Information on EC 3.2.1.91 - cellulose 1,4-beta-cellobiosidase (non-reducing end)

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.2.1.91
-
RECOMMENDED NAME
GeneOntology No.
cellulose 1,4-beta-cellobiosidase (non-reducing end)
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains
show the reaction diagram
-
-
-
-
Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains
show the reaction diagram
mechanism
-
Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains
show the reaction diagram
double-displacement mechanism, transition states, formation of an glycosyl-enzyme intermediate, structure-reactivity studies, the catalytic triad is formed by Glu212, Asp214, and Glu217, the glycosylation step is rate-limiting, overview
-
Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains
show the reaction diagram
progressivity and reaction mechanism of Cel7A
-
Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains
show the reaction diagram
substrate binding structure analysis of Cel7D
Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains
show the reaction diagram
exocellulase Cel6B acts by an inverting hydrolysis mechanism, that involves a proton-transferring network to carry out the catalytic base function
-
Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains
show the reaction diagram
progressivity and reaction mechanism of Cel7A
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
cellulose degradation II (fungi)
-
-
Starch and sucrose metabolism
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
4-beta-D-glucan cellobiohydrolase (non-reducing end)
-
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1,4-beta-cellobiohydrolase
-
-
-
-
1,4-beta-D-glucan cellobiohydrolase
-
-
-
-
1,4-beta-D-glucan cellobiohydrolase I
-
-
1,4-beta-D-glucan cellobiohydrolase I
Trichoderma pseudokoningii S-38
-
-
-
1,4-beta-D-glucan-cellobiohydrolase I
-
-
1,4-beta-D-glucan-cellobiohydrolase I
Trichoderma pseudokoningii S-38
-
-
-
1,4-beta-glucan cellobiohydrolase
-
-
-
-
1,4-beta-glucan cellobiosidase
-
-
-
-
avicelase
-
-
-
-
avicelase II
-
-
-
-
beta-1,4-glucan cellobiohydrolase
-
-
-
-
beta-1,4-glucan cellobiohydrolase
-
-
beta-1,4-glucan cellobiosylhydrolase
-
-
-
-
beta-1,4-glycanase
-
-
Beta-1,4-glycanase CEX
-
-
-
-
Beta-glucancellobiohydrolase
-
-
-
-
C1 cellulase
-
-
-
-
CBH
Fomitopsis pinicola KMJ812
-
-
-
CBH
Penicillium purpurogenum KJS506
-
-
-
CBH 1
-
-
-
-
CBH I
Trichoderma pseudokoningii S-38
-
-
-
CBH Ib
Chrysosporium lucknowense UV18-25
-
-
-
CBH II
-
-
-
-
CBH II
Trichoderma reesei ZU-02
-
-
-
CBH IIb
Chrysosporium lucknowense UV18-25
-
-
-
CBH1
Penicillium chrysogenum FS010
-
-
CBHI
-
-
-
-
CBHI
Penicillium occitanis CL100
-
-
CBHI
Trichoderma pseudokoningii S-38
-
-
-
CBHI
-
Cel7A
CBHII
-
-
-
-
CBHII
-
Cel6A
CBHII
M55080
-
CBHII
M55080
-
-
CBM3-GH5
recombinant enzyme domain construct
CBP120
-
-
-
-
CBP95
-
-
-
-
Cel48C
Paenibacillus sp. BP-23
-
-
-
Cel6A
-
-
-
-
Cel6A
Saccharophagus degradans 2-40T
-
-
-
Cel6B
Chrysosporium lucknowense UV18-25
-
-
-
Cel6C
Coprinopsis cinerea 5338
-
-
Cel7A
Acremonium thermophilum ALKO4245
-
-
Cel7A
Chaetomium thermophilum ALKO4265
-
-
Cel7A
Chrysosporium lucknowense UV18-25
-
-
-
Cel7A
Heterobasidion irregulare TC-32-1
-
-
Cel7A
Thermoascus aurantiacus ALKO4242
-
-
Cel7A
-
formerly CBH I
Cel7A
Trichoderma reesei ALKO 3413
-
-
-
Cel7A
-
formerly CBH I
-
Cel7A
-
formerly known as cellobiohydrolase I
Cel7B
Acremonium thermophilum ALKO4245
-
-
Cel9B
Paenibacillus sp. BP-23
-
-
-
CelA
Neocallimastix patriciarum J11
-
-
-
CelAB
displays cellobiohydrolase and beta-1,4(3) endoglucanase catalytic activities
CelAB
displays cellobiohydrolase and beta-1,4(3) endoglucanase catalytic activities
-
cellobiohydrolase
-
-
-
-
cellobiohydrolase
Acremonium thermophilum ALKO4245
-
-
cellobiohydrolase
-
-
cellobiohydrolase
-
cellobiohydrolase
-
cellobiohydrolase
Chaetomium thermophilum ALKO4265
-
-
cellobiohydrolase
-
-
cellobiohydrolase
Chrysosporium lucknowense UV18-25
-
-
-
cellobiohydrolase
-
-
cellobiohydrolase
Fomitopsis pinicola KMJ812
-
-
-
cellobiohydrolase
Heterobasidion irregulare TC-32-1
-
-
cellobiohydrolase
-
-
cellobiohydrolase
-
-
cellobiohydrolase
-
cellobiohydrolase
-
-
cellobiohydrolase
-
-
cellobiohydrolase
Neocallimastix patriciarum J11
-
-
-
cellobiohydrolase
-
-
cellobiohydrolase
Paenibacillus sp. BP-23
-
-
-
cellobiohydrolase
-
-
cellobiohydrolase
Penicillium purpurogenum KJS506
-
-
-
cellobiohydrolase
-
-
cellobiohydrolase
Piptoporus betulinus CCBAS585
-
-
-
cellobiohydrolase
-
-
cellobiohydrolase
-
-
cellobiohydrolase
Saccharophagus degradans 2-40T
-
-
-
cellobiohydrolase
-
cellobiohydrolase
-
-
cellobiohydrolase
-
cellobiohydrolase
Thermoascus aurantiacus ALKO4242
-
-
cellobiohydrolase
-
-
cellobiohydrolase
-
cellobiohydrolase
-
-
cellobiohydrolase
-
cellobiohydrolase
-
cellobiohydrolase
Trichoderma reesei ALKO 3413, Trichoderma reesei QM9414, Trichoderma reesei ZU-02
-
-
-
cellobiohydrolase
-
-
cellobiohydrolase 1
-
cellobiohydrolase 1
Penicillium chrysogenum FS010
-
-
cellobiohydrolase 1
-
-
cellobiohydrolase I
-
-
-
-
cellobiohydrolase I
-
-
cellobiohydrolase I
-
-
cellobiohydrolase I
-
-
cellobiohydrolase I
-
-
cellobiohydrolase I
-
-
cellobiohydrolase I
-
-
cellobiohydrolase I
-
-
cellobiohydrolase I
Irpex lacteus MC-2
-
-
-
cellobiohydrolase I
-
cellobiohydrolase I
Penicillium occitanis CL100
-
-
cellobiohydrolase I
-
-
cellobiohydrolase I
-
-
cellobiohydrolase I
-
-
cellobiohydrolase I
-
cellobiohydrolase I
-
-
cellobiohydrolase I
-
-
cellobiohydrolase I
Trichoderma pseudokoningii S-38
-
;
-
cellobiohydrolase I
-
-
cellobiohydrolase I
-
cellobiohydrolase I
-
-
cellobiohydrolase I
-
-
cellobiohydrolase I
-
-
cellobiohydrolase I-I
-
cellobiohydrolase I-II
-
cellobiohydrolase II
-
-
-
-
cellobiohydrolase II
-
-
cellobiohydrolase II
-
-
cellobiohydrolase II
Irpex lacteus MC-2
-
-
-
cellobiohydrolase II
M55080
-
cellobiohydrolase II
-
cellobiohydrolase II
M55080
-
-
cellobiohydrolase II
-
-
cellobiohydrolase II-I
-
cellobiohydrolase, exo-
-
-
-
-
cellobiosidase
-
-
-
-
cellobiosidase, 1,4-beta-glucan
-
-
-
-
Celluclast
-
commercial preparation
Celluclast 1.5
-
commercial preparation containing a broad spectrum of cellulolytic enzyme activities, most notably cellobiohydrolases and endo-1,4-alpha-glucanases
Cellulase
-
-
Cellulase
-
-
Cellulase
-
ambiguous
Cellulase
Trichoderma reesei RUT C30
-
ambiguous
-
cellulase, C1
-
-
-
-
CelO
Ruminiclostridium thermocellum F7
-
-
-
Ex-1
Irpex lacteus MC-2
-
-
-
Ex-4
Irpex lacteus MC-2
-
-
-
exo-1, 4-beta-D-glucanase
-
-
exo-1,4-beta-D-glucan cellobiohydrolase
-
-
exo-1,4-beta-D-glucan cellobiohydrolase
Neocallimastix patriciarum J11
-
-
-
exo-1,4-beta-D-glucanase
-
-
exo-1,4-beta-glucanase
-
-
exo-acting cellulase
-
-
exo-beta-1,4-glucan cellobiohydrolase
-
-
-
-
exo-beta-1,4-glucanase
-
exo-beta-1,4-glucanase
Penicillium occitanis CL100
-
-
exo-cellobiohydrolase
-
-
-
-
exo-cellobiohydrolase
-
-
exocellobiohydrolase
-
-
-
-
exocellulase
-
-
exocellulase E3
-
-
exoglucanase
-
-
-
-
exoglucanase
Trichoderma pseudokoningii S-38
-
-
-
OXG-RCBH
Geotrichum sp.
-
PSCase
M55080
-
PSCase
M55080
-
-
GH5
the GH5 domain is a cellobiohydrolase that lacks beta-glucosidase activity
additional information
-
the enzyme Cel7A probably belongs to the cellobiohydrolase family 7
additional information
-
the enzyme Cel7D belongs to the glycoside hydrolase family 7
additional information
the enzyme belongs to the glycosylhydrolase family GH6A
additional information
the enzyme belongs to the glycosylhydrolase family GH7A
CAS REGISTRY NUMBER
COMMENTARY
37329-65-0
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Acremonium thermophilum ALKO4245
-
UniProt
Manually annotated by BRENDA team
Allescheria terrestris
-
-
-
Manually annotated by BRENDA team
CBH I, CBH II
-
-
Manually annotated by BRENDA team
synonym Aspergillus nidulans
-
-
Manually annotated by BRENDA team
strains StA, StB, StC, StD, StE, and StF
-
-
Manually annotated by BRENDA team
Bacillus subtilis 168
168
-
-
Manually annotated by BRENDA team
gene cloned in Escherichia coli
-
-
Manually annotated by BRENDA team
gene cloned in Saccharomyces cerevisiae
-
-
Manually annotated by BRENDA team
Chaetomium thermophile
-
-
-
Manually annotated by BRENDA team
Chaetomium thermophilum ALKO4265
-
UniProt
Manually annotated by BRENDA team
gene cbh1, wild-type and mutant industrial strain, full-length and mutant enzyme forms
-
-
Manually annotated by BRENDA team
strain UV18-25
-
-
Manually annotated by BRENDA team
Chrysosporium lucknowense UV18-25
strain UV18-25
-
-
Manually annotated by BRENDA team
Clostridium stercorarium
-
-
-
Manually annotated by BRENDA team
strain 5338
UniProt
Manually annotated by BRENDA team
Coprinopsis cinerea 5338
strain 5338
UniProt
Manually annotated by BRENDA team
Fomitopsis pinicola KMJ812
-
-
-
Manually annotated by BRENDA team
2 forms: I/II
-
-
Manually annotated by BRENDA team
Geotrichum sp.
-
-
-
Manually annotated by BRENDA team
Geotrichum sp.
strain M128
SwissProt
Manually annotated by BRENDA team
sandfly, Phlebotomus papatasi, infected
-
-
Manually annotated by BRENDA team
Heterobasidion irregulare TC-32-1
-
UniProt
Manually annotated by BRENDA team
white rot fungus, strain MC-2, gene cel2, exo-type cellobiohydrolase Ex-1
-
-
Manually annotated by BRENDA team
Irpex lacteus MC-2
-
-
-
Manually annotated by BRENDA team
sandfly, Phlebotomus papatasi, infected
-
-
Manually annotated by BRENDA team
sandfly, Phlebotomus papatasi, infected
-
-
Manually annotated by BRENDA team
sandfly, Phlebotomus papatasi, infected
-
-
Manually annotated by BRENDA team
sandfly, Phlebotomus papatasi, infected
-
-
Manually annotated by BRENDA team
Neocallimastix patriciarum J11
-
-
-
Manually annotated by BRENDA team
strain BP-23
SwissProt
Manually annotated by BRENDA team
strain BP-23
-
-
Manually annotated by BRENDA team
Paenibacillus sp. BP-23
strain BP-23
SwissProt
Manually annotated by BRENDA team
Paenibacillus sp. BP-23
strain BP-23
-
-
Manually annotated by BRENDA team
strain FS010
UniProt
Manually annotated by BRENDA team
Penicillium chrysogenum FS010
strain FS010
UniProt
Manually annotated by BRENDA team
Penicillium occitanis CL100
-
UniProt
Manually annotated by BRENDA team
2 forms: I/II
-
-
Manually annotated by BRENDA team
Penicillium purpurogenum KJS506
-
-
-
Manually annotated by BRENDA team
i.e. Sporotrichum pruinosum, strain ME446, gene cbhl.2
SwissProt
Manually annotated by BRENDA team
White Rot fungus, Cel7D is the major cellulase
Uniprot
Manually annotated by BRENDA team
Phanerochaete chrysosporium CBH I
CBH I
-
-
Manually annotated by BRENDA team
Phytomonas davidi
sandfly, Phlebotomus papatasi, infected
-
-
Manually annotated by BRENDA team
strain CCBAS585
-
-
Manually annotated by BRENDA team
Piptoporus betulinus CCBAS585
strain CCBAS585
-
-
Manually annotated by BRENDA team
strain JW20, gene cbhA
SwissProt
Manually annotated by BRENDA team
Ruminiclostridium thermocellum CBH III
CBH III
-
-
Manually annotated by BRENDA team
Ruminiclostridium thermocellum F7
strain F7
-
-
Manually annotated by BRENDA team
strain JW20, gene cbhA
SwissProt
Manually annotated by BRENDA team
strain 2-40T
-
-
Manually annotated by BRENDA team
Saccharophagus degradans 2-40T
strain 2-40T
-
-
Manually annotated by BRENDA team
2 forms: I/II
-
-
Manually annotated by BRENDA team
bifunctional beta 1,4-endoglucanase/cellobiohydrolase; strain T7902
UniProt
Manually annotated by BRENDA team
bifunctional beta 1,4-endoglucanase/cellobiohydrolase; strain T7902
UniProt
Manually annotated by BRENDA team
Thermoascus aurantiacus ALKO4242
-
UniProt
Manually annotated by BRENDA team
strain FjSS3-B.1
-
-
Manually annotated by BRENDA team
strain FjSS3-B.1
-
-
Manually annotated by BRENDA team
Torula thermophila
-
-
-
Manually annotated by BRENDA team
Trichoderma pseudokoningii S-38
-
-
-
Manually annotated by BRENDA team
Trichoderma pseudokoningii S-38
strain S-38
-
-
Manually annotated by BRENDA team
anamorph: Trichoderma reesei
-
-
Manually annotated by BRENDA team
CBH I, CBH II
-
-
Manually annotated by BRENDA team
CBH I, CBH II; CBH I is exo-glucanase, CHB II is endo-glucanase
-
-
Manually annotated by BRENDA team
engineered enzymes
-
-
Manually annotated by BRENDA team
formerly Trichoderma reesei
-
-
Manually annotated by BRENDA team
formerly Trichoderma reesei
UniProt
Manually annotated by BRENDA team
gene cbh2
-
-
Manually annotated by BRENDA team
gene cbh2
M55080
UniProt
Manually annotated by BRENDA team
i.e. Hypocrea jecorina
-
-
Manually annotated by BRENDA team
strain ALKO2877
-
-
Manually annotated by BRENDA team
strain QM9414
-
-
Manually annotated by BRENDA team
strain RUT C30
-
-
Manually annotated by BRENDA team
Trichoderma reesei ALKO 3413
-
-
-
Manually annotated by BRENDA team
Trichoderma reesei ALKO2877
strain ALKO2877
-
-
Manually annotated by BRENDA team
Trichoderma reesei CBH I
CBH I
-
-
Manually annotated by BRENDA team
Trichoderma reesei Cel6A
Cel6A
-
-
Manually annotated by BRENDA team
gene cbh2
M55080
UniProt
Manually annotated by BRENDA team
strain QM9414
-
-
Manually annotated by BRENDA team
Trichoderma reesei RUT C30
strain RUT C30
-
-
Manually annotated by BRENDA team
Trichoderma reesei ZU-02
gene cbh2
-
-
Manually annotated by BRENDA team
Exo I /II/III
-
-
Manually annotated by BRENDA team
sandfly, Phlebotomus papatasi, infected
-
-
Manually annotated by BRENDA team
cellobiohydrolase I-I
UniProt
Manually annotated by BRENDA team
cellobiohydrolase I-II
UniProt
Manually annotated by BRENDA team
cellobiohydrolase II-I
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
the cellobiohydrolase Cel7A is the major component of total extract produced by Trichoderma and is the key enzyme for efficient degradation of crystalline cellulose
metabolism
-
Trichoderma harzianum secretes an effective and well-balanced enzymatic system that is able to completely hydrolyze cellulosic substrates into monomeric glucose
physiological function
-
CBH II component has higher specific activity than CBH I and is an important component in cellulase
physiological function
Trichoderma reesei ZU-02
-
CBH II component has higher specific activity than CBH I and is an important component in cellulase
-
metabolism
-
Trichoderma harzianum secretes an effective and well-balanced enzymatic system that is able to completely hydrolyze cellulosic substrates into monomeric glucose
-
additional information
-
the enzyme from overexpressing line C10 performs better than the wild-type from ZU-02 in enzymatic hydrolysis because the exoexo-synergism plays a role, overview
additional information
-
tertiary structure analysis at different pH values, small-angle X-ray scattering, overview
additional information
-
cellobiohydrolase I has a shortened loop at the entrance of the cellulose-binding tunnel, the flexibility of Tyr260 is enhanced as a result of the short side-chains of adjacent Val216 and Ala384 residues and creates an additional gap at the side face of the catalytic tunnel. A larger flexibility in this region might facilitate the entry of the substrate into the tight binding tunnel of the enzyme. Structure analysis and molecular dynamics simulations, overview
additional information
-
cellobiohydrolase I has a shortened loop at the entrance of the cellulose-binding tunnel, the flexibility of Tyr260 is enhanced as a result of the short side-chains of adjacent Val216 and Ala384 residues and creates an additional gap at the side face of the catalytic tunnel. A larger flexibility in this region might facilitate the entry of the substrate into the tight binding tunnel of the enzyme. Structure analysis and molecular dynamics simulations, overview
-
additional information
Trichoderma reesei ZU-02
-
the enzyme from overexpressing line C10 performs better than the wild-type from ZU-02 in enzymatic hydrolysis because the exoexo-synergism plays a role, overview
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2,4-dinitrophenyl beta-cellobioside + H2O
2,4-dinitrophenol + beta-cellobiose
show the reaction diagram
-
-
-
?
2,4-dinitrophenyl beta-glucopyranoside + H2O
2,4-dinitrophenol + beta-D-glucose
show the reaction diagram
-
-
-
?
2,4-dinitrophenyl beta-lactoside + H2O
2,4-dinitrophenol + beta-lactose
show the reaction diagram
-
-
-
?
2,4-dinitrophenyl cellobiose + H2O
2,4-dinitrophenol + cellobiose
show the reaction diagram
-
-
-
?
2-chloro-4-nitrophenyl beta-cellobioside + H2O
2-chloro-4-nitrophenol + beta-cellobiose
show the reaction diagram
-
-
-
?
2-chloro-4-nitrophenyl beta-D-lactoside + H2O
2-chloro-4-nitrophenol + lactose
show the reaction diagram
-
-
-
?
2-chloro-4-nitrophenyl beta-lactoside + H2O
2-chloro-4-nitrophenol + beta-lactose
show the reaction diagram
-
-
-
?
2-chloro-4-nitrophenyl lactoside + H2O
2-chloro-4-nitrophenol + ?
show the reaction diagram
-
-
-
?
2-chloro-4-nitrophenyl-beta-D-cellotrioside + H2O
4-nitrophenol + ?
show the reaction diagram
-
-
-
?
2-chloro-4-nitrophenyl-beta-D-lactoside
2-chloro-4-nitrophenol + beta-D-lactose
show the reaction diagram
-
-
-
-
2-chloro-4-nitrophenyl-beta-D-lactoside
2-chloro-4-nitrophenol + beta-D-lactose
show the reaction diagram
-
-
-
2-chloro-4-nitrophenyl-beta-D-lactoside
2-chloro-4-nitrophenol + beta-D-lactose
show the reaction diagram
-
-
-
2-chloro-4-nitrophenyl-beta-D-lactoside
2-chloro-4-nitrophenol + beta-D-lactose
show the reaction diagram
Chaetomium thermophilum, Chaetomium thermophilum ALKO4265
-
-
-
2-chloro-4-nitrophenyl-beta-D-lactoside
2-chloro-4-nitrophenol + beta-D-lactose
show the reaction diagram
Acremonium thermophilum ALKO4245
-
-
-
2-chloro-4-nitrophenyl-beta-D-lactoside
2-chloro-4-nitrophenol + beta-D-lactose
show the reaction diagram
Thermoascus aurantiacus ALKO4242
-
-
-
2-chloro-4-nitrophenyl-beta-D-lactoside + H2O
2-chloro-4-nitrophenol + D-lactose
show the reaction diagram
-
-
-
?
2-chloro-4-nitrophenyl-beta-lactoside
?
show the reaction diagram
Trichoderma reesei, Trichoderma reesei CBH I
-
-
-
-
?
2-chloro-4-nitrophenyl-beta-lactoside + H2O
4-nitrophenol + 2-chloro-beta-lactose
show the reaction diagram
-
-
-
?
2-chloro-4-nitrophenyl-beta-lactoside + H2O
4-nitrophenol + 2-chloro-beta-lactose
show the reaction diagram
-
-
?
2-chloronitrophenyl-beta-cellotrioside + H2O
?
show the reaction diagram
-
-
-
-
?
2-chloronitrophenyl-beta-D-lactoside + H2O
?
show the reaction diagram
-
-
-
-
?
3,4-dinitrophenyl lactoside + H2O
3,4-dinitrophenol + ?
show the reaction diagram
-
-
-
?
4-bromophenyl beta-cellobioside + H2O
4-bromophenol + beta-cellobiose
show the reaction diagram
-
-
-
?
4-bromophenyl beta-glucopyranoside + H2O
4-bromophenol + beta-D-glucose
show the reaction diagram
-
-
-
?
4-bromophenyl beta-lactoside + H2O
4-bromophenol + beta-lactose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl beta-cellobioside + H2O
4-methylumbelliferol + cellobiose
show the reaction diagram
-
substrate binding analysis of wild-type enzyme and mutant D274A, mutant D274A binds 4-methylumbelliferyl beta-cellobioside to approximately the same extent as the wild-type, overview
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
?
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
?
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
4-methylumbelliferol + beta-D-cellobiose
show the reaction diagram
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
4-methylumbelliferol + beta-D-cellobiose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
4-methylumbelliferone + beta-D-cellobioside
show the reaction diagram
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
4-methylumbelliferone + cellobiose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
4-methylumbelliferone + cellobiose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
4-methylumbelliferone + cellobiose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
4-methylumbelliferone + cellobiose
show the reaction diagram
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
4-methylumbelliferone + cellobiose
show the reaction diagram
Trichoderma reesei ALKO 3413
-
-
-
?
4-methylumbelliferyl beta-D-lactopyranoside + H2O
4-methylumbelliferone + lactose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl beta-D-lactopyranoside + H2O
4-methylumbelliferone + lactose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl beta-D-lactopyranoside + H2O
4-methylumbelliferone + lactose
show the reaction diagram
Heterobasidion irregulare, Heterobasidion irregulare TC-32-1
-
-
?
4-methylumbelliferyl beta-D-lactopyranoside + H2O
4-methylumbelliferone + lactose
show the reaction diagram
Trichoderma reesei ALKO 3413
-
-
-
?
4-methylumbelliferyl beta-D-lactopyranoside + H2O
4-methylumbelliferone lactose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl beta-D-lactoside + H2O
4-methylumbelliferol + beta-D-lactose
show the reaction diagram
-
-
?
4-methylumbelliferyl beta-D-lactoside + H2O
4-methylumbelliferol + beta-D-lactose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl beta-lactoside + H2O
4-methylumbelliferol + beta-lactose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl beta-lactoside + H2O
4-methylumbelliferone + lactose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl lactoside + H2O
4-methylumbelliferone + lactose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-beta-D-cellobioside + H2O
?
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-cellobioside + H2O
?
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-cellobioside + H2O
4-methylumbelliferol + cellobiose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-beta-D-cellohexaoside + H2O
?
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-cellopentaoside + H2O
?
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-cellotetraoside + H2O
?
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-cellotrioside + H2O
?
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-cellotrioside + H2O
?
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
?
show the reaction diagram
Trichoderma reesei, Trichoderma reesei ALKO2877
-
-
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferol + beta-D-lactose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferol + beta-D-lactose
show the reaction diagram
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferol + beta-D-lactose
show the reaction diagram
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferol + beta-D-lactose
show the reaction diagram
Chaetomium thermophilum, Chaetomium thermophilum ALKO4265
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferol + beta-D-lactose
show the reaction diagram
Acremonium thermophilum ALKO4245
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferol + beta-D-lactose
show the reaction diagram
Thermoascus aurantiacus ALKO4242
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferol + D-lactose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferone + lactose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-beta-D-oligoglucosides + H2O
?
show the reaction diagram
-
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
-
-
?
4-nitrophenyl beta-cellobioside + H2O
4-nitrophenol + beta-cellobiose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-cellobioside + H2O
4-nitrophenol + beta-cellobiose
show the reaction diagram
-
-
?
4-nitrophenyl beta-cellobioside + H2O
4-nitrophenol + beta-cellobiose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + beta-D-cellobiose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + beta-D-cellobiose
show the reaction diagram
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + beta-D-cellobiose
show the reaction diagram
-
substrate of wild-type enzyme and recombinant Cex-RsaA fusion mutant
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + beta-D-cellobiose
show the reaction diagram
-
binding of 4-nitrophenyl beta-D-cellobioside to CBHI is an irreversible process, in which heat is released, but where there is no reversible equilibrium between 4-nitrophenyl beta-D-cellobioside-CBHI and CBHI and 4-nitrophenyl beta-D-cellobioside. The energy, which powers the configurational change of 4-nitrophenyl beta-D-cellobioside as it is converted, is generated from cyclic changes in the conformation of CBHI during the binding/de-sorption process
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + beta-D-cellobiose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + beta-D-cellobiose
show the reaction diagram
Penicillium chrysogenum FS010
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + beta-D-cellobiose
show the reaction diagram
Trichoderma pseudokoningii S-38
-
binding of 4-nitrophenyl beta-D-cellobioside to CBHI is an irreversible process, in which heat is released, but where there is no reversible equilibrium between 4-nitrophenyl beta-D-cellobioside-CBHI and CBHI and 4-nitrophenyl beta-D-cellobioside. The energy, which powers the configurational change of 4-nitrophenyl beta-D-cellobioside as it is converted, is generated from cyclic changes in the conformation of CBHI during the binding/de-sorption process
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
show the reaction diagram
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
show the reaction diagram
very low activity
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
show the reaction diagram
-
best substrate
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
show the reaction diagram
-
100% activity, highly preferred substrate
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
show the reaction diagram
Penicillium purpurogenum KJS506
-
best substrate
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
show the reaction diagram
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
show the reaction diagram
Chrysosporium lucknowense UV18-25
-
-
-
?
4-nitrophenyl beta-D-cellopentaoside + H2O
4-nitrophenol + beta-D-cellopentaose
show the reaction diagram
best substrate
-
?
4-nitrophenyl beta-D-cellopentaoside + H2O
?
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-cellotetraoside + H2O
?
show the reaction diagram
Ruminiclostridium thermocellum, Ruminiclostridium thermocellum F7
-
enzyme activity starts from the reducing end in a processive mode after making random cuts
-
-
?
4-nitrophenyl beta-D-cellotrioside + H2O
4-nitrophenol + cellobiose
show the reaction diagram
-
-
?
4-nitrophenyl beta-D-cellotrioside + H2O
?
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + D-galactopyranose
show the reaction diagram
-
0.26% activity compared to 4-nitrophenyl beta-D-cellobioside
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
show the reaction diagram
-
0.11% activity compared to 4-nitrophenyl beta-D-cellobioside
-
?
4-nitrophenyl beta-D-lactopyranoside + H2O
4-nitrophenol + D-lactose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-D-lactoside + H2O
4-nitrophenol + lactose
show the reaction diagram
-
42.1% activity compared to 4-nitrophenyl beta-D-cellobioside
-
?
4-nitrophenyl beta-D-mannopyranoside + H2O
4-nitrophenol + D-mannopyranose
show the reaction diagram
-
0.64% activity compared to 4-nitrophenyl beta-D-cellobioside
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylopyranose
show the reaction diagram
-
0.64% activity compared to 4-nitrophenyl beta-D-cellobioside
-
?
4-nitrophenyl beta-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-lactoside + H2O
4-nitrophenol + ?
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-lactoside + H2O
4-nitrophenol + beta-lactose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-lactoside + H2O
4-nitrophenol + beta-lactose
show the reaction diagram
-
-
-
?
4-nitrophenyl beta-lactoside + H2O
4-nitrophenol + beta-lactose
show the reaction diagram
-
-
?
4-nitrophenyl beta-lactoside + H2O
4-nitrophenol + beta-lactose
show the reaction diagram
-
-
-
?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
show the reaction diagram
-
-
?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
show the reaction diagram
-
-
-
?
4-nitrophenyl cellopentaoside + H2O
4-nitrophenol + cellobiose + D-glucose
show the reaction diagram
-
-
?
4-nitrophenyl cellopentaoside + H2O
4-nitrophenyl-cellobioside + cellotriose
show the reaction diagram
Paenibacillus sp., Paenibacillus sp. BP-23
-
-
?
4-nitrophenyl cellotetraoside + H2O
4-nitrophenol + cellobiose
show the reaction diagram
-
-
?
4-nitrophenyl cellotetraoside + H2O
4-nitrophenyl cellobioside + cellobiose
show the reaction diagram
Paenibacillus sp., Paenibacillus sp. BP-23
-
-
?
4-nitrophenyl cellotrioside + H2O
4-nitrophenol + cellobiose + D-glucose
show the reaction diagram
-
-
?
4-nitrophenyl D-cellobioside + H2O
4-nitrophenol + D-cellobiose
show the reaction diagram
-
-
-
?
4-nitrophenyl D-cellobioside + H2O
4-nitrophenol + D-cellobiose
show the reaction diagram
-
-
?
4-nitrophenyl-beta-D-cellobiose + H2O
4-nitrophenol + D-cellobiose
show the reaction diagram
-
-
-
?
4-nitrophenyl-beta-D-cellobioside + H2O
4-nitrophenol + ?
show the reaction diagram
-
-
-
?
4-nitrophenyl-beta-D-cellobioside + H2O
4-nitrophenol + beta-D-cellobiose
show the reaction diagram
-
-
-
?
4-nitrophenyl-beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
-
-
-
?
4-nitrophenyl-beta-D-lactoside + H2O
4-nitrophenol + ?
show the reaction diagram
-
-
-
?
alpha-cellobiosyl fluoride + H2O
fluoride + cellobiose
show the reaction diagram
-
-
-
?
amorphous cellulose + H2O
?
show the reaction diagram
-
-
-
-
?
avicel + H2O
?
show the reaction diagram
-
-
-
-
?
avicel + H2O
?
show the reaction diagram
-
-
-
-
?
avicel + H2O
?
show the reaction diagram
-
-
-
-
?
avicel + H2O
?
show the reaction diagram
-
-
-
-
?
avicel + H2O
?
show the reaction diagram
-
-
-
-
?
avicel + H2O
?
show the reaction diagram
-
-
-
-
?
avicel + H2O
?
show the reaction diagram
-
-
-
-
?
avicel + H2O
?
show the reaction diagram
-
-
-
-
?
avicel + H2O
?
show the reaction diagram
-
-
-
-
?
avicel + H2O
?
show the reaction diagram
-
-
-
-
?
avicel + H2O
?
show the reaction diagram
-
-
-
?
avicel + H2O
?
show the reaction diagram
-
-
-
-
?
avicel + H2O
?
show the reaction diagram
-
-
-
?
avicel + H2O
?
show the reaction diagram
-
shows a synergistic effect in the degradation of avicel when the enzyme acts together with either cellobiohydrolase I (Ex-1) or endoglucanase (En-1) produced by Irpex lacteus MC-2
-
-
?
avicel + H2O
?
show the reaction diagram
-
microcrystalline cellulose
-
-
?
avicel + H2O
?
show the reaction diagram
-
microcrystalline cellulose
-
-
?
avicel + H2O
?
show the reaction diagram
-
26.9% activity compared to 4-nitrophenyl beta-D-cellobioside
-
-
?
avicel + H2O
?
show the reaction diagram
Penicillium purpurogenum KJS506
-
-
-
-
?
avicel + H2O
?
show the reaction diagram
Irpex lacteus MC-2
-
shows a synergistic effect in the degradation of avicel when the enzyme acts together with either cellobiohydrolase I (Ex-1) or endoglucanase (En-1) produced by Irpex lacteus MC-2
-
-
?
avicel + H2O
cellobiose
show the reaction diagram
-
-
-
?
avicel + H2O
cellobiose
show the reaction diagram
-
-
-
?
avicel + H2O
cellobiose
show the reaction diagram
-
-
-
?
avicel + H2O
cellobiose
show the reaction diagram
-
-
-
?
avicel + H2O
cellobiose
show the reaction diagram
Clostridium stercorarium
-
-
-
?
avicel + H2O
cellobiose
show the reaction diagram
-
-
-
?
avicel + H2O
cellobiose
show the reaction diagram
-
-
-
?
avicel + H2O
cellobiose
show the reaction diagram
-
-
-
?
avicel + H2O
cellobiose
show the reaction diagram
-
-
-
?
avicel + H2O
cellobiose
show the reaction diagram
-
-
-
?
avicel + H2O
cellobiose
show the reaction diagram
-
-
?
avicel + H2O
cellobiose
show the reaction diagram
-
-
plus traces of cellotriose
?
avicel + H2O
cellobiose
show the reaction diagram
-
low specific activity
-
?
avicel + H2O
cellobiose
show the reaction diagram
-
191% activity compared to cellulose
-
?
avicel + H2O
cellobiose
show the reaction diagram
Coprinopsis cinerea 5338
-
-
?
avicel + H2O
cellobiose
show the reaction diagram
Ruminiclostridium thermocellum CBH III
-
-
-
?
avicel + H2O
cellobiose
show the reaction diagram
Neocallimastix patriciarum J11
-
low specific activity
-
?
avicel + H2O
cellobiose + ?
show the reaction diagram
-
-
-
?
avicel + H2O
cellobiose + ?
show the reaction diagram
-
-
-
?
avicel + H2O
cellobiose + ?
show the reaction diagram
-
-
-
?
avicel + H2O
cellobiose + ?
show the reaction diagram
-
-
-
?
avicel + H2O
cellobiose + ?
show the reaction diagram
-
-
-
?
avicel + H2O
cellobiose + ?
show the reaction diagram
-
-
-
?
avicel + H2O
cellobiose + ?
show the reaction diagram
-
-
?
avicel + H2O
cellobiose + ?
show the reaction diagram
-
-
-
?
avicel + H2O
cellobiose + ?
show the reaction diagram
-
-
-
?
avicel + H2O
cellobiose + ?
show the reaction diagram
-
-
?
avicel + H2O
cellobiose + ?
show the reaction diagram
-
-
?
avicel + H2O
cellobiose + ?
show the reaction diagram
Chrysosporium lucknowense UV18-25
-
-
-
?
avicel + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
-
-
?
avicel + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
absorption to avicel at 4C is 84%
-
?
avicel + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
absorption to avicel at 4C is 87.5%
-
?
avicel + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
-
absorption to avicel at 4C is 95.5%
-
?
avicel + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
Chaetomium thermophilum ALKO4265
absorption to avicel at 4C is 84%
-
?
avicel + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
Acremonium thermophilum ALKO4245
absorption to avicel at 4C is 87.5%
-
?
avicel + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
Thermoascus aurantiacus ALKO4242
-
-
?
Avicel PH-101 + H2O
?
show the reaction diagram
M55080
-
-
-
?
Avicel PH-101 + H2O
?
show the reaction diagram
-
-
-
?
Avicel PH-101 + H2O
?
show the reaction diagram
M55080
-
-
-
?
bacterial microcrystalline cellulose + H2O
?
show the reaction diagram
-
-
-
-
?
bacterial microcrystalline cellulose + H2O
?
show the reaction diagram
-
best substrate
-
-
?
bacterial microcrystalline cellulose + H2O
?
show the reaction diagram
best substrate
-
-
?
barley beta-glucan + H2O
?
show the reaction diagram
Neocallimastix patriciarum, Neocallimastix patriciarum J11
-
highest specific activity
-
-
?
barley straw + H2O
?
show the reaction diagram
-
-
-
-
?
beta-cellobiosyl fluoride + H2O
fluoride + cellobiose
show the reaction diagram
-
-
-
?
beta-glucan + H2O
?
show the reaction diagram
-
from barley
-
-
?
beta-glucan + H2O
?
show the reaction diagram
-
227% activity compared to cellulose
-
-
?
beta-glucan + H2O
?
show the reaction diagram
Ruminiclostridium thermocellum F7
-
from barley
-
-
?
carboxymethyl cellulose + H2O
?
show the reaction diagram
-
-
-
-
?
carboxymethyl cellulose + H2O
?
show the reaction diagram
-
-
-
-
?
carboxymethyl cellulose + H2O
?
show the reaction diagram
-
-
-
?
carboxymethyl cellulose + H2O
?
show the reaction diagram
-
-
-
-
?
carboxymethyl cellulose + H2O
?
show the reaction diagram
-
-
-
?
carboxymethyl cellulose + H2O
?
show the reaction diagram
-
worst substrate
-
-
?
carboxymethyl cellulose + H2O
?
show the reaction diagram
-
low specific activity
-
-
?
carboxymethyl cellulose + H2O
?
show the reaction diagram
Ruminiclostridium thermocellum F7
-
-
-
-
?
carboxymethyl cellulose + H2O
?
show the reaction diagram
Irpex lacteus MC-2
-
-
-
-
?
carboxymethyl cellulose + H2O
?
show the reaction diagram
worst substrate
-
-
?
carboxymethyl cellulose + H2O
?
show the reaction diagram
Neocallimastix patriciarum J11
-
low specific activity
-
-
?
carboxymethylcellulose + H2O
?
show the reaction diagram
Fomitopsis pinicola, Fomitopsis pinicola KMJ812
-
0.26% activity compared to 4-nitrophenyl beta-D-cellobioside
-
-
?
carboxymethylcellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
carboxymethylcellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
carboxymethylcellulose + H2O
cellobiose
show the reaction diagram
Clostridium stercorarium
-
-
-
?
carboxymethylcellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
carboxymethylcellulose + H2O
cellobiose
show the reaction diagram
-
-
CBH I, exo-glucanase
?
carboxymethylcellulose + H2O
cellobiose
show the reaction diagram
-
little activity
-
-
carboxymethylcellulose + H2O
cellobiose
show the reaction diagram
-
not significantly
-
-
carboxymethylcellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
carboxymethylcellulose + H2O
glucose + cellobiose + cellutetraose
show the reaction diagram
-
-
-
?
carboxymethylcellulose + H2O
glucose + cellobiose + cellutetraose
show the reaction diagram
-
-
-
?
carboxymethylcellulose + H2O
glucose + cellobiose + cellutetraose
show the reaction diagram
-
-
-
?
carboxymethylcellulose + H2O
glucose + cellobiose + cellutetraose
show the reaction diagram
-
-
CBH II, endo-glucanase
?
carboxymethylcellulose + H2O
glucose + cellobiose + cellutetraose
show the reaction diagram
Ruminiclostridium thermocellum CBH III
-
-
-
?
carboxymethylcellulose + H2O
cellobiose + ?
show the reaction diagram
-
-
-
?
carboxymethylcellulose + H2O
cellobiose + ?
show the reaction diagram
-
-
-
?
cello-oligosaccharides + H2O
?
show the reaction diagram
-
natural and derivatized cello-oligosaccharides, H3PO4-swollen cellulose, Avicel, laminarin, lichenan, barley glucan
-
-
?
cellobiose + H2O
?
show the reaction diagram
-
-
-
?
cellobiose + H2O
?
show the reaction diagram
-
0.11% activity compared to 4-nitrophenyl beta-D-cellobioside
-
-
?
cellodextrin + H2O
?
show the reaction diagram
-
-
-
-
?
cellodextrin + H2O
?
show the reaction diagram
-
-
-
?
cellodextrin + H2O
?
show the reaction diagram
Ruminiclostridium thermocellum F7
-
-
-
-
?
cellodextrin + H2O
?
show the reaction diagram
Paenibacillus sp. BP-23
-
-
-
?
cellodextrins + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
-
?
cellohexaose + H2O
cellotriose + cellobiose + cellotetraose
show the reaction diagram
-
-
-
?
cellohexaose + H2O
cellotriose + cellobiose + cellotetraose
show the reaction diagram
-
-
-
?
cellohexaose + H2O
cellotriose + cellobiose + cellotetraose
show the reaction diagram
-
-
-
?
cellohexaose + H2O
?
show the reaction diagram
-
-
-
-
?
cellohexaose + H2O
cellobiose
show the reaction diagram
-
-
-
?
celloligosaccharides + H2O
cellobiose + H2O
show the reaction diagram
-
-
-
?
cellononaose + H2O
?
show the reaction diagram
-
-
-
?
cellopentaose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
-
?
cellopentaose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
-
?
cellopentaose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
-
?
cellopentaose + H2O
?
show the reaction diagram
-
-
-
-
?
cellopentaose + H2O
cellobiose + cellotriose
show the reaction diagram
-
good substrate
-
?
cellopentaose + H2O
cellobiose + D-glucose
show the reaction diagram
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
show the reaction diagram
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
show the reaction diagram
-
cellobiose is preferentialls released from the nonreducing end by exocellulase E3, cellopentaose is labeled at the reducing end with (18)O, the products are analyzed by ionspray mass spectrometry, 61% of the (18)O is found in cellotriose
-
?
cellopentaose + H2O
cellotriose + cellobiose
show the reaction diagram
-
cellobiose is preferentially released from the nonreducing end by CBH II, cellopentaose is labeled at the reducing end with (18)O, the products are analyzed by ionspray mass spectrometry, 63% of the (18)O is found in cellotriose
-
?
cellopentaose + H2O
cellotriose + cellobiose
show the reaction diagram
-
-
?
cellopentaose + H2O
cellobiose + ?
show the reaction diagram
Penicillium purpurogenum, Penicillium purpurogenum KJS506
-
-
cellobiose is the major product
?
cellotetraose + H2O
2 cellobiose
show the reaction diagram
-
-
?
cellotetraose + H2O
2 cellobiose
show the reaction diagram
-
-
-
?
cellotetraose + H2O
2 cellobiose
show the reaction diagram
-
-
?
cellotetraose + H2O
2 cellobiose
show the reaction diagram
Ruminiclostridium thermocellum F7
-
-
-
?
cellotetraose + H2O
2 cellobiose
show the reaction diagram
-
-
?
cellotetraose + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
-
-
?
cellotetraose + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
-
-
-
?
cellotetraose + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
Clostridium stercorarium
-
-
-
?
cellotetraose + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
-
-
-
?
cellotetraose + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
-
-
-
?
cellotetraose + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products
?
cellotetraose + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products
?
cellotetraose + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
-
-
preferably cellobiose
?
cellotetraose + H2O
?
show the reaction diagram
-
-
-
-
?
cellotetraose + H2O
?
show the reaction diagram
-
-
-
?
cellotetraose + H2O
cellobiose + ?
show the reaction diagram
-
-
cellobiose is the major product
?
cellotetraose + H2O
cellobiose + ?
show the reaction diagram
-
good substrate
-
?
cellotriitol + H2O
cellobiose + sorbitol
show the reaction diagram
-
-
-
?
cellotriose + H2O
?
show the reaction diagram
-
-
-
-
?
cellotriose + H2O
cellobiose + glucose
show the reaction diagram
-
-
-
?
cellotriose + H2O
cellobiose + glucose
show the reaction diagram
-
-
-
?
cellotriose + H2O
cellobiose + glucose
show the reaction diagram
-
-
-
?
cellotriose + H2O
cellobiose + glucose
show the reaction diagram
-
-
-
?
cellotriose + H2O
glucose + cellobiose
show the reaction diagram
-
-
?
cellulose + H2O
?
show the reaction diagram
-
-
-
-
?
cellulose + H2O
?
show the reaction diagram
-
-
-
-
?
cellulose + H2O
?
show the reaction diagram
-
-
-
-
?
cellulose + H2O
?
show the reaction diagram
-
-
-
-
?
cellulose + H2O
?
show the reaction diagram
-
-
-
-
?
cellulose + H2O
?
show the reaction diagram
-
-
-
-
?
cellulose + H2O
?
show the reaction diagram
-
cellobiohydrolases act from one end of a cellulose chain and processively cleave off cellobiose as the main product. Processivity and synergism are important properties of cellulases, particularly for hydrolysis of crystalline substrates, substrates are phosphoric acid-treated cotton, carboxymethylcellulose, bacterial microcrystalline cellulose, and phosphoric acid-swollen cellulose, as well as 8-mg/ml Whatman no. 1 filter paper, substrate specificity of wild-type and mutant enzymes, overview
-
-
?
cellulose + H2O
?
show the reaction diagram
-
hydrolysis of amorphous cellulose by different concentrations of enzyme using a cellobiose dehydrogenase biosensor, the enzyme TrCel7A is a retaining cellulase and therefore produces solely the beta-anomer
-
-
?
cellulose + H2O
?
show the reaction diagram
Saccharophagus degradans 2-40T
-
-
-
-
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
-
-
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
Clostridium stercorarium
-
-
-
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
-
-
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
Clostridium stercorarium
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
Torula thermophila
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
Chaetomium thermophile, Allescheria terrestris
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
only cellobiose
-
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
Cel6A is a more endo-processive enzyme, whereas Cel7A is essentially a processive enzyme, both forms show a synergistic effect in the digestion of bacterial cellulose
-
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
Ruminiclostridium thermocellum CBH III
-
-
-
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
Phanerochaete chrysosporium CBH I
-
-
-
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
Trichoderma reesei Cel6A
-
-
-
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
-
-
cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
hydrolysis of filter paper by intact cellobiohydrolase I in the presence of additional cellulose binding domains has a synergistic effect, leading to an increase of the sugar production of up to 30%
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
cellulolytic enzyme
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
cellulolytic enzyme, the enzyme is active on most cellulosic substrates
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
the enzyme hydrolyzes beta-1,4-linkages
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
the enzyme hydrolyzes beta-1,4-linkages
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
the enzyme acts on anthranilic-acid-labelled bacterial cellulose, bacterial microcrystalline cellulose, and endoglucanase-pretreated bacterial cellulose, preparation, overview
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
100% activity with 5 mg cellulose, 30% activity with 0.5 mg cellulose as substrate
-
?
cellulose + H2O
cellobiose
show the reaction diagram
Heterobasidion irregulare TC-32-1
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
the enzyme acts on anthranilic-acid-labelled bacterial cellulose, bacterial microcrystalline cellulose, and endoglucanase-pretreated bacterial cellulose, preparation, overview
-
?
cellulose + H2O
cellobiose
show the reaction diagram
Paenibacillus sp. BP-23
-
cellulolytic enzyme, the enzyme is active on most cellulosic substrates
-
?
cellulose + H2O
cellobiose
show the reaction diagram
Penicillium occitanis CL100
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
?
cellulose + H2O
cellobiose + ?
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose + ?
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose + ?
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose + ?
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose + ?
show the reaction diagram
-
-
?
cellulose + H2O
cellobiose + ?
show the reaction diagram
-
cellulose Ialpha from Cladophora sp. and cellulose Ibeta from Halocynthia roretzi
-
?
cellulose + H2O
cellobiose + ?
show the reaction diagram
-
activity with bacterial microcrystalline cellulose, phosphoric acid-treated swollen cellulose, phosphoric acid-treated cotton, and carboxymethyl cellulose
-
?
cellulose + H2O
cellobiose + cellohexaose
show the reaction diagram
hydrolyzes Avicel and filter paper, efficiency of hydrolysis increases in the following order: Gh9, Gh9-Fn31,2, Gh9-Fn31,2-CBDIII
-
?
cellulose + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
Paenibacillus sp., Paenibacillus sp. BP-23
acid-swollen cellulose, bacterial microcrystlline cellulose
-
?
cellulose + H2O
beta-cellobiose
show the reaction diagram
Trichoderma reesei, Trichoderma reesei RUT C30
-
-
-
?
cellulose + H2O
beta-D-cellobiose
show the reaction diagram
-
from cotton
-
?
corn stover + H2O
cellobiose + ?
show the reaction diagram
-
-
?
cotton + H2O
?
show the reaction diagram
-
-
-
-
?
crystalline cellulose + H2O
?
show the reaction diagram
-
-
-
?
crystalline cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
filter paper + H2O
?
show the reaction diagram
-
-
-
-
?
filter paper + H2O
?
show the reaction diagram
-
-
-
-
?
filter paper + H2O
?
show the reaction diagram
Penicillium purpurogenum KJS506
-
-
-
-
?
highly crystalline cellulose + H2O
cellobiose
show the reaction diagram
Trichoderma reesei, Trichoderma reesei ALKO 3413
-
-
-
?
laminarin + H2O
?
show the reaction diagram
Fomitopsis pinicola, Fomitopsis pinicola KMJ812
-
1.5% activity compared to 4-nitrophenyl beta-D-cellobioside
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
high specific activity
-
-
?
lichenan + H2O
?
show the reaction diagram
-
33.8% activity compared to 4-nitrophenyl beta-D-cellobioside
-
-
?
lichenan + H2O
?
show the reaction diagram
Ruminiclostridium thermocellum CBH III
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
Fomitopsis pinicola KMJ812
-
33.8% activity compared to 4-nitrophenyl beta-D-cellobioside
-
-
?
lichenan + H2O
?
show the reaction diagram
Neocallimastix patriciarum J11
-
high specific activity
-
-
?
methylumbelliferyl-lactoside + H2O
methylumberlliferone + lactose
show the reaction diagram
-
-
-
?
nanocellulose + H2O
cellobiose + ?
show the reaction diagram
-
-
-
?
p-nitrophenyl beta-D-cellobioside + H2O
p-nitrophenol + beta-D-cellobiose
show the reaction diagram
Trichoderma pseudokoningii, Trichoderma pseudokoningii S-38
-
-
-
?
p-nitrophenyl beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
show the reaction diagram
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
show the reaction diagram
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
show the reaction diagram
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
show the reaction diagram
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
show the reaction diagram
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
show the reaction diagram
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
show the reaction diagram
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
show the reaction diagram
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
show the reaction diagram
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
show the reaction diagram
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
show the reaction diagram
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
show the reaction diagram
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
show the reaction diagram
Phanerochaete chrysosporium CBH I
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
show the reaction diagram
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + beta-D-cellobiose
show the reaction diagram
Piptoporus betulinus, Piptoporus betulinus CCBAS585
-
-
-
?
p-nitrophenyl-lactoside + H2O
p-nitrophenol + lactose
show the reaction diagram
-
-
-
?
p-nitrophenyl-lactoside + H2O
p-nitrophenol + lactose
show the reaction diagram
-
-
-
?
p-nitrophenyl-lactoside + H2O
p-nitrophenol + lactose
show the reaction diagram
-
-
-
?
p-nitrophenyl-lactoside + H2O
p-nitrophenol + lactose
show the reaction diagram
Ruminiclostridium thermocellum, Ruminiclostridium thermocellum CBH III
-
-
-
-
phosphoric acid swollen cellulose + H2O
?
show the reaction diagram
-
-
-
-
?
phosphoric acid swollen cellulose + H2O
?
show the reaction diagram
-
-
-
?
phosphoric acid swollen cellulose + H2O
?
show the reaction diagram
M55080
-
-
-
?
phosphoric acid swollen cellulose + H2O
?
show the reaction diagram
-
217% activity compared to cellulose
-
-
?
phosphoric acid swollen cellulose + H2O
?
show the reaction diagram
M55080
-
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + cellotriose + ?
show the reaction diagram
Irpex lacteus, Irpex lacteus MC-2
-
shows 9fold higher activity toward phosphoric acid swollen cellulose than toward avicel
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
-
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
Chaetomium thermophilum ALKO4265
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
Acremonium thermophilum ALKO4245
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
Thermoascus aurantiacus ALKO4242
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
phosphoric acid-swollen Avicel + H2O
cellobiose
show the reaction diagram
-
low specific activity
-
?
phosphoric acid-swollen cellulose + H2O
cellobiose
show the reaction diagram
Trichoderma reesei, Trichoderma reesei ALKO 3413
-
-
-
?
sigmacell 20 + H2O
?
show the reaction diagram
-
-
-
-
?
sigmacell 20 + H2O
?
show the reaction diagram
-
-
-
?
sodium hydroxide pretreated corn stover + H2O
?
show the reaction diagram
Trichoderma reesei, Trichoderma reesei ZU-02
-
-
-
-
?
sulforhodamine-conjugated cellohexaose + H2O
cellotetraose + cellotriose
show the reaction diagram
-
-
-
?
wheat straw + H2O
?
show the reaction diagram
-
-
-
-
?
wheat straw + H2O
cellobiose + ?
show the reaction diagram
-
-
-
?
xylan + H2O
?
show the reaction diagram
Fomitopsis pinicola, Fomitopsis pinicola KMJ812
-
1.13% activity compared to 4-nitrophenyl beta-D-cellobioside
-
-
?
xylan + H2O
xylobiose + xylotetraose + xylohexaose
show the reaction diagram
-
-
-
?
xylan + H2O
xylobiose + xylotetraose + xylohexaose
show the reaction diagram
Clostridium stercorarium
-
-
-
?
xylan + H2O
xylobiose + xylotetraose + xylohexaose
show the reaction diagram
-
-
-
?
xylan + H2O
xylobiose + xylotetraose + xylohexaose
show the reaction diagram
-
-
-
?
microcrystalline cellulose Ibeta + H2O
?
show the reaction diagram
-
enzyme-substrate complex, computational simulations and molecular dynamics, modelling of the enzyme interacting with a model segment of a cellulose microfibril, detailed overview
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
substrate specificity, overview
-
-
-
additional information
?
-
-
not: cellobiose
-
-
?
additional information
?
-
-
not: cellobiose
-
-
?
additional information
?
-
-
not: cellobiose
-
-
?
additional information
?
-
-
cellobiose slightly
-
-
-
additional information
?
-
-
hydrolyses internal glucosidic linkages of beta-1,3, 1,4-D-glucan
-
-
?
additional information
?
-
Geotrichum sp.
-
enzyme recognizes the reducing end of oligoxyloglucan and releases two glucosyl residue segments from the main chain
-
-
-
additional information
?
-
-
role in the cellusome, an active cellulase system
-
-
-
additional information
?
-
-
enzyme has detectable cellobiohydrolase activity at pH 5 and pH 7, releases reducing sugars from filter paper and acid swollen Solca Floc-cellulose at acidic pH, enzyme has no endoglucanase activity
-
-
-
additional information
?
-
Geotrichum sp.
enzyme has endoglucanase activity, releases two glucosyl residue segments from the main chain
-
-
-
additional information
?
-
-
enzyme is exclusively an exocellulase
-
-
-
additional information
?
-
no activity on carboxymethyl cellulose, cellobiose, cellotriose or 4-methylumbelliferyl alpha-D-glucoside
-
-
-
additional information
?
-
-
no hydrolysis of a soluble cellulose derivative and barley (1-3),(1-4)-beta-D-glucan
-
-
-
additional information
?
-
-
Cel5A treated cellulose is no longer a substrate for Cel6A or Cel7A
-
-
-
additional information
?
-
-
structure-reactivity studies
-
-
-
additional information
?
-
substrate binding structure analysis of Cel7D
-
-
-
additional information
?
-
-
the full-length and mutant enzyme forms show similar substrate specificities
-
-
-
additional information
?
-
-
no detectable hydrolysis is observed with carboxymethylcellulose, laminarin and p-nitrophenyl beta-D-glucopyranoside
-
-
-
additional information
?
-
-
has a multi domain structure composed of a cellulose-binding domain, a Ser/Thr/Pro-rich linker, and a catalytic domain belonging to family 6 of glycosyl hydrolases, from the N-terminus
-
-
-
additional information
?
-
inability of Cel7B to hydrolyze cellotriose
-
-
-
additional information
?
-
no activity with 4-methylumbelliferyl-beta-D-lactoside
-
-
-
additional information
?
-
-
no activity on oat spelt xylan, carboxymethylcellulose, xylobiose, cellobiose, 4-nitrophenyl-cellobiose, and 4-nitrophenyl derivatives of other disaccharides, overview, no activity on oat spelt xylan, carboxymethylcellulose, xylobiose, cellobiose, and 4-nitrophenyl derivatives of other disaccharides, overview
-
-
-
additional information
?
-
4-nitrophenyl beta-D-glucopyranoside is not a substrate
-
-
-
additional information
?
-
-
does not hydrolyze carboxymethylcellulose
-
-
-
additional information
?
-
-
no activity with cellotriose, and cellotetraose
-
-
-
additional information
?
-
-
the enzyme liberates cellobiose and cellotriose from the nonreducing ends and requires at least four contiguous beta-1,4-linked glucosyl units for a substrate but does not recognize sulforhodamine-conjugated 1-amino-1-deoxyglucitol. ulforhodamine-conjugated cellotetraose, carboxymethylcellulose, hydroxyethyl cellulose, xylan, and mannan are no substrates
-
-
-
additional information
?
-
-
binding properties between the cellulose binding module Cel6A and cellulose substrates, e.g. crystalline cellulose, microcrystalline cellulose Avicel PH101, partially crystalline cellulose, and phosphoric acid swollen amorphous cellulose, thermodynamics, overview. Binding between cellulose binding module CBMCel6A and cellulose to some extent relates to the crystallinity of cellulose
-
-
-
additional information
?
-
-
isoform CBHII is not active towards 4-methylumbelliferyl beta-D-cellobioside and 4-methylumbelliferyl beta-D-lactopyranoside
-
-
-
additional information
?
-
-
no detectable activity on laminarin, 4-nitrophenyl-beta-D-glucopyranoside, oat spelt xylan, and birch wood xylan
-
-
-
additional information
?
-
-
the enzyme is efficient in hydrolyzing crystalline cellulosic substrates, such as Avicel and Sigmacell 20, but is not effective in the hydrolysis of substituted substrates, such as caboxymethyl cellulose
-
-
-
additional information
?
-
Fomitopsis pinicola KMJ812
-
no activity with cellotriose, and cellotetraose
-
-
-
additional information
?
-
Melanocarpus albomyces ALKO4237
-
enzyme has detectable cellobiohydrolase activity at pH 5 and pH 7, releases reducing sugars from filter paper and acid swollen Solca Floc-cellulose at acidic pH, enzyme has no endoglucanase activity
-
-
-
additional information
?
-
Penicillium purpurogenum KJS506
-
does not hydrolyze carboxymethylcellulose
-
-
-
additional information
?
-
-
Cel5A treated cellulose is no longer a substrate for Cel6A or Cel7A
-
-
-
additional information
?
-
Irpex lacteus MC-2
-
has a multi domain structure composed of a cellulose-binding domain, a Ser/Thr/Pro-rich linker, and a catalytic domain belonging to family 6 of glycosyl hydrolases, from the N-terminus
-
-
-
additional information
?
-
Acremonium thermophilum ALKO4245
no activity with 4-methylumbelliferyl-beta-D-lactoside
-
-
-
additional information
?
-
Paenibacillus sp. BP-23
no activity on carboxymethyl cellulose, cellobiose, cellotriose or 4-methylumbelliferyl alpha-D-glucoside
-
-
-
additional information
?
-
the enzyme is efficient in hydrolyzing crystalline cellulosic substrates, such as Avicel and Sigmacell 20, but is not effective in the hydrolysis of substituted substrates, such as caboxymethyl cellulose
-
-
-
additional information
?
-
Neocallimastix patriciarum J11
-
no detectable activity on laminarin, 4-nitrophenyl-beta-D-glucopyranoside, oat spelt xylan, and birch wood xylan
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
cellulose + H2O
?
show the reaction diagram
-
-
-
-
?
cellulose + H2O
?
show the reaction diagram
-
cellobiohydrolases act from one end of a cellulose chain and processively cleave off cellobiose as the main product. Processivity and synergism are important properties of cellulases, particularly for hydrolysis of crystalline substrates
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
Q7LIJ0
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
P62694
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
Q68HC2
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
I1SB08
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
Q60029
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
G0SD43
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
cellulolytic enzyme
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
cellulolytic enzyme, the enzyme is active on most cellulosic substrates
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
the enzyme hydrolyzes beta-1,4-linkages
-
?
cellulose + H2O
cellobiose + ?
show the reaction diagram
-
-
-
?
cellulose + H2O
beta-cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
Heterobasidion irregulare TC-32-1
I1SB08
-
-
?
cellulose + H2O
beta-cellobiose
show the reaction diagram
Trichoderma reesei RUT C30
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
Paenibacillus sp. BP-23
-
cellulolytic enzyme, the enzyme is active on most cellulosic substrates
-
?
cellulose + H2O
cellobiose
show the reaction diagram
Penicillium occitanis CL100
Q68HC2
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose
show the reaction diagram
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
Q9P8P3
-
-
?
additional information
?
-
-
role in the cellusome, an active cellulase system
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ba2+
-
120% activity at 1 mM
Ca2+
-
required for maximal activity
Ca2+
-
one mol of calcium per each domain
Ca2+
-
bound by all enzyme domains, except for the immunoglobulin-like module
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+
-
contains Ca2+
Ca2+
-
121% activity at 1 mM
Co2+
-
activates
Co2+
-
activates
Co2+
-
146% activity at 1 mM
Cu2+
-
-
Cu2+
-
127% activity at 1 mM
Fe2+
-
117% activity at 1 mM
Fe3+
-
138% activity at 1 mM
Mg2+
-
hexa-co-ordinate
Mg2+
-
activates
Mn2+
-
activates
Mn2+
-
activates
Zn2+
-
115% activity at 1 mM
Mn2+
-
116% activity at 1 mM
additional information
-
enzyme activity is not stimulated by Ba2+, Mg2+, Mn2+, Zn2+, Ca2+, Ni2+, or Co2+ (each at 1 mM)
additional information
-
not activated by Mg2+ and Li+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(R)-2-[2-hydroxy-3-(phenanthren-9-yloxy)propylamino]-propane-1,3-diol
-
-
(S)-1-isopropylamino-3-(phenanthren-9-yloxy)-propan-2-ol
-
-
(S)-2-[2-hydroxy-3-(naphthalen-1-yloxy)-propylamino]-propane-1,3-diol
-
-
(S)-2-[2-hydroxy-3-(phenanthren-9-yloxy)propylamino]-propane-1,3-diol
-
-
(S)-propranolol
-
-
1,10-phenanthroline
-
-
4-nitrophenyl beta-D-cellopentaoside
-
-
Ag+
-
9% residual activity at 1 mM
cellobioimidazole
i.e. (5R,6R,7S,8S)-6-(beta-D-glucopyranosyloxy)-5,6,7,8-tetrahydro-5-[(hydroxy)methyl]imidazol[1,2a] pyridine-7,8-diol, the disaccharide binds in the glycosyl-binding subsites +1 and +2 close to the exit of the cellulose-binding tunnel/cleft of Cel7D, binding structure analysis
cellobiose
-
-
cellobiose
-
CBH I
cellobiose
-
presence of cellobiose dehydrogenase relieves inhibition
cellobiose
-
-
cellobiose
-
competitive with wild-type enzyme, mixed inhibition with mutant enzyme
cellobiose
-
competitive inhibition
cellobiose
-
competitive inhibitor with 4-nitrophenyl lactoside as substrate
cellobiose
competitive inhibition
cellobiose
competitive inhibition
cellobiose
weakly inhibits, competitive inhibition
cellobiose
-
competitive inhibition
cellobiose
-
the enzyme shows decreased hydrolysis of SR-C6 as the cellobiose concentration increases in the reaction mixture
cellobiose
product inhibition by cellobiose
cellobiose
-
competitive inhibition
cellobiose
-
competitive inhibition; competitive inhibition
Co2+
-
33.7% inhibition at 1 mM
D-xylose
-
-
EDTA
-
slight
EDTA
-
-
EDTA
-
24.6% inhibition at 1 mM
Fe2+
-
complete inhibition at 1 mM
Hg2+
-
complete inhibition at 1 mM
Hg2+
-
60% inhibition at 1 mM
Hg2+
-
4% residual activity at 1 mM, complete inhibition at 10 mM
kanamycin
-
-
lactose
-
competitive inhibition of CBHIA and CBHIB isoform, but only minimal effect on CBHII
lactose
the disaccharide binds in the glycosyl-binding subsites +1 and +2 close to the exit of the cellulose-binding tunnel/cleft of Cel7D, binding structure analysis
lignin
-
increase in temperature from 45 to 65C increases the inhibitory effect of lignin
-
N-bromosuccinimide
-
-
N-bromosuccinimide
-
-
N-bromosuccinimide
-
-
N-ethylmaleimide
-
30% inhibition at 10 mM
NaN3
-
-
neomycin
-
-
suramin
-
slight
viomycin
-
-
xylobiose
-
strong competitive inhibitor
xylotriose
-
strong competitive inhibitor
Zn2+
-
21.2% inhibition at 1 mM
methyl (4S)-beta-cellobiosyl-4-thio-beta-cellobioside
a thio-linked substrate analogue, the disaccharide binds in the glycosyl-binding subsites +1 and +2 close to the exit of the cellulose-binding tunnel/cleft of Cel7D, binding structure analysis
additional information
cellobiose concentrations up to 30 mM do not inhibit cellobiohydrolase activity
-
additional information
-
the enzyme is neither inhibited nor activated by EDTA at concentrations ranging from 1 to 10 mM
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
136.5% activity at 0.5 mM
isopropyl beta-D-1-thiogalactopyranoside
inducer
-
additional information
-
wild-type and recombinant endoglucanases Cel9B and Cel48C associated with endo- or exo-acting glucanases from Thermobifida fusca synergistically enhance the enzyme activity, optimization, overview
-
additional information
enzyme domain GH5 activity on avicel and corn stover is enhanced upon pretreatment with 1-ethyl-3-methylimidazolium acetate, and activity is further improved when the CBM3 domain was fused to GH5
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.55
2,4-dinitrophenyl beta-lactoside
-
pH 5.7, 37C, wild-type enzyme
0.61
2,4-dinitrophenyl beta-lactoside
-
pH 5.7, 37C, mutant E217Q
0.67
2,4-dinitrophenyl beta-lactoside
-
pH 5.7, 37C, mutant D214N
0.0015
2,4-dinitrophenyl cellobiose
-
pH 5.5, 50C, recombinant mutant D274A
0.0023
2,4-dinitrophenyl cellobiose
-
pH 5.5, 50C, recombinant wild-type enzyme
0.0065
2,4-dinitrophenyl cellobiose
-
pH 5.5, 50C, recombinant mutant D226A
0.044
2,4-dinitrophenyl cellobiose
-
pH 5.5, 50C, recombinant mutant S232A
0.161
2,4-dinitrophenyl cellobiose
-
pH 5.5, 50C, recombinant mutant Y220A
0.214
2,4-dinitrophenyl cellobiose
-
pH 5.5, 50C, recombinant mutant D497A
3.7
2-chloro-4-nitrophenyl beta-D-lactoside
-
50 mM sodium acetate buffer, pH 5.0, at 50C
-
0.46
2-chloro-4-nitrophenyl beta-lactoside
-
pH 5.7, 37C, wild-type enzyme
0.57
2-chloro-4-nitrophenyl beta-lactoside
-
pH 5.7, 37C, mutant D214N
0.68
2-chloro-4-nitrophenyl beta-lactoside
-
pH 5.7, 37C, mutant E212Q
0.78
2-chloro-4-nitrophenyl beta-lactoside
-
pH 5.7, 37C, mutant E217Q
4.5
2-chloro-4-nitrophenyl-beta-D-cellotrioside
-
pH 5, 50C, CBHII isoform
0.52
2-chloro-4-nitrophenyl-beta-D-lactoside
-
in 50 mM sodium phosphate buffer, pH 5.7, at 22C
0.62
2-chloro-4-nitrophenyl-beta-D-lactoside
-
Cel7B wild-type expressed in Trichoderma reesei, at 22C, pH 6.0
0.75
2-chloro-4-nitrophenyl-beta-D-lactoside
-
Cel7B mutant S290T/G4C/M70C expressed in Saccharomyces cerevisiae, at 22C, pH 6.0
0.8
2-chloro-4-nitrophenyl-beta-D-lactoside
-
Cel7B wild-type expressed in Saccharomyces cerevisiae, at 22C, pH 6.0
0.99
2-chloro-4-nitrophenyl-beta-D-lactoside
in 50 mM sodium phosphate buffer, pH 5.7, at 22C
1
2-chloro-4-nitrophenyl-beta-D-lactoside
-
Cel7B mutant G4C/M70C expressed in Saccharomyces cerevisiae, at 22C, pH 6.0
1.16
2-chloro-4-nitrophenyl-beta-D-lactoside
-
Cel7B mutant S290T expressed in Saccharomyces cerevisiae, at 22C, pH 6.0
2
2-chloro-4-nitrophenyl-beta-D-lactoside
in 50 mM sodium phosphate buffer, pH 5.7, at 22C
2.1
2-chloro-4-nitrophenyl-beta-D-lactoside
in 50 mM sodium phosphate buffer, pH 5.7, at 22C
0.46
2-chloro-4-nitrophenyl-beta-lactoside
-
-
0.57
2-chloro-4-nitrophenyl-beta-lactoside
-
D214N
0.68
2-chloro-4-nitrophenyl-beta-lactoside
-
E212Q
0.78
2-chloro-4-nitrophenyl-beta-lactoside
-
E217Q
3.7
2-chloro-4-nitrophenyl-beta-lactoside
-
pH 5.0, 50C
0.83
2-chloronitrophenyl-beta-D-lactoside
-
pH 6, 60C
11
3,4-dinitrophenyl-cellobioside
-
25C, pH 7, wild-type
14
3,4-dinitrophenyl-cellobioside
-
25C, pH 5, wild-type
48
3,4-dinitrophenyl-cellobioside
-
25C, pH 5, E223S/A224H/L225V/T226A/D262G mutant
161
3,4-dinitrophenyl-cellobioside
-
25C, pH 7, E223S/A224H/L225V/T226A/D262G mutant
380
3,4-dinitrophenyl-lactoside
-
25C, pH 5, wild-type
543
3,4-dinitrophenyl-lactoside
-
25C, pH 5, E223S/A224H/L225V/T226A/D262G mutant
0.52
4-bromophenyl beta-lactoside
-
pH 5.7, 37C, wild-type enzyme
0.318
4-methylumbelliferyl beta-D-lactopyranoside
-
mutant enzyme W40A, at pH 5.0 and 27C
-
0.358
4-methylumbelliferyl beta-D-lactopyranoside
-
wild type enzyme, at pH 5.0 and 27C
-
0.52
4-methylumbelliferyl beta-lactoside
-
pH 5.7, 37C, wild-type enzyme
0.53
4-methylumbelliferyl beta-lactoside
-
pH 5.7, 37C, mutant E212Q
0.65
4-methylumbelliferyl beta-lactoside
-
pH 5.7, 37C, mutant E217Q
0.79
4-methylumbelliferyl beta-lactoside
-
pH 5.7, 37C, mutant D214N
0.00187
4-methylumbelliferyl-beta-D-lactoside
-
at pH 5.0 and 50C
0.22
4-methylumbelliferyl-beta-D-lactoside
in 50 mM sodium acetate buffer, pH 5.0, at 22C
0.221
4-methylumbelliferyl-beta-D-lactoside
in 50 mM sodium acetate buffer, pH 5.0, at 22C
0.23
4-methylumbelliferyl-beta-D-lactoside
-
Cel7B wild-type expressed in Trichoderma reesei, at 22C, pH 6.0
0.268
4-methylumbelliferyl-beta-D-lactoside
in 50 mM sodium acetate buffer, pH 5.0, at 22C
0.28
4-methylumbelliferyl-beta-D-lactoside
-
Cel7B mutant S290T expressed in Saccharomyces cerevisiae, at 22C, pH 6.0; Cel7B wild-type expressed in Saccharomyces cerevisiae, at 22C, pH 6.0
0.287
4-methylumbelliferyl-beta-D-lactoside
-
in 50 mM sodium acetate buffer, pH 5.0, at 22C
0.3
4-methylumbelliferyl-beta-D-lactoside
-
Cel7B mutant G4C/M70C expressed in Saccharomyces cerevisiae, at 22C, pH 6.0; Cel7B mutant S290T/G4C/M70C expressed in Saccharomyces cerevisiae, at 22C, pH 6.0
0.6
4-nitrophenyl beta-D-cellobioside
-
wild-type Cex
1.1
4-nitrophenyl beta-D-cellobioside
-
recombinant Cex-RsaA fusion mutant
1.1
4-nitrophenyl beta-D-cellobioside
-
at pH 5.0, 60C
2.1
4-nitrophenyl beta-D-cellobioside
-
in 100 mM sodium acetate buffer (pH 5.0) at 50C
2.2
4-nitrophenyl beta-D-cellobioside
domain GH5, at pH 5.5 and 80C,
2.4
4-nitrophenyl beta-D-cellobioside
domain construct CBM3-GH5, at pH 5.5 and 80C,
3.4
4-nitrophenyl beta-D-cellobioside
-
50 mM sodium acetate buffer, pH 5.0, at 50C
0.21
4-nitrophenyl beta-lactoside
-
pH 5.7, 37C, mutant E217Q
0.22
4-nitrophenyl beta-lactoside
-
pH 5.7, 37C, wild-type enzyme
0.27
4-nitrophenyl beta-lactoside
-
pH 5.7, 37C, mutant E212Q
0.37
4-nitrophenyl beta-lactoside
-
pH 5.7, 37C, mutant D214N
3.4
4-nitrophenyl D-cellobioside
-
pH 5.0, 50C
-
0.04
4-nitrophenyl lactoside
-
pH 5, 30C, Y247F mutant
0.041
4-nitrophenyl lactoside
-
pH 5, 30C, wild-type enzyme
0.44
4-nitrophenyl lactoside
-
pH 5, 30C, D241C/D249C mutant
1.8
4-nitrophenyl lactoside
-
pH 5, 30C, DELTAG245-Y252 mutant
0.42
4-nitrophenyl-beta-D-cellobioside
-
pH 6, 60C
3.7
4-nitrophenyl-beta-D-lactoside
-
pH 5, 50C, CBHIB isoform
10.7
4-nitrophenyl-beta-D-lactoside
-
pH 5, 50C, CBHIA isoform
0.77
alpha-cellobiosyl fluoride
-
pH 5, 20C
2.35
alpha-cellobiosyl fluoride
-
pH 5, 20C
12
Avicel
-
exo III
-
44.1
Avicel
-
exo II
-
0.022
beta-cellobiosyl fluoride
-
pH 5, 20C
0.15
beta-cellobiosyl fluoride
-
pH 5, 20C
14
cellohexaose
-
pH 5, 27C, wild-type enzyme
1.3
Cellopentaose
-
pH 5, 27C, wild-type enzyme
1.4
Cellopentaose
-
pH 5, 27C, D175A mutant
2.6
Cellotetraose
-
pH 5, 27C, wild-type enzyme
4
Cellotetraose
-
pH 5, 27C, D175A mutant
0.58
p-nitrophenyl beta-D-cellobioside
-
-
0.1
p-nitrophenyl-beta-D-cellobioside
-
-
0.21
p-nitrophenyl-beta-D-cellobioside
-
extracellular
0.27
p-nitrophenyl-beta-D-cellobioside
-
periplasmic
0.384
p-nitrophenyl-beta-D-cellobioside
-
-
0.4
p-nitrophenyl-beta-D-cellobioside
-
-
3.08
p-nitrophenyl-beta-D-cellobioside
-
-
3
p-Nitrophenyl-lactoside
-
-
17
cellotriose
-
pH 5, 27C, wild-type enzyme
additional information
additional information
-
-
-
additional information
additional information
-
cellulose: 1.0 mg/ml
-
additional information
additional information
-
H3PO4-swollen cellulose: 0.0067 mM
-
additional information
additional information
-
detailed kinetic analysis of wild-type enzyme and mutants E212Q, D214N, and E217Q
-
additional information
additional information
-
active-site titration kinetics of Cel7A, i.e. burst kinetics, for quantitation of the progressivity of the enzyme, overview
-
additional information
additional information
-
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.9
2,4-dinitrophenyl beta-lactoside
Trichoderma reesei
-
pH 5.7, 37C, mutant D214N
12.2
2,4-dinitrophenyl beta-lactoside
Trichoderma reesei
-
pH 5.7, 37C, mutant E217Q
104
2,4-dinitrophenyl beta-lactoside
Trichoderma reesei
-
pH 5.7, 37C, wild-type enzyme
0.0001
2,4-dinitrophenyl cellobiose
Thermobifida fusca
-
pH 5.5, 50C, recombinant mutant D497A
0.0005
2,4-dinitrophenyl cellobiose
Thermobifida fusca
-
pH 5.5, 50C, recombinant mutant S232A
0.0015
2,4-dinitrophenyl cellobiose
Thermobifida fusca
-
pH 5.5, 50C, recombinant mutant Y220A
0.0018
2,4-dinitrophenyl cellobiose
Thermobifida fusca
-
pH 5.5, 50C, recombinant mutant D226A
0.038
2,4-dinitrophenyl cellobiose
Thermobifida fusca
-
pH 5.5, 50C, recombinant mutant D274A
0.057
2,4-dinitrophenyl cellobiose
Thermobifida fusca
-
pH 5.5, 50C, recombinant wild-type enzyme
0.74
2-chloro-4-nitrophenyl beta-D-lactoside
Trichoderma harzianum
-
50 mM sodium acetate buffer, pH 5.0, at 50C
-
0.0063
2-chloro-4-nitrophenyl beta-lactoside
Trichoderma reesei
-
pH 5.7, 37C, mutant E212Q
0.035
2-chloro-4-nitrophenyl beta-lactoside
Trichoderma reesei
-
pH 5.7, 37C, mutant E217Q
0.15
2-chloro-4-nitrophenyl beta-lactoside
Trichoderma reesei
-
pH 5.7, 37C, mutant D214N
12.8
2-chloro-4-nitrophenyl beta-lactoside
Trichoderma reesei
-
pH 5.7, 37C, wild-type enzyme
0.0153
2-chloro-4-nitrophenyl-beta-D-lactoside
Melanocarpus albomyces
-
Cel7B wild-type expressed in Saccharomyces cerevisiae, at 22C, pH 6.0
0.0165
2-chloro-4-nitrophenyl-beta-D-lactoside
Melanocarpus albomyces
-
Cel7B mutant S290T/G4C/M70C expressed in Saccharomyces cerevisiae, at 22C, pH 6.0
0.0167
2-chloro-4-nitrophenyl-beta-D-lactoside
Melanocarpus albomyces
-
Cel7B wild-type expressed in Trichoderma reesei, at 22C, pH 6.0
0.01817
2-chloro-4-nitrophenyl-beta-D-lactoside
Melanocarpus albomyces
-
Cel7B mutant G4C/M70C expressed in Saccharomyces cerevisiae, at 22C, pH 6.0
0.0205
2-chloro-4-nitrophenyl-beta-D-lactoside
Melanocarpus albomyces
-
Cel7B mutant S290T expressed in Saccharomyces cerevisiae, at 22C, pH 6.0
0.0283
2-chloro-4-nitrophenyl-beta-D-lactoside
Thermoascus aurantiacus
A7WNU2
in 50 mM sodium phosphate buffer, pH 5.7, at 22C
0.043
2-chloro-4-nitrophenyl-beta-D-lactoside
Trichoderma reesei
-
in 50 mM sodium phosphate buffer, pH 5.7, at 22C
0.0467
2-chloro-4-nitrophenyl-beta-D-lactoside
Acremonium thermophilum
A7WNT9, A7WNU0
in 50 mM sodium phosphate buffer, pH 5.7, at 22C
0.3167
2-chloro-4-nitrophenyl-beta-D-lactoside
Chaetomium thermophilum
A7WNU1
in 50 mM sodium phosphate buffer, pH 5.7, at 22C
0.74
2-chloro-4-nitrophenyl-beta-lactoside
Trichoderma harzianum
-
pH 5.0, 50C
8.9
2-chloronitrophenyl-beta-D-cellotrioside
Rasamsonia emersonii
-
pH 5, 50C, CBHII isoform
9108
2-chloronitrophenyl-beta-D-lactoside
Ruminiclostridium thermocellum
-
pH 6, 60C
1.7
4-bromophenyl beta-lactoside
Trichoderma reesei
-
pH 5.7, 37C, wild-type enzyme
0.33
4-methylumbelliferyl beta-D-lactopyranoside
Trichoderma reesei
-
mutant enzyme W40A, at pH 5.0 and 27C
-
0.49
4-methylumbelliferyl beta-D-lactopyranoside
Trichoderma reesei
-
wild type enzyme, at pH 5.0 and 27C
-
0.0073
4-methylumbelliferyl beta-lactoside
Trichoderma reesei
-
pH 5.7, 37C, mutant E217Q
0.063
4-methylumbelliferyl beta-lactoside
Trichoderma reesei
-
pH 5.7, 37C, mutant E212Q
2.3
4-methylumbelliferyl beta-lactoside
Trichoderma reesei
-
pH 5.7, 37C, mutant D214N
47
4-methylumbelliferyl beta-lactoside
Trichoderma reesei
-
pH 5.7, 37C, wild-type enzyme
0.083
4-methylumbelliferyl-beta-D-lactoside
Melanocarpus albomyces
-
Cel7B mutant G4C/M70C expressed in Saccharomyces cerevisiae, at 22C, pH 6.0
0.1067
4-methylumbelliferyl-beta-D-lactoside
Melanocarpus albomyces
-
Cel7B wild-type expressed in Saccharomyces cerevisiae, at 22C, pH 6.0
0.1083
4-methylumbelliferyl-beta-D-lactoside
Melanocarpus albomyces
-
Cel7B mutant S290T expressed in Saccharomyces cerevisiae, at 22C, pH 6.0
0.12
4-methylumbelliferyl-beta-D-lactoside
Melanocarpus albomyces
-
Cel7B mutant S290T/G4C/M70C expressed in Saccharomyces cerevisiae, at 22C, pH 6.0
0.143
4-methylumbelliferyl-beta-D-lactoside
Melanocarpus albomyces
-
Cel7B wild-type expressed in Trichoderma reesei, at 22C, pH 6.0
0.1883
4-methylumbelliferyl-beta-D-lactoside
Acremonium thermophilum
A7WNT9, A7WNU0
in 50 mM sodium acetate buffer, pH 5.0, at 22C
0.325
4-methylumbelliferyl-beta-D-lactoside
Thermoascus aurantiacus
A7WNU2
in 50 mM sodium acetate buffer, pH 5.0, at 22C
0.4783
4-methylumbelliferyl-beta-D-lactoside
Trichoderma reesei
-
in 50 mM sodium acetate buffer, pH 5.0, at 22C
1.15
4-methylumbelliferyl-beta-D-lactoside
Chaetomium thermophilum
A7WNU1
in 50 mM sodium acetate buffer, pH 5.0, at 22C
0.08
4-nitrophenyl beta-D-cellobioside
Cellulomonas fimi
-
recombinant Cex-RsaA fusion mutant
0.39
4-nitrophenyl beta-D-cellobioside
Trichoderma harzianum
-
50 mM sodium acetate buffer, pH 5.0, at 50C
15.8
4-nitrophenyl beta-D-cellobioside
Cellulomonas fimi
-
wild-type Cex
0.00066
4-nitrophenyl beta-lactoside
Trichoderma reesei
-
pH 5.7, 37C, mutant E217Q
0.0041
4-nitrophenyl beta-lactoside
Trichoderma reesei
-
pH 5.7, 37C, mutant E212Q
0.042
4-nitrophenyl beta-lactoside
Trichoderma reesei
-
pH 5.7, 37C, mutant D214N
3.5
4-nitrophenyl beta-lactoside
Trichoderma reesei
-
pH 5.7, 37C, wild-type enzyme
0.39
4-nitrophenyl D-cellobioside
Trichoderma harzianum
-
pH 5.0, 50C
-
0.061
4-nitrophenyl lactoside
Trichoderma reesei
-
pH 5, 30C, Y247F mutant
0.093
4-nitrophenyl lactoside
Trichoderma reesei
-
pH 5, 30C, wild-type enzyme
0.19
4-nitrophenyl lactoside
Trichoderma reesei
-
pH 5, 30C, DELTAG245-Y252 mutant
0.82
4-nitrophenyl lactoside
Trichoderma reesei
-
pH 5, 30C, D241C/D249C mutant
2952
4-nitrophenyl-beta-D-cellobioside
Ruminiclostridium thermocellum
-
pH 6, 60C
13.4
4-nitrophenyl-beta-D-lactoside
Rasamsonia emersonii
-
pH 5, 50C, CBHIA and CBHIB isoform
0.01
alpha-cellobiosyl fluoride
Humicola insolens
-
pH 5, 20C
0.54
alpha-cellobiosyl fluoride
Trichoderma reesei
-
pH 5, 20C
5.1
amorphous cellulose
Trichoderma reesei
-
in 50 mM sodium acetate with 2 mM CaCl2 and pH 5.0 at 25C
-
4.75
Avicel
Trichoderma reesei
-
in 50 mM sodium acetate with 2 mM CaCl2 and pH 5.0 at 25C
-
2.4
bacterial microcrystalline cellulose
Trichoderma reesei
-
in 50 mM sodium acetate with 2 mM CaCl2 and pH 5.0 at 25C
-
0.071
beta-cellobiosyl fluoride
Humicola insolens
-
pH 5, 20C
4
beta-cellobiosyl fluoride
Trichoderma reesei
-
pH 5, 20C
0.02
cellohexaose
Trichoderma reesei
-
pH 5, 27C, D175A mutant
14
cellohexaose
Trichoderma reesei
-
pH 5, 27C, wild-type enzyme
0.025
Cellopentaose
Trichoderma reesei
-
pH 5, 27C, D175A mutant
1.1
Cellopentaose
Trichoderma reesei
-
pH 5, 27C, wild-type enzyme
0.0013
Cellotetraose
Trichoderma reesei
-
pH 5, 27C, D175A mutant
0.5
Cellotetraose
Trichoderma reesei
-
pH 5, 27C, wild-type enzyme
0.58
Cellotetraose
Trichoderma reesei
-
pH 5, 27C, Y247F mutant and D241C/D249C mutant
0.83
Cellotetraose
Trichoderma reesei
-
pH 5, 27C, DELTAG245-Y252 mutant
4.1
Cellotetraose
Trichoderma reesei
-
pH 5, 27C, wild-type enzyme
0.0003
cellotriose
Trichoderma reesei
-
pH 5, 27C, D175A mutant
0.06
cellotriose
Trichoderma reesei
-
pH 5, 27C, wild-type enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.03
4-methylumbelliferyl beta-D-lactopyranoside
Trichoderma reesei
-
mutant enzyme W40A, at pH 5.0 and 27C
202189
1.37
4-methylumbelliferyl beta-D-lactopyranoside
Trichoderma reesei
-
wild type enzyme, at pH 5.0 and 27C
202189
15.8
4-nitrophenyl beta-D-cellobioside
Fomitopsis pinicola
-
in 100 mM sodium acetate buffer (pH 5.0) at 50C
4692
additional information
additional information
Thermobifida fusca
-
-
2
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.4
4-nitrophenyl beta-D-cellopentaoside
at pH 4.5 and 30C
-
0.0055
cellobiose
-
Cel7B mutant G4C/M70C expressed in Saccharomyces cerevisiae, at 22C, pH 6.0
0.006
cellobiose
-
Cel7B wild-type expressed in Trichoderma reesei, at 22C, pH 6.0
0.0063
cellobiose
-
Cel7B wild-type expressed in Saccharomyces cerevisiae, at 22C, pH 6.0
0.0066
cellobiose
-
Cel7B mutant S290T expressed in Saccharomyces cerevisiae, at 22C, pH 6.0
0.019
cellobiose
-
Cel7B mutant S290T/G4C/M70C expressed in Saccharomyces cerevisiae, at 22C, pH 6.0
0.019
cellobiose
-
-
0.02
cellobiose
-
25C, wild-type enzyme
0.02
cellobiose
-
pH 5.0, 50C
0.16
cellobiose
-
2-chloro-4-nitrophenyl-D-cellotrioside as substrate, pH 5, 50C, CBHII isoform
0.18
cellobiose
-
4-nitrophenyl-beta-D-cellobioside as substrate, pH 5, 50C, CBHIB isoform
0.755
cellobiose
-
25C, E223S/A224H/L225V/T226A/D262G mutant
1.4
cellobiose
pH 4.5, 30C
2.5
cellobiose
-
4-nitrophenyl-beta-D-cellobioside as substrate, pH 5, 50C, CBHIA isoform
7.2
cellobiose
-
50 mM sodium acetate buffer, pH 5.0, at 50C
14.8
cellobiose
-
at pH 5.0, 50C
22
cellobiose
-
pH 5, 30C, Y247F mutant
24
cellobiose
-
pH 5, 30C, wild-type enzyme
300
cellobiose
-
pH 5, 30C, DELTAG245-Y252 mutant
0.34
lactose
-
4-nitrophenyl-beta-D-cellobioside as substrate, pH 5, 50C, CBHIB isoform
18.2
lactose
-
4-nitrophenyl-beta-D-cellobioside as substrate, pH 5, 50C, CBHIA isoform
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.2
cellobiose
Trichoderma harzianum
-
pH 5.0, 50C
30
cellobiose
Caldicellulosiruptor saccharolyticus
A4XIF7
domain GH5, in 50 mM MES buffer at pH 5.5 and 80C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.00188
bacterial microcrystalline cellulose as substrate
0.00488
acid swollen cellulose as substrate
0.037
Clostridium stercorarium
-
-
0.114
-
CBH II
0.151
-
CBH I
1.1
-
CBHIA isoform, 4-nitrophenyl-beta-lactoside as substrate
1.1
-
after 23.1fold purification, at pH 6.0 and 37C for 15 min using avicel as substrate
1.6
-
purified recombinant enzyme, substrate 4-methylumbelliferyl beta-D-lactoside
1.72
M55080
purified recombinant enzyme from Pichia pastoris, pH 5.0, 50C
2.1
-
with phosphoric acid swollen cellulose as substrate
2.15
-
purified recombinant enzyme, substrate 4-methylumbelliferyl beta-D-cellobioside
2.4
M55080
purified recombinant enzyme from Yarrowia lipolytica, pH 5.0, 50C
2.5
-
CBHIB isoform, 4-nitrophenyl-beta-lactoside as substrate
2.6
-
crude enzyme, pH 5.0, 60C
3.3
-
after 23.1fold purification, at pH 6.0 and 37C for 15 min using phosphoric acid-swollen avicel as substrate
4
-
crude cell extract, using 4-nitrophenyl beta-D-cellobioside as substrate, at pH 5.0, 50C
5.6
-
CBHIB isoform, avicel as substrate
7.5
-
with carboxymethylcellulose as substrate
8.7
-
crude enzyme, at pH 6.0 and 37C for 15 min using 0.5% lichenan as substrate
10.8
-
after4.2fold purification, pH 5.0, 60C
15.31
Geotrichum sp.
-
16.5
-
CBHII isoform, avicel as substrate
18
-
p-nitrophenyl lactose
18.7
-
p-nitrophenyl-beta-D-cellobioside
18.8
-
carboxymethyl cellulose
20.9
-
native Ex-1, substrate Avicel
23.9
-
deglycosylated recombinant Ex-1, substrate Avicel
24.8
-
CBHIA isoform, avicel as substrate
25
-
deglycosylated recombinant Ex-1, substrate carboxymethyl cellulose
26
-
native Ex-1, substrate carboxymethyl cellulose
26
-
after 6.8fold purification, using 4-nitrophenyl beta-D-cellobioside as substrate, at pH 5.0, 50C
26
-
isoform CBHI, with 4-methylumbelliferyl beta-D-lactopyranoside as substrate, at 50C, pH 5.0 in 50 mM sodium acetate
41
-
isoform CBHI, with 4-methylumbelliferyl beta-D-cellobioside as substrate, at 50C, pH 5.0 in 50 mM sodium acetate
108
-
after 23.1fold purification, at pH 6.0 and 37C for 15 min using carboxymethyl cellulose as substrate
317
-
after 23.1fold purification, at pH 6.0 and 37C for 15 min using lichenan as substrate
340
-
with barley beta-glucan as substrate
1809
-
after 23.1fold purification, at pH 6.0 and 37C for 15 min using barley beta-glucan as substrate
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
-
additional information
-
cellulose substrate type specificity of wild-type and mutant enzymes, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2.5
-
isozyme I
3.5 - 4
-
amorphous cellulose
3.5 - 5
Geotrichum sp.
-
3.6
-
CBHIA isoform
3.8
-
CBHII isoform
4 - 4.5
-
isozyme II
4 - 5
-
crystalline cellulose
4 - 5
-
isozyme I
4 - 6
-
thermophilic fungi
4 - 6.5
substrate 4-nitrophenyl beta-D-cellotrioside; with 4-nitrophenyl beta-D-cellotrioside as substrate
4 - 8
substrate 4-nitrophenyl beta-D-cellopentaoside; with 4-nitrophenyl beta-D-cellopentaoside as substrate
4.1
-
CBHIB isoform
4.2
-
avicel
4.5
-
cellulose
4.5
-
isozyme II
4.5 - 5.5
-
-
4.5 - 6.5
-
isoform CBHI
4.5 - 7
-
exo III
4.7
pH-optimum for domain construct CBM3-GH5
4.8
-
isoform CBHII
5
-
p-nitrophenyl-lactoside
5
-
assay at
5
-
assay at; assay at
5
-
recombinant enzyme
5
-
assay at
5 - 5.5
-
full-length and mutant enzyme forms
5 - 6
Clostridium stercorarium
-
-
5.5
pH-optimum for domain GH5
5.5
-
assay at
5.5 - 5.7
-
exo I
5.5 - 6
M55080
-
5.5 - 6.5
-
avicel
5.7
-
assay at
6.8 - 7.8
-
-
additional information
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 6
-
recombinant enzyme, activity range, 76% of maximal activity at pH 3..0, inactive at pH 7.0, profile overview
3 - 6
about 65% activity at pH 3.0, 71% activity at pH 5.0, 23% activityat pH 6.0
4 - 7
-
82% and 79% of the maximum activity at pH 4.0 and and pH 6.0
4.5 - 5.5
-
90% and 93% of the maximum activity appearing at pH 4.5 and 5.5
5 - 7
-
optimum at pH 5, drop of activity between pH 6 and pH 7 to about 30% of the maximal activity
5 - 7.5
-
pH 5: 50% of maximal activity, pH 7.5: 25% of maximal activity at
5 - 7.5
-
more than 50% activity between pH 5.0 and 7.5
5.1 - 9
-
50% of maximal activity
additional information
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
avicel
37
-
assay at
40
-
assay at
44
-
assay at
46
-
isoform CBHII
50
-
cellulose
50
-
assay at
50
-
assay at; assay at
50
-
assay at
50
-
recombinant enzyme
50
-
assay at
50 - 60
Geotrichum sp.
-
52
-
isoform CBHI
55
M55080
optimum activity around 55C, followed by a sharp decline at temperatures above 60C
55 - 70
-
thermophilic fungi
60
-
activity decreases rapidly at temperatures over 60C
66 - 69
-
CBHIB isoform
68
-
CBHII isoform
70
Clostridium stercorarium
-
-
78
-
CBHIA isoform
80
temperature optimum for domain construct CBM3-GH5
80 - 90
temperature optimum for domain GH5
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 70
-
recombinant enzyme, activity range, profile overview
23 - 60
-
10% of maximal activity
30 - 50
about 45% activity at 30C, about 19% activity at 50C
30 - 55
-
about 60% activity at 30C, about 55% activity at 35C, about 80% activity at 40C, about 75% activity at 45C, 100% activity at 50C, about 40% activity at 55C, and almost no activity at 60C
45 - 55
-
80% and 95% of the maximum activity appearing at 45C and 55C
60 - 70
-
60C: optimum, 70C: appreciable amount of activity
additional information
-
thermodynamics and kinetics of the immunoglobulin-like module/catalytic module pair, wild-type and mutant enzymes, overview
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.8
-
isoelectric focusing, Cel7A
3.9
-
isoelectric focusing
4
-
pI around 4, isoelectric focusing
4.5
-
full-length and mutant enzyme forms
4.7
-
calculated from amino acid sequence
4.8
-
isoelectric focusing
4.9
-
isoelectric focusing, pH gradient pH 3.5-9.5, CBHIA isoform
4.9
calculated from amino acid sequence
5.1
-
isoelectric focusing
5.6
-
isoelectric focusing, Cel6A
6
Geotrichum sp.
-
6
-
isoelectric focusing, pH gradient pH 3.5-9.5, CBHII isoform
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
commercial enzyme blend, Spezyme CP; commercial enzyme blend, Spezyme CP
Manually annotated by BRENDA team
Fomitopsis pinicola KMJ812
-
-
-
Manually annotated by BRENDA team
Fomitopsis pinicola KMJ812
-
-
-
Manually annotated by BRENDA team
Fomitopsis pinicola KMJ812
-
-
-
Manually annotated by BRENDA team
Piptoporus betulinus CCBAS585
-
-
-
Manually annotated by BRENDA team
; secretion into gut for wood degradation
Manually annotated by BRENDA team
additional information
-
cells are produced on steam-treated spruce, willow, and corn stover, with delignified lignocellulose as a reference, effects on enzyme activity, corn stover is the preferred substrate and carbon source, overview
Manually annotated by BRENDA team
additional information
Trichoderma reesei RUT C30
-
cells are produced on steam-treated spruce, willow, and corn stover, with delignified lignocellulose as a reference, effects on enzyme activity, corn stover is the preferred substrate and carbon source, overview
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bacillus pumilus (strain SAFR-032)
Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
Clostridium thermocellum
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Thermobifida fusca (strain YX)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22000
-
gel filtration
393787
40000
-
gel filtration
393770
41800
-
sedimentation equilibrium analysis
393763
42000
-
gel filtration
393740
43720
sequence analysis
695369
45000
gel filtration; gel filtration/multiangle laser light scattering
732818
46000
-
chromatography of reduced and alkylated enzyme
393764
46300
-
isozyme I, gel filtration
393756
46300
-
gel filtration
393760
46500
calculated
732818
46900
sequence analysis
696875
47100
sequence analysis
696875
47500
-
estimated from amino acid sequence
677386
47500
-
SDS-PAGE
679574
50000
-
isozyme II, gel filtration
393754
50000
-
SDS-PAGE
655382
50300
-
light scattering
393749
50700
-
isozyme II, gel filtration
393756
52500
-
gel filtration
393786
53700
sequence analysis
696875
54600
sequence analysis
696875
55000
-
SDS-PAGE
677761
56000
SDS-PAGE
677289
56240
-
SDS-PAGE, CBHII isoform
654836
56330
-
SDS-PAGE, CBHIB isoform
654836
57000
-
isozyme I, gel filtration
393754
60000
-
gel filtration
393785
60000
-
SDS-PAGE, Cel7A
678850
61000
-
gel filtration
713792
62000 - 68000
-
gel filtration
326313
62000 - 68000
-
gel filtration
393744
64000
-
II, gel filtration
393746
64000
-
gel filtration
393747
64000
-
gel filtration
715879
65000
-
gel filtration
393739
66000
-
SDS-PAGE
677286
66000
-
-
701209
66100
-
SDS-PAGE, CBHIA isoform
654836
70000
-
SDS-PAGE, Cel6A
678850
75240
-
calculated from nucleic acid sequence
656720
79000
-
SDS-PAGE
654177
81900
-
estimated from amino acid sequence
674279
84000
-
isozyme I, gel filtration
393746
97000
Geotrichum sp.
SDS-PAGE
646831
118000
calculated from amino acid sequence
655460
122000
SDS-PAGE
655460
200000
-
gel filtration
393758
230000
-
gel filtration
393768
additional information
-
-
393752
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 72000, SDS-PAGE
?
-
x * 81000, SDS-PAGE
?
-
x * 75000, SDS-PAGE
?
-
CBH I, x * 128000, SDS-PAGE
?
-
CHH II, 53000, SDS-PAGE
?
-
x * 58000, SDS-PAGE
?
Clostridium stercorarium
-
x * 87000, SDS-PAGE
?
-
x * 75000, SDS-PAGE
?
x * 50000-60000, recombinant enzyme, SDS-PAGE
?
-
x * 65000, full-length enzyme form 1, SDS-PAGE, x * 52000, truncated catalytic core enzyme form 2, SDS-PAGE
?
-
x * 60000, recombinant Ex-1, SDS-PAGE, x * 54733, Ex-1, amino acid sequence calculation
?
x * 48951, SDS-PAGE
?
-
x * 50000, SDS-PAGE
?
-
x * 40000, SDS-PAGE of Ex-4 purified from commercial driselase, x * 60000, SDS-PAGE of purified recombinant Ex-4
?
x * 52500, calculated from amino acid sequence
?
x * 50000, SDS-PAGE
?
M55080
x * 60000-63000, recombinant enzyme from Yarrowia lipolytica , SDS-PAGE, x * 65000, recombinant His-tagged enzyme from Pichia pastoris , SDS-PAGE
?
-
x * 53950, calculated from amino acid sequence
?
Coprinopsis cinerea 5338
-
x * 48951, SDS-PAGE
-
?
Heterobasidion irregulare TC-32-1
-
x * 50000, SDS-PAGE
-
?
Irpex lacteus MC-2
-
x * 40000, SDS-PAGE of Ex-4 purified from commercial driselase, x * 60000, SDS-PAGE of purified recombinant Ex-4
-
?
Neocallimastix patriciarum J11
-
x * 53950, calculated from amino acid sequence
-
?
Penicillium occitanis CL100
-
x * 52500, calculated from amino acid sequence
-
?
-
x * 60000-63000, recombinant enzyme from Yarrowia lipolytica , SDS-PAGE, x * 65000, recombinant His-tagged enzyme from Pichia pastoris , SDS-PAGE
-
dimer
-
2 * 100000, SDS-PAGE
dimer
-
2 * 118000, SDS-PAGE
monomer
-
carboxymethylated derivative
monomer
-
1 * 66100, CBHIA isoform, 1 * 56330, CBHIB isoform, 1 * 56420, CBHII isoform, SDS-PAGE
monomer
-
1 * 60000, SDS-PAGE
monomer
-
1 * 64000, SDS-PAGE
monomer
1* 45000, SDS-PAGE
monomer
Fomitopsis pinicola KMJ812
-
1 * 64000, SDS-PAGE
-
monomer
Penicillium purpurogenum KJS506
-
1 * 60000, SDS-PAGE
-
additional information
-
structure-reactivity studies of wild-type enzyme and mutants E212Q, D214N, and E217Q, preparation of enzyme catalytic core domains of wild-type and mutant enzymes by papain treatment
additional information
-
peptide sequencing of Cel7A and CBH I
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
additional information
-
has a multi domain structure composed of a cellulose-binding domain, a Ser/Thr/Pro-rich linker, and a catalytic domain belonging to family 6 of glycosyl hydrolases, from the N-terminus
additional information
-
identification of enzyme peptides by mass spectrometry; identification of enzyme peptides by mass spectrometry
additional information
-
structural model of the Cel6B catalytic domain, structure comparisons to other exocellulases, overview
additional information
-
enzyme molecular surface and structure analysis, overview
additional information
Irpex lacteus MC-2
-
has a multi domain structure composed of a cellulose-binding domain, a Ser/Thr/Pro-rich linker, and a catalytic domain belonging to family 6 of glycosyl hydrolases, from the N-terminus
-
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
-
additional information
-
enzyme molecular surface and structure analysis, overview
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
CBH I: 10.7% reducing sugar, CBH II 8.2% reducing sugar
glycoprotein
-
8-16% reducing sugar
glycoprotein
-
-
glycoprotein
-
alpha-linked mannose and N-linked glycolysation
glycoprotein
-
Ex-1 contains two putative N-glycosylation sites, O-linked carbohydrates may also occur, glycosyl chains stabilize but are not essential for activity
proteolytic modification
-
a putative N-terminal 18 amino acid signal peptide is removed
glycoprotein
-
8% reducing sugar
glycoprotein
Penicillium occitanis CL100
-
-
-
glycoprotein
-
-
glycoprotein
-
-
glycoprotein
-
36-38% carbohydrate content
glycoprotein
-
predicted N-glycosylation sites at N126, N283 and N397 and the O-glycosylated linker, structure, overview
glycoprotein
-
predicted N-glycosylation sites at N126, N283 and N397 and the O-glycosylated linker, structure, overview
-
glycoprotein
-
CBH 1, 9% reducing sugar, CBH 1a 33% reducing sugar
glycoprotein
-
-
glycoprotein
-
74% of the glycans found on Asn310 are high mannose, predominantly Hex7-9-N-acetylglucosamine-2, whereas the remaining amount was single N-acetylglucosamine. Asn289 has 18% single N-acetylglucosamine occupancy and Asn145 remains unoccupied
glycoprotein
M55080
deglycosylation of the recombinant enzyme does not radically alter the specific activity
glycoprotein
-
deglycosylation of the recombinant enzyme does not radically alter the specific activity
-
glycoprotein
-
attached carbohydrate in addition to glycoprotein constituents
glycoprotein
Trichoderma viride QM 9414
-
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 20% (w/v) polyethylene glycol 6000, 0.1 M HEPES pH 7.0, 0.14 M lithium chloride
by the hanging-drop vapour-diffusion method, to 1.6 A resolution. Square prismatic crystal belongs to the triclinic space group P1, with unit-cell parameters a=44.04, b=45.11, c=48.90 A, alpha=77.81, beta=87.34, gamma=68.79
hanging drop vapor diffusion method
Geotrichum sp.
-
hanging drop vapor diffusion method, apoenzyme using 20 mM MgCl2, 0.1 M HEPES, pH 7.5, 22% (w/v) polyacrylic acid 5100 sodium salt, or in complex with thio-beta-D-xylopentaose using 20mM MgCl2, 0.1 M HEPES, pH 7.7, 15-22% (w/v) polyethylene glycol 3350
D416A mutant, hanging drop vapor diffusion method, complexed with methyl cellobiosyl-4-thio-beta-cellobioside
-
wild-type and mutant forms in complex with nonhydrolyzable thio-oligosaccharides, hanging drop vapor diffusion method
-
apo form at 1.6 A resolution, and three ligand bound complexes ranging from 1.9 A to 1.14 A resolution. Enzyme exhibits an extended substrate-binding motif at the tunnel entrance, which may aid in substrate acquisition and processivity. Enzyme stability and activity remain unchanged, or increase at high salt concentration; vapor diffusion method, using 0.1 M CH3CO2Na pH 4.5, 15% (w/v) PEG 6000 and 0.5 M CaCl2
Cel7B free and in complex with cellobiose, cellotriose, and cellotetraose, at high resolution (1.6-2.1 A). Cel7B crystals are pseudo-merohedrally twinned and belong to space group P21, with unit cell dimensions of a=50.9 A, b=94.5 A, c=189.8 A, beta=90.0. The loops extending from the core beta-sandwich structure form a long tunnel composed of multiple subsites for the binding of the glycosyl units of a cellulose chain
hanging drop vapour diffusion method with 12% PEG 8000, 0.1 M sodium cacodylate pH 6.5 and 0.1 M calcium chloride
-
deglycosylated Cel7D complexed with cellobiose, or with inhibitors cellobioimidazole, lactose, or methyl (4S)-beta-cellobiosyl-4-thio-beta-cellobioside, hanging drop vapour diffusion method, 18 mg/ml protein in 10 mM Tris-HCl, pH 7.0, 5 mM CaCl2, 15-22.5% PEG 5000, and 12% glycerol, soaking of crystals in ligand solution containing 10 mM ligand, X-ray diffraction structure determination and analysis at -173C and 1.7-1.8 A resolution
catalytic domain in complex with cellohexaose and cellobiose
-
Ig-GH9 CbhA: immunoglobulin-like module and the catalytic module, and Ig-GH9 CbhA-(E795Q) mutant in complex with cellotetraose
-
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
-
hanging drop vapor diffusion method, using 20% (w/v) polyethylene glycol 6000, 0.1 M sodium citrate (pH 4.0) and 1 M lithium chloride
bound to cellononaose, hanging drop vapor diffusion method
catalytic domain, cocrystallized with the (S)-enantiomer of the beta-blocker propranolol
-
engineered enzymes
-
hanging drop vapor diffusion method
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 7
-
4C, 24 h, CBH II
393743
2 - 7
-
enzyme is stable at pH 3-7 at 37C, but loses 90% of activity at pH 2 after 20 min
654486
2.5 - 6
-
4C, 24 h, CBH I
393743
3 - 10
-
6C, 48 h
393747
3 - 5
-
native Ex-1
665332
3 - 8
-
recombinant Ex-1
665332
3 - 8
-
retains 80% activity when incubated for 60 min at 60C
696830
3 - 9
-
-
677761
3.5 - 5.6
-
optimal stability, gradual decrease in stability at more alkaline pH values
655473
3.5 - 9.5
-
-
326320
4 - 8
Geotrichum sp.
90% activity at 45C
646831
4.5 - 5
-
highest stability
393740
4.5 - 7
-
-
393785
5.2 - 11.3
-
the enzyme is stable over a wide range of pH 5.2-11.3 after 1 h incubation (more than 70% activity remaining)
732870
5.5 - 6
M55080
purified recombiant enzymes, 100% stable in the range pH 5-6, undergoing rapid inactivation at alkaline pH and showing some instability below pH 5
732493
5.5 - 8
-
25C, 24 h
393738
5.5 - 8
-
highest stability
393758
5.5 - 8.4
-
stable at 4C for 48 h
654177
6
-
complete loss of activity below pH 6 at 60C for 48 h
654177
6
-
wild-type enzyme is more stable than E107Q and E107Q/D170N/D366N mutants
654671
6 - 8.4
-
stable at 60C for 5 h, stability decreases with incubation time above 5 h
654177
8
-
wild-type enzyme is less stable than E107Q and E107Q/D170N/D366N mutants
654671
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
-
3 hours
393734
40
M55080
purified recombiant enzymes, 30 min, good stability up to 40C
732493
40 - 70
-
the enzyme maintains about 90% activity when incubated at 60C for 24 h. About 90% activity is maintained after 8 h of incubation at 70C. At temperatures over 80C, the enzyme activity sharply decreases depending on the incubation time. The enzyme shows half-life values of 552 h, 144 h, 96 h, and 42 h at 40C, 50C, 60C, and 70C, respectively
715879
50
-
-
393785
50
Geotrichum sp.
90% activity after 10 min at pH 4
646831
50
-
enzyme retains full activity between pH 4 and 6, but is rapidly inactivated at lower pH values
654486
50
-
24 h, stable, full-length and mutant enzyme forms
664783
50 - 60
-
unstable at temperatures lower than 50C, retains about 80% of its activity after a 30 min incubation at 50C and is completely inactivated after a 30 min pre-incubation at or above 60C
677761
55 - 70
-
thermal unfolding behavior of Th Cel7A is found to be a two-step process at pH 5.0. The first step leads to the formation of molten globule-like states between 55C and 65C, followed by a second step that was due to the unfolding of the molten globule-like state at temperatures above 70C
731737
60
-
pH 5.5, 10 min, complete loss of activity
393739
60
-
stable for 10 min
393747
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
654263
60
-
7 h, 90% remaining activity of the full-length enzyme form
664783
60
-
retains 80% activity when incubated for 60 min in buffers at pH 3-8
696830
60
-
the enzyme shows a half-life of 72 h, 46 h, 22 h, 4 h, and 0.5 h at 30C, 40C, 50C, 60C, and 70 C, respectively
713792
60
M55080
purified recombiant enzymes, loss of 50% of the initial activity after 30 min
732493
60 - 70
-
the enzyme maintains approximately 50% of the maximum activity in response to the treatment at 60-70C for 1 h
732870
65
-
stable for 5 min
326320
65
-
60% loss of activity after 10 min /CBH I
393743
65
-
3 h, 50% remaining activity of the full-length enzyme form
664783
65
-
the enzyme is not active at temperatures higher than 65C
716818
70
-
CHB II: 40% loss of activity after 10 min
393743
70 - 80
the recombinant GH5 and CBM3-GH5 constructs are both stable at 80C with half-lives of 23 h and 39 h, respectively, and retain more than 94% activity after 48 h at 70C. The melting temperature of domain GH5 is at 89C, while the melting temperature of the domain construct CBM3-GH5 is at 80C
714507
75
-
the wild type enzyme is inactive at 75C
731514
75
-
the wild type enzyme shows a half-life of more than 2.5 min at 75C and T50 of 65.2C
731514
75
-
the wild type enzyme shows a half-life of more than 2.5 min at 75C and T50 of 60.2C
731514
78
-
complete denaturation after 3 min
393763
80
-
50% loss of activity after 3 hours
393734
80
-
t1/2 CBHIA: 34 min, t1/2 CBHIB: 68 min, t1/2 CBHII: 38 min at pH 5
654836
90
-
the enzyme is inactivated after 15-minute incubation at 90C and pH 7.0
731342
100
-
95% loss of activity after 10 min
393739
100
-
5 min, loss of 50% of activity of the purified recombinant enzyme
663568
additional information
-
the full-length enzyme form is more thermostable than the truncated mutant enzyme form
664783
additional information
-
irreversible thermal unfolding kinetics of recombinant enzyme domains, overview
664959
additional information
-
thermal unfolding kinetics of wild-type and mutant enzymes, overview
666803
additional information
-
the Trichoderma reesei produced fusion protein Cel7B-CBM has 2.5C improved unfolding temperature when compared to the Trichoderma reesei produced catalytic module (Cel7B wild-type)
695830
additional information
-
cellobiose-binding influences the enzyme's thermal stability
731737
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol stabilizes
-
freezing and thawing, stable
-
bovine serum albumin stabilizes
-
ribonuclease stabilizes
-
dilute solutions, unstable
-
Ca2+ and cysteine stabilizes
-
freezing and thawing, stable
-
cellotetraose stabilizes the protein fold
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C, pH 4.5, 50 mM citrate buffer
-
-20C, concentrated solutions, several months
-
0-4C, 0.05 M acetate buffer, pH 5.0, at least 2 weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni2+ affinity column chromatography
-
on affinity column and by gel filtration
overexpressed in Escherichia coli
-
Ni2+-NTA column chromatography and HiTrap Q HP anion-exchange column chromatography
gene cloned in Escherichia coli
-
Ni-NTA column chromatography
-
Ni2+ affinity column chromatography
-
on affinity column and by gel filtration
Q Sepharose column chromatography, MonoQ column chromatography, and Sephadex G-25 gel filtration
Source 15Q column chromatography
-
avicellase II
Clostridium stercorarium
-
DEAE Sepharose column chromatography, Sephacryl S-300 gel filtration, and Mono Q column chromatography
-
-
Geotrichum sp.
anion exchange column chromatography and gel filtration
His-Trap column chromatography
-
homogeneity
-
Ni-NTA column chromatography
-
polypeptide of recombinant Ex-4 from day-3 culture fluid purified by affinity binding toward insoluble phosphoric acid swollen cellulose, to apparent homogeneity
-
secreted recombinant Ex-1 from Aspergillus oryzae culture fluid by ammonium sulfate fractionation, cellulose adsorption chromatography, and gel filtration
-
Q-Trap column chromatography
DEAE Sepharose FF column chromatography
-
wild-type and mutants purified with one-step purification using gel filtration
-
Ni-NTA agarose column chromatography and T7-tag antibody agarose column chromatography
-
DEAE-Sepharose column chromatography, Mono Q column chromatography, and Sephacryl S-300 gel filtration
-
HiTrap phenyl column chromatography and Superdex 200 gel filtration
-
Ni-NTA column chromatography
-
Ni2+ affinity column chromatography
-
three forms: CBHIA, CBHIB and CBHII, homogeneity
-
Ni-IDA resin column chromatography and Superdex 75pg gel filtration
-
Ni-NTA column chromatography, Source 15S column chromatography, and Superdex 75 gel filtration
-
recombinant enzyme and truncated versions, homogeneity
-
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
-
nickel-NTA resin column chromatography
-
High Trap DEAE column chromatography
Ni2+ affinity column chromatography
-
on affinity column and by gel filtration
recombinant wild-type Cel6B and mutant enzymes from Escherichia coli strain BL21(DE3) by hydrophobic interaction and anion exchange chromatography
-
Source 30Q column chromatography
Superdex 75 gel filtration and Mono-Q column chromatography
-
Bio-Gel P-6 gel filtration, DEAE-Sepharose column chromatography and phenyl Sepharose column chromatography
-
CBH I and CBH II
-
cloned in Escherichia coli
-
DEAE Sepharose column chromatography
-
extracellular Cel5A, Cel6A, and Cel7A from culture medium
-
His-Trap column chromatography
-
HiTrap phenyl column chromatography and Superdex 200 gel filtration
-
native enzyme from commercial enzyme blend, Spezyme CP by ammonium sulfate fractionation, anion exchange chromatography, and p-aminophenyl-1-thio-beta-D-cellobioside-based affinity chromatography; native enzyme from commercial enzyme blend, Spezyme CP by ammonium sulfate fractionation, anion exchange chromatography, and p-aminophenyl-1-thio-beta-D-cellobioside-based affinity chromatography
-
Ni-NTA column chromatography
-
Ni2+ affinity column chromatography
-
on affinity column and by gel filtration
-
Q-Sepharose Fast-Flow column chromatography and Mono Q column chromatography
-
recombinant enzyme 2.5fold from Yarrowia lipolytica by ultrafiltration and cation exchange chromatography, recombinant His-tagged enzyme 4.4fold from Pichia pastoris strain X-33 by metal affiity chromatography
M55080
recombinant family 1 cellulose binding modules CBMCel7A and CBMCel6A from Escherichia coli
-
wild-type and mutants
-
HiTrap Q HP column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae strain YDR483W
-
wild-type Cel7A expressed in Trichoderma reesei; wild-type Cel7B expressed in Trichoderma reesei
expressed in Pichia pastoris
-
expressed in Escherichia coli
cloned in Saccharomyces cerevisiae, cloned in Escherichia coli
-
expressed in Aspergillus oryzae JaL250 cells
expressed in Saccharomyces cerevisiae strain YDR483W
-
expressed in Saccharomyces cerevisiae strain YDR483W BY4742
-
wild-type Cel7A expressed in Trichoderma reesei
gene cbh1, DNA and amino acid sequence determination
-
expressed as a C-terminal His6-tag in Escherichia coli
expressed in Escherichia coli
Geotrichum sp.
expressed in Aspergillus oryzae
-
expressed in Saccharomyces cerevisiae strain YDR483W BY4742
-
full-length cel4 cDNA expressed in Pichia pastoris strain X-33 using vector pPICZalphaA
-
gene cel2, expression of Ex-1 in Aspergillus oryzae, secretion of the recombinant enzyme to the culture fluid
-
expressed in Aspergillus oryzae and Aspergillus niger; expression in Aspergillus oryzae and Aspergillus niger
expressed in Saccharomyces cerevisiae strain NY179
-
wild-type and mutants expressed in Saccharomyces cerevisiae strain INVSc1. Cel7B wild-type and a two-module version containing as a C-terminal fusion the linker and cellulose-binding module (CBM) of Trichoderma reesei Cel7A expressed in Trichoderma reesei strain A36
-
expressed in Escherichia coli Rosetta-gami B (DE3) cells
-
functional expression of Cel9B and Cel48C in Escherichia coli
-
expressed in Saccharomyces cerevisiae strain H158
gene cbhl.2, expression in Escherichia coli strain XL 1-Blue in membranes and inclusion bodies
-
gene cbhl.2, genomic library construction, DNA and amino acid sequence determination and analysis, expression of inactive enzyme in Escherichia coli strain XL 1-Blue in membranes and inclusion bodies
-
expressed in Saccharomyces cerevisiae
-
expressed in Saccharomyces cerevisiae strain YDR483W
-
expressed in yeast strain YDR483W BY4742
-
3 truncated forms: Gh9, Gh9-Fn31,2, Gh9-Fn31,2-CBDIII
-
cloned in Escherichia coli
-
expressed in Escherichia coli BL21 cells
-
expressed in Escherichia coli strain BL21(DE3)
-
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)
-
native enzyme and truncated versions
-
expressed in Escherichia coli
-
expressed in Kluyveromyces lactis strain DELTActs1
expressed in Saccharomyces cerevisiae strain YDR483W
-
wild-type Cel7A, Cel7A genetically linked to the linker and carbohydrate-binding module of Trichoderma reesei Cel7A or to the linker and carbohydrate-binding module of Chaetomium thermophilum Cel7A expressed in Trichoderma reesei
cloning in Escherichia coli strain DH5alpha, expression of wild-type and mutant enzymes in Escherichia coli strain BL21 RPIL DE3
-
expressed in Nicotiana tabacum chloroplasts
-
expressed in Streptomyces lividans
expression of wild-type Cel6B and mutant enzymes in Escherichia coli strain BL21(DE3)
-
expressed in Aspergillus niger
-
cloned in Escherichia coli
-
expressed in Escherichia coli
-
expressed in Escherichia coli strain DH5alpha
-
expressed in Fusarium venenatum
-
expressed in Saccharomyces cerevisiae
-
expressed in Saccharomyces cerevisiae strain CEN.PK102-3A
-
expressed in Saccharomyces cerevisiae strain YDR483W
-
expressed in Saccharomyces cerevisiae strain YDR483W BY4742
-
gene cbh2, expression under control of the cbh1 strong promoter in Trichoderma reesei via optimized Agrobacterium tumefaciens AGL-1-mediated transformation, 324 transformants are screened, C10 has the highest activity
-
gene cbh2, recombinant expression of His-tagged enzyme in Pichia pastoris strain X-33 under the control of the AOX1 promoter, cloning and recombinant expression in Yarrowia lipolytica strain Po1d under the control of the POX2 or TEF promoters, and using either the native or preproLip2 secretion signals. The expression level of cellobiohydrolase from the TEF-preproLip2-cbhII cassette is higher in Yarrowia lipolytica than in Pichia pastoris
M55080
recombinant expression of family 1 cellulose binding modules CBMCel7A and CBMCel6A in Escherichia coli
-
the cellulose-binding domain 2 of CBHII is fused to the beta-glucosidase enzyme from Saccharomycopsis fibuligera and expressed in Saccharomyces cerevisiae strain CENPK42
-
wild-type Cel7A expressed in Trichoderma reesei
-
expressed in Escherichia coli XL-1 Blue cells; expressed in Escherichia coli XL-1 Blue cells; expressed in Escherichia coli XL-1 Blue cells
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Y466A
the mutation greatly reduces the cellulose-binding ability
Y492A
the mutation greatly reduces the cellulose-binding ability
Y493A
the mutation greatly reduces the cellulose-binding ability
A385P
-
the mutant shows a T50 value of 64.7C
C313S
-
random mutagenesis, the mutation causes increased thermostability of the mutant enzyme compared to the wild-type, with decreased inactivation, increased maximum Avicel hydrolysis temperature, and improved long time hydrolysis performance
D405A
-
about 1% enzyme activity
D405N
-
only small structural changes, about 1% enzyme activity
D416A
-
active center N-terminal loop has a more open conformation
D416A
-
crystal structure similar to wild-type enzyme, mutant retains about 10% of wild-type activity
M235P
-
the mutant shows a T50 value of 63.1C
Q390P
-
the mutant shows a T50 value of 66.1C
S215P
-
the mutant shows a T50 value of 65.6C
A163T
-
improved thermostability
A30T
-
mutant shows improved unfolding temperature by 1.5C compared to the wild type enzyme (64.5C)
A3D
-
improved thermostability
D411G
-
improved thermostability
G184D
-
mutant has higher specific activity and shows wild type unfolding temperature (64.5C)
G346D
-
improved thermostability
G386V
-
improved thermostability
G4C/M70C
-
disulfide bridge mutation located near the N-terminus, close to the entrance of the active site tunnel of Cel7B, which leads to improved thermostability. The unfolding temperature is increased by 2.5C compared to that of the wild-type. The mutant has increased activity towards microcrystalline cellulose (avicel) at 75C
G4C/M70C/S290T
-
thermostability-increasing mutation together with disulfide bridge mutation, the unfolding temperature is increased by 4C compared to that of the wild-type, additive effect on thermostability. The mutant has increased activity towards microcrystalline cellulose (avicel) at 75C
G75D
-
improved thermostability
P114T
-
improved thermostability
R166Q
-
improved thermostability
S290T
-
mutant has slightly lower specific activity and shows improved unfolding temperature by 3.5C compared to the wild type enzyme (64.5C)
S290T
-
can hydrolyse crystalline cellulose at 70C 2fold more effectively than the wild-type, the unfolding temperature is increased by 1.5C compared to that of the wild-type
T56S
-
improved thermostability
Y100N
-
improved thermostability
C313S
-
random mutagenesis, the mutation causes increased thermostability of the mutant enzyme compared to the wild-type, with decreased inactivation, increased maximum Avicel hydrolysis temperature, and improved long time hydrolysis performance
E217Q
inactive mutant
A383Y
-
the mutation increases stability and results in a 10C increase in the optimal temperature for activity, to 65C, and a 50% increase in total sugar production from crystalline cellulose compared to the wild type
D354V
-
the mutation increases stability and results in a 10C increase in the optimal temperature for activity, to 65C, and a 50% increase in total sugar production from crystalline cellulose compared to the wild type
H208Y
-
the mutation increases stability and results in a 10C increase in the optimal temperature for activity, to 65C, and a 50% increase in total sugar production from crystalline cellulose compared to the wild type
N93K
-
the mutation increases stability and results in a 10C increase in the optimal temperature for activity, to 65C, and a 50% increase in total sugar production from crystalline cellulose compared to the wild type
S324P
-
the mutation increases stability and results in a 10C increase in the optimal temperature for activity, to 65C, and a 50% increase in total sugar production from crystalline cellulose compared to the wild type
T392I
-
the mutation increases stability and results in a 10C increase in the optimal temperature for activity, to 65C, and a 50% increase in total sugar production from crystalline cellulose compared to the wild type
Y430F
-
the mutation increases stability and results in a 10C increase in the optimal temperature for activity, to 65C, and a 50% increase in total sugar production from crystalline cellulose compared to the wild type
Y60L
-
the mutation increases stability and results in a 10C increase in the optimal temperature for activity, to 65C, and a 50% increase in total sugar production from crystalline cellulose compared to the wild type
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
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
-
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
-
D226A
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme. The D226A enzyme has a very low activity on insoluble cellulose, not improved by sodium azide
D226A/S232A
-
site-directed mutagenesis, the mutant is almost inactive and shows slightly decreased ligand binding compared to the wild-type enzyme
D274A
-
site-directed mutagenesis, the mutant shows altered and highly reduced substrate specificity compared to the wild-type enzyme
D497A
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
D512A
-
site-directed mutagenesis, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
E495A
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
L230A
-
site-directed mutagenesis, the mutation causes slightly increased processivity and increased activity with phosphoric acid-treated cotton over 250%, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
M514A
-
site-directed mutagenesis, the mutation alters the secondary structure of the enzyme, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
N282A
-
site-directed mutagenesis, mutation in residue near the tunnel entrance causes a twofold increase in processivity, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
N282D
-
site-directed mutagenesis, mutation in residue near the tunnel entrance causes a twofold increase in processivity, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
R180A
-
site-directed mutagenesis, mutation in residue near the tunnel exit causes a twofold increase in processivity, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
R180K
-
site-directed mutagenesis, mutation in residue near the tunnel exit causes a twofold increase in processivity, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
S232A
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme. The S232A enzyme retains near wild-type activity on most substrates, but carboxymethylcellulose activity is drastically reduced
W464A
-
site-directed mutagenesis, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
W464Y
-
site-directed mutagenesis, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
Y220A
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme, alomost inactive mutant
C313S
-
random mutagenesis, the mutation causes increased thermostability of the mutant enzyme compared to the wild-type, with decreased inactivation, increased maximum Avicel hydrolysis temperature, and improved long time hydrolysis performance. The C313S mutation increases total Humicola jecorina CBH II activity secreted by the Saccharomyces cerevisiae expression host more than 10fold
D175A
-
mutant retains some activity on longer oligosaccharides
D214N
-
impaired catalytic activity
D214N
-
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
D221A
-
almost complete loss of activity
D241C/D249C
-
thermostability similar to wild-type enzyme
DELTAG245-Y252
-
reduced thermostability
E107Q
-
mutant enzyme is destabilized at acidic pH and stabilized at alkaline pH
E107Q/D170N/D366N
-
mutant enzyme is destabilized at acidic pH and stabilized at alkaline pH
E212Q
-
impaired catalytic activity
E212Q
-
no enantioselectivity
E212Q
-
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
E217Q
-
impaired catalytic activity
E217Q
-
stability similar to wild-type enzyme, catalytically inactive
E217Q
-
no enantioselectivity
E217Q
-
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
E223S/A224H/L225V/T226A/D262G
-
mutant has a more alkaline pH optimum
E223S/A224H/L225V/T226A/D262G
-
mutant has a more alkaline pH optimum, mutation destabilizes the protein fold at both acidic and alkaline pH
Q276L
-
the mutant shows a T50 value of 58.6C
S30F
-
the mutant shows a T50 value of 60.3C
S316P
-
the mutant shows a T50 value of 61.9C
S406P
-
the mutant shows a T50 value of 61.5C
S413P
-
the mutant shows a T50 value of 63.8C
W272A
-
mutant
W272D
-
mutant
W40A
-
the mutation causes a loss of crystalline cellulose-degrading ability. The mutant shows reduced specific activity for crystalline cellulose and diffused the cellulose chain from the entrance of the active site tunnel
Y169F
-
mutant
Y247F
-
slight reduction of kcat on 4-nitrophenyl lactoside, but only a small effect on cellulose hydrolysis
Y31A
-
structural role minor, but does not bind strongly to cellulose
Y32A
-
structural role minor, but does not bind strongly to cellulose
Y5A
-
complete loss of binding affinity to cellulose
W40A
Trichoderma reesei ALKO 3413
-
the mutation causes a loss of crystalline cellulose-degrading ability. The mutant shows reduced specific activity for crystalline cellulose and diffused the cellulose chain from the entrance of the active site tunnel
-
E217Q
Trichoderma reesei ALKO2877
-
stability similar to wild-type enzyme, catalytically inactive
-
E223S/A224H/L225V/T226A/D262G
Trichoderma reesei ALKO2877
-
mutant has a more alkaline pH optimum, mutation destabilizes the protein fold at both acidic and alkaline pH
-
D214N
Trichoderma reesei CBH I
-
impaired catalytic activity
-
E212Q
Trichoderma reesei CBH I
-
impaired catalytic activity
-
E217Q
Trichoderma reesei CBH I
-
impaired catalytic activity
-
W272A
Trichoderma reesei Cel6A
-
mutant
-
W272D
Trichoderma reesei Cel6A
-
mutant
-
additional information
-
construction of the recombinant Cex-RsaA fusion mutant by fusion of the C-terminus of Caulobacter crescentus surface (S)-layer protein RsaA with the beta-1,4-glycanase Cex from the cellulolytic bacterium Cellulomonas fimi, the RsaA C-terminus causes a spontaneous unstructured aggregation of the recombinant protein
additional information