preferentially cleaves the second or the fourth glycosidic bond, cleaves the second bond between putative sub-sites -2 and -1 or +1 and +2, cleaves the fourth bond between putative sub-sites -1 and +1
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-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
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-
-
-
?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
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-
-
?
4-nitrophenyl cellopentaoside + H2O
4-nitrophenol + cellobiose + D-glucose
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-
-
?
4-nitrophenyl cellotetraoside + H2O
cellobiose + 4-nitrophenyl cellobioside
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-
-
?
4-nitrophenyl cellotrioside + H2O
4-nitrophenol + cellobiose + D-glucose
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-
-
?
carboxymethylcellulose + H2O
glucose + cellobiose + cellutetraose
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-
-
-
?
cello-oligosaccharides + H2O
?
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natural and derivatized cello-oligosaccharides, H3PO4-swollen cellulose, Avicel, laminarin, lichenan, barley glucan
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-
?
cellulose + H2O
cellobiose + cellohexaose
hydrolyzes Avicel and filter paper, efficiency of hydrolysis increases in the following order: Gh9, Gh9-Fn31,2, Gh9-Fn31,2-CBDIII
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
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-
-
-
?
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ca2+
2.45 mol bound by one pair of immunoglobulin-like module and catalytic module in the wild-type enzyme, the metal content is similar in the mutant enzymes, overview
Ca2+
bound by all enzyme domains, except for the immunoglobulin-like module
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
thermodynamics and kinetics of the immunoglobulin-like module/catalytic module pair, wild-type and mutant enzymes, overview
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme is composed of an N-terminal carbohydrate-binding module of family 4 CBD4, an immunoglobulin-like module Ig, a catalytic module of glycoside hydrolase family 9 GH9, X1 1 and X1 2 modules, a carbohydrate-binding module of family 3 CBD3, and finally a C-terminal dockerin module, intramolecular interaction analysis, residues T230, D262, and D264 are important, analysis of doamin coupling, overview
additional information
-
the enzyme is composed of an N-terminal carbohydrate-binding module of family 4 CBD4, an immunoglobulin-like module Ig, a catalytic module of glycoside hydrolase family 9 GH9, X1 1 and X1 2 modules, a carbohydrate-binding module of family 3 CBD3, and finally a C-terminal dockerin module, intramolecular interaction analysis, residues T230, D262, and D264 are important, analysis of doamin coupling, overview
additional information
the enzyme is composed of an N-terminal carbohydrate-binding module of family 4, an immunoglobulin-like module, a catalytic module of glycoside hydrolase family 9, X1 1 and X1 2 modules, a carbohydrate-binding module of family 3 and finally a C-terminal dockerin module, elimination of the immunoglobulin-like module leads to complete inactivation of the catalytic module, intramolecular interaction analysis, residues T230, D262, and D264 are important, analysis of secondary and tertiary structure of the enzyme, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
microbatch and hanging drop vapour diffusion methods with 16.25% PEG 8000, 0.05 M sodium acetate pH 4.5, 0.12 M Li2SO4
sitting drop vapor diffusion method, using in 0.2 M ammonium iodide, 20% (w/v) polyethylene glycol 3350 pH 6.2 or 0.2 M CaCl2, 20% (w/v) polyethylene glycol 3350 pH 5.1
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D262A
site-directed mutagenesis, mutation of the the module interface residue affects the interaction of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
D264A
site-directed mutagenesis, mutation of the the module interface residue affects the interaction of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
T230A
site-directed mutagenesis, mutation of the module interface residue affects the final fold and stability of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
T230A/D262A
site-directed mutagenesis, mutation of the residues affects the interaction of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
W678G
the binding free energies between the substrate and the mutant are higher than those of the wild type enzyme. The pull forces and energy barrier in the mutant is also reduced significantly
Y555S
the binding free energies between the substrate and the mutant are higher than those of the wild type enzyme. The pull forces and energy barrier in the mutant is also reduced significantly
additional information
elimination of the enzyme's immunoglobulin-like module leads to its complete inactivation
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8.4
-
stable at 60°C for 5 h, stability decreases with incubation time above 5 h
654177
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
half-life of Gh9: 116 h, half-life of Gh9-Fn31,2: 97 h, half-life of Gh9-Fn31,2-CBDIII: 88.5 h
additional information
additional information
irreversible thermal unfolding kinetics of recombinant enzyme domains, overview
additional information
-
irreversible thermal unfolding kinetics of recombinant enzyme domains, overview
additional information
thermal unfolding kinetics of wild-type and mutant enzymes, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-IDA resin column chromatography and Superdex 75pg gel filtration
Ni-NTA column chromatography, Source 15S column chromatography, and Superdex 75 gel filtration
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recombinant His-tagged enzyme domain constructs from Escherichia coli strain BL21(DE3) to near homogeneity by nickel affinity chromatography and gel filtration
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) to near homogeneity by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli strain BL21(DE3) of the enzyme domain constructs: X1 2, X1 1/X1 2, CBD3, X1 1/X1 2-CBD3, Ig, GH9, Ig-GH9, Ig-GH9-X1 1/X1 2, and Ig-GH9-X1 1/X1 2-CBD3, overview
gene cbhA, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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 might influence substrate specificity by affecting the local structure of the CelK-specific N-terminal region containing an immunoglobulin-like domain
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Singh, R.N.; Akimenko, V.K.
Isolation of a cellobiohydrolase of Clostridium thermocellum capable of degrading natural crystalline substrates
Biochem. Biophys. Res. Commun.
192
1123-1130
1993
Acetivibrio thermocellus, Acetivibrio thermocellus CBH III
Bhat, S.; Owen, E.; Bhat, M.K.
Isolation and characterisation of a major cellobiohydrolase (S8) and a major endoglucanase (S11) subunit from the cellulosome of Clostridium thermocellum
Anaerobe
7
171-179
2001
Acetivibrio thermocellus
-
Kataeva, I.A.; Seidel, R.D., 3rd; Shah, A.; West, L.T.; Li, X.L.; Ljungdahl, L.G.
The fibronectin type 3-like repeat from the Clostridium thermocellum cellobiohydrolase CbhA promotes hydrolysis of cellulose by modifying its surface
Appl. Environ. Microbiol.
68
4292-4300
2002
Acetivibrio thermocellus (Q59325)
Kataeva, I.A.; Brewer, J.M.; Uversky, V.N.; Ljungdahl, L.G.
Domain coupling in a multimodular cellobiohydrolase CbhA from Clostridium thermocellum
FEBS Lett.
579
4367-4373
2005
Acetivibrio thermocellus (Q59325), Acetivibrio thermocellus, Acetivibrio thermocellus JW20 (Q59325)
Kataeva, I.A.; Uversky, V.N.; Brewer, J.M.; Schubot, F.; Rose, J.P.; Wang, B.C.; Ljungdahl, L.G.
Interactions between immunoglobulin-like and catalytic modules in Clostridium thermocellum cellulosomal cellobiohydrolase CbhA
Protein Eng. Des. Sel.
17
759-769
2004
Acetivibrio thermocellus (Q59325), Acetivibrio thermocellus JW20 (Q59325)
Jindou, S.; Petkun, S.; Shimon, L.; Bayer, E.A.; Lamed, R.; Frolow, F.
Crystallization and preliminary diffraction studies of CBM3b of cellobiohydrolase 9A from Clostridium thermocellum
Acta Crystallogr. Sect. F
F63
1044-1047
2007
Acetivibrio thermocellus (Q59325), Acetivibrio thermocellus
Brunecky, R.; Alahuhta, M.; Bomble, Y.J.; Xu, Q.; Baker, J.O.; Ding, S.Y.; Himmel, M.E.; Lunin, V.V.
Structure and function of the Clostridium thermocellum cellobiohydrolase A X1-module repeat: enhancement through stabilization of the CbhA complex
Acta Crystallogr. Sect. D
68
292-299
2012
Acetivibrio thermocellus
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 (A3DCH1), Acetivibrio thermocellus DSM 1237 (A3DCH1)
Han, F.; Liu, Y.; E, J.; Guan, S.; Han, W.; Shan, Y.; Wang, S.; Zhang, H.
Effects of Tyr555 and Trp678 on the processivity of cellobiohydrolase A from Ruminiclostridium thermocellum A simulation study
Biopolymers
109
e23238
2018
Acetivibrio thermocellus (Q59325), Acetivibrio thermocellus
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