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 ACCESSION NO.
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
Q7LIJ0
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
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
cellulose degradation II (fungi)
-
Metabolic pathways
-
Starch and sucrose metabolism
-
SYSTEMATIC NAME
IUBMB Comments
4-beta-D-glucan cellobiohydrolase (non-reducing end)
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
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
Hypocrea pseudokoningii S-38
-
-
-
1,4-beta-D-glucan-cellobiohydrolase I
-
-
1,4-beta-D-glucan-cellobiohydrolase I
Hypocrea 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
Q6E5B1, Q6E5B2, Q6E5B3
-
CBH 1
-
-
-
-
CBH I
P62694
-
CBH I
Hypocrea pseudokoningii S-38
-
-
-
CBH Ib
Chrysosporium lucknowense UV18-25
-
-
-
CBH II
-
-
-
-
CBH II
P07987
-
CBH IIb
Chrysosporium lucknowense UV18-25
-
-
-
CBH1
Penicillium chrysogenum FS010
Q5S1P9
-
-
CBH1
Trichoderma sp.
-
-
CBH2
Trichoderma sp.
-
-
CBHI
-
-
-
-
CBHI
-
Cel7A
CBHI
Hypocrea pseudokoningii S-38
-
-
-
CBHI
Penicillium occitanis CL100
Q68HC2
-
-
CBHII
-
-
-
-
CBHII
-
Cel6A
CBM3-GH5
A4XIF7
recombinant enzyme domain construct
CBP120
-
-
-
-
CBP95
-
-
-
-
Cel48C
Paenibacillus sp. BP-23
-
-
-
Cel6A
-
-
-
-
Cel6A
Saccharophagus degradans 2-40T
-
-
-
Cel6B
Chrysosporium lucknowense UV18-25
-
-
-
Cel6B
Trichoderma sp.
-
-
Cel6C
B7X9Z2
-
Cel6C
Coprinopsis cinerea 5338
B7X9Z2
-
-
Cel7A
Acremonium thermophilum ALKO4245
A7WNT9
-
-
Cel7A
Chaetomium thermophilum ALKO4265
A7WNU1
-
-
Cel7A
Chrysosporium lucknowense UV18-25
-
-
-
Cel7A
-
formerly CBH I
Cel7A
-
-
Cel7A
-
formerly known as cellobiohydrolase I
Cel7A
Thermoascus aurantiacus ALKO4242
A7WNU2
-
-
Cel7A
Trichoderma sp.
-
-
Cel7B
Acremonium thermophilum ALKO4245
A7WNU0
-
-
Cel9B
Paenibacillus sp. BP-23
-
-
-
CelAB
A9Q634
displays cellobiohydrolase and beta-1,4(3) endoglucanase catalytic activities
CelAB
A9Q634
displays cellobiohydrolase and beta-1,4(3) endoglucanase catalytic activities
-
cellobiohydrolase
-
-
-
-
cellobiohydrolase
A7WNT9, A7WNU0
-
cellobiohydrolase
Acremonium thermophilum ALKO4245
A7WNT9, A7WNU0
-
-
cellobiohydrolase
A7WNU1
-
cellobiohydrolase
Chaetomium thermophilum ALKO4265
A7WNU1
-
-
cellobiohydrolase
-
-
cellobiohydrolase
Chrysosporium lucknowense UV18-25
-
-
-
cellobiohydrolase
Q59325
-
cellobiohydrolase
Q59325
-
-
cellobiohydrolase
-
-
cellobiohydrolase
Fomitopsis pinicola KMJ812
-
-
-
cellobiohydrolase
-
-
cellobiohydrolase
-
-
cellobiohydrolase
-
-
cellobiohydrolase
-
-
cellobiohydrolase
Paenibacillus sp. BP-23
-
-
-
cellobiohydrolase
-
-
cellobiohydrolase
Penicillium purpurogenum KJS506
-
-
-
cellobiohydrolase
Q7LHI2
-
cellobiohydrolase
-
-
cellobiohydrolase
Piptoporus betulinus CCBAS585
-
-
-
cellobiohydrolase
-
-
cellobiohydrolase
Saccharophagus degradans 2-40T
-
-
-
cellobiohydrolase
A9Q634
-
cellobiohydrolase
A9Q634
-
-
cellobiohydrolase
A7WNU2
-
cellobiohydrolase
Thermoascus aurantiacus ALKO4242
A7WNU2
-
-
cellobiohydrolase
-
-
cellobiohydrolase
-
-
cellobiohydrolase 1
-
-
cellobiohydrolase 1
Q5S1P9
-
cellobiohydrolase 1
Penicillium chrysogenum FS010
Q5S1P9
-
-
cellobiohydrolase 9A
Q59325
-
cellobiohydrolase A
-
-
cellobiohydrolase I
-
-
-
-
cellobiohydrolase I
-
-
cellobiohydrolase I
-
-
cellobiohydrolase I
-
-
cellobiohydrolase I
-
-
cellobiohydrolase I
-
-
cellobiohydrolase I
P62694
-
cellobiohydrolase I
-
-
cellobiohydrolase I
Hypocrea pseudokoningii S-38
-
;
-
cellobiohydrolase I
-
-
cellobiohydrolase I
-
-
cellobiohydrolase I
-
-
cellobiohydrolase I
Irpex lacteus MC-2
-
-
-
cellobiohydrolase I
Q68HC2
-
cellobiohydrolase I
Penicillium occitanis CL100
Q68HC2
-
-
cellobiohydrolase I
-
-
cellobiohydrolase I
Trichoderma sp.
-
-
cellobiohydrolase I
-
-
cellobiohydrolase I-I
Q6E5B3
-
cellobiohydrolase I-II
Q6E5B2
-
cellobiohydrolase II
-
-
-
-
cellobiohydrolase II
P07987
-
cellobiohydrolase II
-
-
cellobiohydrolase II
Irpex lacteus MC-2
-
-
-
cellobiohydrolase II
Trichoderma sp.
-
-
cellobiohydrolase II-I
Q6E5B1
-
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
Hypocrea jecorina RUT C30
-
ambiguous
-
Cellulase
-
-
cellulase, C1
-
-
-
-
CelO
Clostridium 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-glucanase
-
-
exo-1,4-beta-glucanase
-
-
exo-beta-1,4-glucan cellobiohydrolase
-
-
-
-
exo-beta-1,4-glucanase
Q68HC2
-
exo-beta-1,4-glucanase
Penicillium occitanis CL100
Q68HC2
-
-
exo-cellobiohydrolase
-
-
-
-
exo-cellobiohydrolase
-
-
exocellobiohydrolase
-
-
-
-
exocellulase
-
-
exocellulase E3
-
-
exoglucanase
-
-
-
-
exoglucanase
-
-
exoglucanase
Hypocrea pseudokoningii S-38
-
-
-
OXG-RCBH
Geotrichum sp.
Q8J0D2
-
GH5
A4XIF7
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
P07987
the enzyme belongs to the glycosylhydrolase family GH6A
additional information
P62694
the enzyme belongs to the glycosylhydrolase family GH7A
additional information
-
the enzyme Cel7D belongs to the glycoside hydrolase family 7
CAS REGISTRY NUMBER
COMMENTARY
37329-65-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
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
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
strain JW20, gene cbhA
SwissProt
Manually annotated by BRENDA team
Clostridium thermocellum CBH III
CBH III
-
-
Manually annotated by BRENDA team
Clostridium thermocellum F7
strain F7
-
-
Manually annotated by BRENDA team
strain JW20, gene cbhA
SwissProt
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
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
strain ALKO2877
-
-
Manually annotated by BRENDA team
strain QM9414
-
-
Manually annotated by BRENDA team
strain RUT C30
-
-
Manually annotated by BRENDA team
Hypocrea jecorina ALKO2877
strain ALKO2877
-
-
Manually annotated by BRENDA team
Hypocrea jecorina CBH I
CBH I
-
-
Manually annotated by BRENDA team
Hypocrea jecorina Cel6A
Cel6A
-
-
Manually annotated by BRENDA team
Hypocrea jecorina RUT C30
strain RUT C30
-
-
Manually annotated by BRENDA team
Hypocrea pseudokoningii S-38
-
-
-
Manually annotated by BRENDA team
Hypocrea pseudokoningii S-38
strain S-38
-
-
Manually annotated by BRENDA team
Exo I /II/III
-
-
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
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 funiculosum
-
-
-
Manually annotated by BRENDA team
Penicillium occitanis CL100
-
UniProt
Manually annotated by BRENDA team
Penicillium pinophilum
2 forms: I/II
-
-
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 2-40T
-
-
Manually annotated by BRENDA team
Saccharophagus degradans 2-40T
strain 2-40T
-
-
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 sp.
-
-
-
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
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-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
A7WNT9, A7WNU0
-
-
-
-
2-chloro-4-nitrophenyl-beta-D-lactoside
2-chloro-4-nitrophenol + beta-D-lactose
show the reaction diagram
A7WNU2
-
-
-
-
2-chloro-4-nitrophenyl-beta-D-lactoside
2-chloro-4-nitrophenol + beta-D-lactose
show the reaction diagram
Chaetomium thermophilum, Chaetomium thermophilum ALKO4265
A7WNU1
-
-
-
-
2-chloro-4-nitrophenyl-beta-D-lactoside
2-chloro-4-nitrophenol + beta-D-lactose
show the reaction diagram
Acremonium thermophilum ALKO4245
A7WNT9, A7WNU0
-
-
-
-
2-chloro-4-nitrophenyl-beta-D-lactoside
2-chloro-4-nitrophenol + beta-D-lactose
show the reaction diagram
Thermoascus aurantiacus ALKO4242
A7WNU2
-
-
-
-
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
Hypocrea jecorina, Hypocrea jecorina CBH I
-
-
-
-
?
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
Q7LHI2
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
4-methylumbelliferol + beta-D-cellobiose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl beta-D-lactoside + H2O
4-methylumbelliferol + beta-D-lactose
show the reaction diagram
Q7LHI2
-
-
-
?
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-methylumbelliferyl + beta-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
Hypocrea jecorina, Hypocrea jecorina 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
A7WNT9, A7WNU0
-
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferol + beta-D-lactose
show the reaction diagram
A7WNU2
-
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferol + beta-D-lactose
show the reaction diagram
Chaetomium thermophilum, Chaetomium thermophilum ALKO4265
A7WNU1
-
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferol + beta-D-lactose
show the reaction diagram
Acremonium thermophilum ALKO4245
A7WNT9, A7WNU0
-
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferol + beta-D-lactose
show the reaction diagram
Thermoascus aurantiacus ALKO4242
A7WNU2
-
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferol + D-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
Q7LHI2
-
-
-
?
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
-, Q5S1P9
-
-
-
?
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
Penicillium chrysogenum FS010
Q5S1P9
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + beta-D-cellobiose
show the reaction diagram
Hypocrea 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
A4XIF7, -
-
-
-
?
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
Chrysosporium lucknowense UV18-25
-
-
-
-
?
4-nitrophenyl beta-D-cellotetraoside + H2O
?
show the reaction diagram
Clostridium thermocellum, Clostridium thermocellum F7
-
enzyme activity starts from the reducing end in a processive mode after making random cuts
-
-
?
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-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
Q7LHI2
-
-
-
?
4-nitrophenyl beta-lactoside + H2O
4-nitrophenol + beta-lactose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
show the reaction diagram
Q59325
-
-
-
?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl cellopentaoside + H2O
4-nitrophenol + cellobiose + D-glucose
show the reaction diagram
Q59325
-
-
-
?
4-nitrophenyl cellopentaoside + H2O
4-nitrophenyl-cellobioside + cellotriose
show the reaction diagram
Paenibacillus sp., Paenibacillus sp. BP-23
Q8KKF7
-
-
-
?
4-nitrophenyl cellotetraoside + H2O
4-nitrophenol + cellobiose
show the reaction diagram
Q59325
-
-
-
?
4-nitrophenyl cellotetraoside + H2O
4-nitrophenyl cellobioside + cellobiose
show the reaction diagram
Paenibacillus sp., Paenibacillus sp. BP-23
Q8KKF7
-
-
-
?
4-nitrophenyl cellotrioside + H2O
4-nitrophenol + cellobiose + D-glucose
show the reaction diagram
Q59325
-
-
-
?
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-lactoside + H2O
4-nitrophenol + ?
show the reaction diagram
-
-
-
-
?
alpha-cellobiosyl fluoride + H2O
fluoride + cellobiose
show the reaction diagram
-
-
-
-
?
avicel + H2O
?
show the reaction diagram
-
-
-
-
?
avicel + H2O
?
show the reaction diagram
-
-
-
-
?
avicel + H2O
?
show the reaction diagram
Trichoderma sp.
-
-
-
-
?
avicel + H2O
?
show the reaction diagram
-
-
-
-
?
avicel + H2O
?
show the reaction diagram
-
-
-
-
?
avicel + H2O
?
show the reaction diagram
Q7LHI2
-
-
-
?
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
-
-
-
-
?
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
B7X9Z2, -
-
-
-
?
avicel + H2O
cellobiose
show the reaction diagram
-
-
plus traces of cellotriose
?
avicel + H2O
cellobiose
show the reaction diagram
-
not
-
-
-
avicel + H2O
cellobiose
show the reaction diagram
-
191% activity compared to cellulose
-
-
?
avicel + H2O
cellobiose
show the reaction diagram
Coprinopsis cinerea 5338
B7X9Z2
-
-
-
?
avicel + H2O
cellobiose
show the reaction diagram
Clostridium thermocellum CBH III
-
-
-
-
?
avicel + H2O
cellobiose + ?
show the reaction diagram
-
-
-
-
?
avicel + H2O
cellobiose + ?
show the reaction diagram
-
-
-
-
?
avicel + H2O
cellobiose + ?
show the reaction diagram
-, Q12621
-
-
-
?
avicel + H2O
cellobiose + ?
show the reaction diagram
-
-
-
-
?
avicel + H2O
cellobiose + ?
show the reaction diagram
-
-
-
-
?
avicel + H2O
cellobiose + ?
show the reaction diagram
A4XIF7, -
-
-
-
?
avicel + H2O
cellobiose + ?
show the reaction diagram
Chrysosporium lucknowense UV18-25
-
-
-
-
?
avicel + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
A7WNU2
-
-
-
?
avicel + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
A7WNU1
absorption to avicel at 4C is 84%
-
-
?
avicel + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
A7WNT9, A7WNU0
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
A7WNU1
absorption to avicel at 4C is 84%
-
-
?
avicel + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
Acremonium thermophilum ALKO4245
A7WNT9, A7WNU0
absorption to avicel at 4C is 87.5%
-
-
?
avicel + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
Thermoascus aurantiacus ALKO4242
A7WNU2
-
-
-
?
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
Clostridium 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
Q7LHI2
-
-
-
?
carboxymethyl cellulose + H2O
?
show the reaction diagram
-
-
-
-
?
carboxymethyl cellulose + H2O
?
show the reaction diagram
A4XIF7, -
-
-
-
?
carboxymethyl cellulose + H2O
?
show the reaction diagram
Irpex lacteus MC-2
-
-
-
-
?
carboxymethyl cellulose + H2O
?
show the reaction diagram
Clostridium thermocellum F7
-
-
-
-
?
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
-
-
-
-
?
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
-
not
-
-
-
carboxymethylcellulose + H2O
cellobiose
show the reaction diagram
-
not
-
-
-
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
-
-
CBH II, endo-glucanase
?
carboxymethylcellulose + H2O
glucose + cellobiose + cellutetraose
show the reaction diagram
Clostridium 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
Q8J0K6
-
-
-
?
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
Paenibacillus sp., Paenibacillus sp. BP-23
Q8KKF7
-
-
-
?
cellodextrin + H2O
?
show the reaction diagram
Clostridium thermocellum F7
-
-
-
-
?
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
-
-
-
?
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
Q59325
-
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
show the reaction diagram
A9Q634, -
-
-
-
?
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
A9Q634
-
-
-
?
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
Q59325
-
-
-
?
cellotetraose + H2O
2 cellobiose
show the reaction diagram
-
-
-
-
?
cellotetraose + H2O
2 cellobiose
show the reaction diagram
A9Q634, -
-
-
-
?
cellotetraose + H2O
2 cellobiose
show the reaction diagram
Clostridium thermocellum F7
-
-
-
-
?
cellotetraose + H2O
2 cellobiose
show the reaction diagram
A9Q634
-
-
-
?
cellotetraose + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
P07987
-
-
-
?
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
-
-
-
-
?
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
Q8J0K6
-
-
-
?
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
Q59325
-
-
-
?
cellulose + H2O
?
show the reaction diagram
-
-
-
-
?
cellulose + H2O
?
show the reaction diagram
Trichoderma sp.
-
-
-
-
?
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
Saccharophagus degradans 2-40T
-
-
-
-
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
-
-
-
-
-
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
P62694
-
-
-
?
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
-
-
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
Penicillium funiculosum
-
-
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
Penicillium pinophilum
-
-
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
Phanerochaete chrysosporium CBH I
-
-
-
-
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
Hypocrea jecorina Cel6A
-
-
-
-
?
cellulose + H2O
cellobiose + glucose + cellotriose
show the reaction diagram
Clostridium thermocellum CBH III
-
-
-
-
?
cellulose + H2O
cellobiose + glucose + cellotriose
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
-
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
Q68HC2
-
-
-
?
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
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
-
-
-
?
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
A4XIF7, -
-
-
-
?
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
Q59325
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
Q8KKF7
acid-swollen cellulose, bacterial microcrystlline cellulose
-
-
?
cellulose + H2O
beta-cellobiose
show the reaction diagram
Hypocrea jecorina, Hypocrea jecorina RUT C30
-
-
-
-
?
cellulose + H2O
beta-D-cellobiose
show the reaction diagram
-
from cotton
-
-
?
corn stover + H2O
cellobiose + ?
show the reaction diagram
A4XIF7, -
-
-
-
?
cotton + H2O
?
show the reaction diagram
Trichoderma sp.
-
-
-
-
?
filter paper + H2O
?
show the reaction diagram
-
-
-
-
?
filter paper + H2O
?
show the reaction diagram
Trichoderma sp.
-
-
-
-
?
filter paper + H2O
?
show the reaction diagram
Penicillium purpurogenum KJS506
-
-
-
-
?
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
Fomitopsis pinicola, Fomitopsis pinicola KMJ812
-
33.8% activity compared to 4-nitrophenyl beta-D-cellobioside
-
-
?
lichenan + H2O
?
show the reaction diagram
Clostridium thermocellum CBH III
-
-
-
-
?
methylumbelliferyl-lactoside + H2O
methylumberlliferone + lactose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl beta-D-cellobioside + H2O
p-nitrophenol + beta-D-cellobiose
show the reaction diagram
Hypocrea pseudokoningii, Hypocrea 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
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
Clostridium thermocellum, Clostridium thermocellum CBH III
-
-
-
-
-
phosphoric acid swollen cellulose + H2O
?
show the reaction diagram
-
-
-
-
?
phosphoric acid swollen cellulose + H2O
?
show the reaction diagram
-
217% activity compared to cellulose
-
-
?
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
A7WNT9, A7WNU0
-
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
A7WNU2
-
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
Chaetomium thermophilum, Chaetomium thermophilum ALKO4265
A7WNU1
-
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
Acremonium thermophilum ALKO4245
A7WNT9, A7WNU0
-
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + D-glucose + cellotriose
show the reaction diagram
Thermoascus aurantiacus ALKO4242
A7WNU2
-
-
-
?
sulforhodamine-conjugated cellohexaose + H2O
cellotetraose + cellotriose
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
-
-
-
-
?
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.
Q8J0D2
enzyme has endoglucanase activity, releases two glucosyl residue segments from the main chain
-
-
-
additional information
?
-
-
enzyme is exclusively an exocellulase
-
-
-
additional information
?
-
Q8KKF7
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
?
-
Q7LIJ0
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
?
-
Q8J0K6
inability of Cel7B to hydrolyze cellotriose
-
-
-
additional information
?
-
A7WNT9, A7WNU0
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
?
-
A4XIF7, -
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
?
-
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
?
-
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
A7WNT9, A7WNU0
no activity with 4-methylumbelliferyl-beta-D-lactoside
-
-
-
additional information
?
-
Paenibacillus sp. BP-23
Q8KKF7
no activity on carboxymethyl cellulose, cellobiose, cellotriose or 4-methylumbelliferyl alpha-D-glucoside
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
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
Q7LIJ0
-
-
-
?
cellulose + H2O
cellobiose
show the reaction diagram
Q68HC2
-
-
-
?
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
Hypocrea jecorina, Hypocrea jecorina RUT C30
-
-
-
-
?
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
-
-
-
?
additional information
?
-
-
role in the cellusome, an active cellulase system
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
Co2+
-
activates
Co2+
-
activates
Cu2+
-
-
Mg2+
-
hexa-co-ordinate
Mg2+
-
activates
Mn2+
-
activates
Mn2+
-
activates
additional information
-
enzyme activity is not stimulated by Ba2+, Mg2+, Mn2+, Zn2+, Ca2+, Ni2+, or Co2+ (each at 1 mM)
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
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
-
-
cellobioimidazole
Q7LIJ0
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
-
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
A7WNT9, A7WNU0
competitive inhibition
cellobiose
A7WNU1
competitive inhibition
cellobiose
-
competitive inhibition
cellobiose
A7WNU2
weakly inhibits, competitive inhibition
cellobiose
-
the enzyme shows decreased hydrolysis of SR-C6 as the cellobiose concentration increases in the reaction mixture
cellobiose
A4XIF7, -
product inhibition by cellobiose
cellobiose
Q68HC2
-
cellobiose
-
competitive inhibition
Co2+
-
33.7% inhibition at 1 mM
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
lactose
-
competitive inhibition of CBHIA and CBHIB isoform, but only minimal effect on CBHII
lactose
Q7LIJ0
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
N-bromosuccinimide
-
-
N-bromosuccinimide
-
-
N-ethylmaleimide
-
30% inhibition at 10 mM
suramin
-
slight
Zn2+
-
21.2% inhibition at 1 mM
methyl (4S)-beta-cellobiosyl-4-thio-beta-cellobioside
Q7LIJ0
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
A9Q634, -
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
136.5% activity at 0.5 mM
isopropyl beta-D-1-thiogalactopyranoside
B7X9Z2, -
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
A4XIF7, -
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]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
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
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
A7WNU2
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
A7WNU1
in 50 mM sodium phosphate buffer, pH 5.7, at 22C
2.1
-
2-chloro-4-nitrophenyl-beta-D-lactoside
A7WNT9, A7WNU0
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
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
0.52
-
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
0.22
-
4-methylumbelliferyl-beta-D-lactoside
A7WNT9, A7WNU0
in 50 mM sodium acetate buffer, pH 5.0, at 22C
0.221
-
4-methylumbelliferyl-beta-D-lactoside
A7WNU1
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
A7WNU2
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
A4XIF7, -
domain GH5, at pH 5.5 and 80C,
2.4
-
4-nitrophenyl beta-D-cellobioside
A4XIF7, -
domain construct CBM3-GH5, at pH 5.5 and 80C,
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
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
Penicillium funiculosum
-
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
Q7LIJ0
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2.9
-
2,4-dinitrophenyl beta-lactoside
-
pH 5.7, 37C, mutant D214N
12.2
-
2,4-dinitrophenyl beta-lactoside
-
pH 5.7, 37C, mutant E217Q
104
-
2,4-dinitrophenyl beta-lactoside
-
pH 5.7, 37C, wild-type enzyme
0.0001
-
2,4-dinitrophenyl cellobiose
-
pH 5.5, 50C, recombinant mutant D497A
0.0005
-
2,4-dinitrophenyl cellobiose
-
pH 5.5, 50C, recombinant mutant S232A
0.0015
-
2,4-dinitrophenyl cellobiose
-
pH 5.5, 50C, recombinant mutant Y220A
0.0018
-
2,4-dinitrophenyl cellobiose
-
pH 5.5, 50C, recombinant mutant D226A
0.038
-
2,4-dinitrophenyl cellobiose
-
pH 5.5, 50C, recombinant mutant D274A
0.057
-
2,4-dinitrophenyl cellobiose
-
pH 5.5, 50C, recombinant wild-type enzyme
0.0063
-
2-chloro-4-nitrophenyl beta-lactoside
-
pH 5.7, 37C, mutant E212Q
0.035
-
2-chloro-4-nitrophenyl beta-lactoside
-
pH 5.7, 37C, mutant E217Q
0.15
-
2-chloro-4-nitrophenyl beta-lactoside
-
pH 5.7, 37C, mutant D214N
12.8
-
2-chloro-4-nitrophenyl beta-lactoside
-
pH 5.7, 37C, wild-type enzyme
0.0153
-
2-chloro-4-nitrophenyl-beta-D-lactoside
-
Cel7B wild-type expressed in Saccharomyces cerevisiae, at 22C, pH 6.0
0.0165
-
2-chloro-4-nitrophenyl-beta-D-lactoside
-
Cel7B mutant S290T/G4C/M70C expressed in Saccharomyces cerevisiae, at 22C, pH 6.0
0.0167
-
2-chloro-4-nitrophenyl-beta-D-lactoside
-
Cel7B wild-type expressed in Trichoderma reesei, at 22C, pH 6.0
0.01817
-
2-chloro-4-nitrophenyl-beta-D-lactoside
-
Cel7B mutant G4C/M70C expressed in Saccharomyces cerevisiae, at 22C, pH 6.0
0.0205
-
2-chloro-4-nitrophenyl-beta-D-lactoside
-
Cel7B mutant S290T expressed in Saccharomyces cerevisiae, at 22C, pH 6.0
0.0283
-
2-chloro-4-nitrophenyl-beta-D-lactoside
A7WNU2
in 50 mM sodium phosphate buffer, pH 5.7, at 22C
0.043
-
2-chloro-4-nitrophenyl-beta-D-lactoside
-
in 50 mM sodium phosphate buffer, pH 5.7, at 22C
0.0467
-
2-chloro-4-nitrophenyl-beta-D-lactoside
A7WNT9, A7WNU0
in 50 mM sodium phosphate buffer, pH 5.7, at 22C
0.3167
-
2-chloro-4-nitrophenyl-beta-D-lactoside
A7WNU1
in 50 mM sodium phosphate buffer, pH 5.7, at 22C
8.9
-
2-chloronitrophenyl-beta-D-cellotrioside
-
pH 5, 50C, CBHII isoform
9108
-
2-chloronitrophenyl-beta-D-lactoside
-
pH 6, 60C
1.7
-
4-bromophenyl beta-lactoside
-
pH 5.7, 37C, wild-type enzyme
0.0073
-
4-methylumbelliferyl beta-lactoside
-
pH 5.7, 37C, mutant E217Q
0.063
-
4-methylumbelliferyl beta-lactoside
-
pH 5.7, 37C, mutant E212Q
2.3
-
4-methylumbelliferyl beta-lactoside
-
pH 5.7, 37C, mutant D214N
47
-
4-methylumbelliferyl beta-lactoside
-
pH 5.7, 37C, wild-type enzyme
0.083
-
4-methylumbelliferyl-beta-D-lactoside
-
Cel7B mutant G4C/M70C expressed in Saccharomyces cerevisiae, at 22C, pH 6.0
0.1067
-
4-methylumbelliferyl-beta-D-lactoside
-
Cel7B wild-type expressed in Saccharomyces cerevisiae, at 22C, pH 6.0
0.1083
-
4-methylumbelliferyl-beta-D-lactoside
-
Cel7B mutant S290T expressed in Saccharomyces cerevisiae, at 22C, pH 6.0
0.12
-
4-methylumbelliferyl-beta-D-lactoside
-
Cel7B mutant S290T/G4C/M70C expressed in Saccharomyces cerevisiae, at 22C, pH 6.0
0.143
-
4-methylumbelliferyl-beta-D-lactoside
-
Cel7B wild-type expressed in Trichoderma reesei, at 22C, pH 6.0
0.1883
-
4-methylumbelliferyl-beta-D-lactoside
A7WNT9, A7WNU0
in 50 mM sodium acetate buffer, pH 5.0, at 22C
0.325
-
4-methylumbelliferyl-beta-D-lactoside
A7WNU2
in 50 mM sodium acetate buffer, pH 5.0, at 22C
0.4783
-
4-methylumbelliferyl-beta-D-lactoside
-
in 50 mM sodium acetate buffer, pH 5.0, at 22C
1.15
-
4-methylumbelliferyl-beta-D-lactoside
A7WNU1
in 50 mM sodium acetate buffer, pH 5.0, at 22C
0.08
-
4-nitrophenyl beta-D-cellobioside
-
recombinant Cex-RsaA fusion mutant
15.8
-
4-nitrophenyl beta-D-cellobioside
-
wild-type Cex
0.00066
-
4-nitrophenyl beta-lactoside
-
pH 5.7, 37C, mutant E217Q
0.0041
-
4-nitrophenyl beta-lactoside
-
pH 5.7, 37C, mutant E212Q
0.042
-
4-nitrophenyl beta-lactoside
-
pH 5.7, 37C, mutant D214N
3.5
-
4-nitrophenyl beta-lactoside
-
pH 5.7, 37C, wild-type enzyme
0.061
-
4-nitrophenyl lactoside
-
pH 5, 30C, Y247F mutant
0.093
-
4-nitrophenyl lactoside
-
pH 5, 30C, wild-type enzyme
0.19
-
4-nitrophenyl lactoside
-
pH 5, 30C, DELTAG245-Y252 mutant
0.82
-
4-nitrophenyl lactoside
-
pH 5, 30C, D241C/D249C mutant
2952
-
4-nitrophenyl-beta-D-cellobioside
-
pH 6, 60C
13.4
-
4-nitrophenyl-beta-D-lactoside
-
pH 5, 50C, CBHIA and CBHIB isoform
0.01
-
alpha-cellobiosyl fluoride
-
pH 5, 20C
0.54
-
alpha-cellobiosyl fluoride
-
pH 5, 20C
0.071
-
beta-cellobiosyl fluoride
-
pH 5, 20C
4
-
beta-cellobiosyl fluoride
-
pH 5, 20C
0.02
-
Cellohexaose
-
pH 5, 27C, D175A mutant
14
-
Cellohexaose
-
pH 5, 27C, wild-type enzyme
0.025
-
Cellopentaose
-
pH 5, 27C, D175A mutant
1.1
-
Cellopentaose
-
pH 5, 27C, wild-type enzyme
0.0013
-
Cellotetraose
-
pH 5, 27C, D175A mutant
0.5
-
Cellotetraose
-
pH 5, 27C, wild-type enzyme
0.58
-
Cellotetraose
-
pH 5, 27C, Y247F mutant and D241C/D249C mutant
0.83
-
Cellotetraose
-
pH 5, 27C, DELTAG245-Y252 mutant
4.1
-
Cellotetraose
-
pH 5, 27C, wild-type enzyme
0.0003
-
cellotriose
-
pH 5, 27C, D175A mutant
0.06
-
cellotriose
-
pH 5, 27C, wild-type enzyme
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
15.8
-
4-nitrophenyl beta-D-cellobioside
-
in 100 mM sodium acetate buffer (pH 5.0) at 50C
214148
additional information
-
additional information
-
-
0
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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
0.039
-
cellobiose
A7WNU1
-
0.107
-
cellobiose
A7WNU2
-
0.141
-
cellobiose
A7WNT9, A7WNU0
-
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
2.5
-
cellobiose
-
4-nitrophenyl-beta-D-cellobioside as substrate, pH 5, 50C, CBHIA isoform
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]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
30
-
cellobiose
A4XIF7, -
domain GH5, in 50 mM MES buffer at pH 5.5 and 80C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.00188
-
Q8KKF7
bacterial microcrystalline cellulose as substrate
0.00488
-
Q8KKF7
acid swollen cellulose as substrate
0.0571
-
-
-
0.114
-
-
CBH II
0.151
-
-
CBH I
1.1
-
-
CBHIA isoform, 4-nitrophenyl-beta-lactoside as substrate
1.4
-
-
cellulose
1.6
-
-
purified recombinant enzyme, substrate 4-methylumbelliferyl beta-D-lactoside
2.1
-
-
with phosphoric acid swollen cellulose as substrate
2.15
-
-
purified recombinant enzyme, substrate 4-methylumbelliferyl beta-D-cellobioside
2.5
-
-
CBHIB isoform, 4-nitrophenyl-beta-lactoside as substrate
2.6
-
-
crude enzyme, pH 5.0, 60C
4
-
-
crude cell extract, using 4-nitrophenyl beta-D-cellobioside as substrate, at pH 5.0, 50C
5.6
-
-
CBHIB isoform, avicel as substrate
6.67
-
-
-
7.5
-
-
with carboxymethylcellulose as substrate
10.8
-
-
after4.2fold purification, pH 5.0, 60C
15.31
-
Geotrichum sp.
Q8J0D2
-
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
24.6
-
-
lichenan
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
340
-
-
with 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
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2.5
-
Penicillium pinophilum
-
isozyme I
3.5
4
-
amorphous cellulose
3.5
5
Geotrichum sp.
Q8J0D2
-
3.6
-
-
CBHIA isoform
3.8
-
-
CBHII isoform
4
4.5
-
isozyme II
4
5
-
crystalline cellulose
4
6
-
thermophilic fungi
4.1
-
-
CBHIB isoform
4.2
-
-
avicel
4.5
7
-
exo III
4.5
-
-
cellulose
4.5
-
Penicillium pinophilum
-
isozyme II
4.7
-
A4XIF7, -
pH-optimum for domain construct CBM3-GH5
4.8
-
-
-
5
5.5
-
full-length and mutant enzyme forms
5
-
-
p-nitrophenyl-lactoside
5
-
-
assay at
5
-
A7WNT9, A7WNU0
-
5
-
-
assay at; assay at
5.5
5.7
-
exo I
5.5
6.5
-
avicel
5.5
-
-
assay at
5.5
-
A4XIF7, -
pH-optimum for domain GH5
5.7
-
-
assay at
6
-
Q8KKF7
-
6.8
7.8
-
-
7
-
Q7LIJ0
assay at
additional information
-
Penicillium funiculosum
-
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
5.1
9
-
50% of maximal activity
additional information
-
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-
assay at
30
-
Q7LIJ0
assay at
37
-
-
avicel
37
-
-
assay at
40
-
-
assay at
44
-
-
assay at
45
-
Q8KKF7
-
50
60
Geotrichum sp.
Q8J0D2
-
50
-
-
cellulose
50
-
-
assay at
50
-
-
assay at; assay at
50
-
-
assay at
55
70
-
thermophilic fungi
55
-
-
isozyme I
55
-
-
-
60
-
-
isozyme II
60
-
Penicillium funiculosum
-
-
60
-
A7WNT9, A7WNU0
-
60
-
-
activity decreases rapidly at temperatures over 60C
66
69
-
CBHIB isoform
68
-
-
CBHII isoform
78
-
-
CBHIA isoform
80
90
A4XIF7, -
temperature optimum for domain GH5
80
-
A4XIF7, -
temperature optimum for domain construct CBM3-GH5
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
23
60
-
10% of maximal activity
45
55
-
80% and 95% of the maximum activity appearing at 45C and 55C
60
70
Penicillium funiculosum
-
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
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
4.67
-
A7WNT9, A7WNU0
-
4.8
-
-
isoelectric focusing
4.83
-
A7WNT9, A7WNU0
-
4.9
-
-
isoelectric focusing, pH gradient pH 3.5-9.5, CBHIA isoform
4.9
-
Q8KKF7
calculated from amino acid sequence
5.1
-
-
isoelectric focusing
5.6
-
-
isoelectric focusing, Cel6A
6
-
Geotrichum sp.
Q8J0D2
-
6
-
-
isoelectric focusing, pH gradient pH 3.5-9.5, CBHII isoform
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
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
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
Hypocrea jecorina 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
Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
Thermobifida fusca (strain YX)
Thermobifida fusca (strain YX)
Trichoderma harzianum
Trichoderma harzianum
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
22000
-
-
gel filtration
40000
-
-
gel filtration
41800
-
-
sedimentation equilibrium analysis
42000
-
-
gel filtration
43720
-
B7X9Z2, -
sequence analysis
46000
-
-
chromatography of reduced and alkylated enzyme
46300
-
Penicillium pinophilum
-
isozyme I, gel filtration
46300
-
Penicillium funiculosum
-
gel filtration
46900
-
A7WNU2
sequence analysis
47100
-
A7WNT9, A7WNU0
sequence analysis
47500
-
-
estimated from amino acid sequence
47500
-
-
SDS-PAGE
50000
-
-
isozyme II, gel filtration
50000
-
-
SDS-PAGE
50300
-
-
light scattering
50700
-
Penicillium pinophilum
-
isozyme II, gel filtration
52500
-
-
gel filtration
53700
-
A7WNT9, A7WNU0
sequence analysis
54600
-
A7WNU1
sequence analysis
55000
-
-
SDS-PAGE
56000
-
-, Q5S1P9
SDS-PAGE
56240
-
-
SDS-PAGE, CBHII isoform
56330
-
-
SDS-PAGE, CBHIB isoform
57000
-
-
isozyme I, gel filtration
60000
-
-
gel filtration
60000
-
-
SDS-PAGE, Cel7A
61000
-
-
gel filtration
62000
68000
-
gel filtration
62000
68000
-
gel filtration
64000
-
-
II, gel filtration
64000
-
-
gel filtration
64000
-
-
gel filtration
65000
-
-
gel filtration
66000
-
-
SDS-PAGE
66100
-
-
SDS-PAGE, CBHIA isoform
70000
-
-
SDS-PAGE, Cel6A
75240
-
-
calculated from nucleic acid sequence
79000
-
-
SDS-PAGE
81900
-
-
estimated from amino acid sequence
84000
-
-
isozyme I, gel filtration
97000
-
Geotrichum sp.
Q8J0D2
SDS-PAGE
118000
-
Q8KKF7
calculated from amino acid sequence
122000
-
Q8KKF7
SDS-PAGE
200000
-
-
gel filtration
230000
-
-
gel filtration
additional information
-
-
-
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
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
?
-
x * 87000, SDS-PAGE
?
-
x * 75000, SDS-PAGE
?
Q7LHI2
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
?
B7X9Z2, -
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
?
Q68HC2
x * 52500, calculated from amino acid sequence
?
Coprinopsis cinerea 5338
-
x * 48951, 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
-
?
Penicillium occitanis CL100
-
x * 52500, calculated from amino acid sequence
-
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
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
-
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
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
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
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
-
-
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
-
CBH 1, 9% reducing sugar, CBH 1a 33% reducing sugar
glycoprotein
-
attached carbohydrate in addition to glycoprotein constituents
glycoprotein
Hypocrea rufa QM 9414
-
-
-
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
Q68HC2
-
glycoprotein
Penicillium occitanis CL100
-
-
-
glycoprotein
-
-
glycoprotein
-
-
glycoprotein
Q7LIJ0
Cel7D
glycoprotein
-
36-38% carbohydrate content
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
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
-
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
B7X9Z2, -
hanging drop vapor diffusion method
Geotrichum sp.
-
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
-
catalytic domain, cocrystallized with the (S)-enantiomer of the beta-blocker propranolol
-
engineered enzymes
-
hanging drop vapor diffusion method
-
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
Q8J0K6
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
Q7LIJ0
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2
7
-
4C, 24 h, CBH II
2
7
-
enzyme is stable at pH 3-7 at 37C, but loses 90% of activity at pH 2 after 20 min
2.5
6
-
4C, 24 h, CBH I
3
10
-
6C, 48 h
3
5
-
native Ex-1
3
8
-
recombinant Ex-1
3
8
-
retains 80% activity when incubated for 60 min at 60C
3.5
5.6
-
optimal stability, gradual decrease in stability at more alkaline pH values
4
8
Geotrichum sp.
Q8J0D2
90% activity at 45C
4.5
5
-
highest stability
5.5
8
-
25C, 24 h
5.5
8
-
highest stability
5.5
8.4
-
stable at 4C for 48 h
6
8.4
-
stable at 60C for 5 h, stability decreases with incubation time above 5 h
6
-
-
complete loss of activity below pH 6 at 60C for 48 h
6
-
-
wild-type enzyme is more stable than E107Q and E107Q/D170N/D366N mutants
8
-
-
wild-type enzyme is less stable than E107Q and E107Q/D170N/D366N mutants
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
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
50
-
Geotrichum sp.
Q8J0D2
90% activity after 10 min at pH 4
50
-
-
enzyme retains full activity between pH 4 and 6, but is rapidly inactivated at lower pH values
50
-
-
24 h, stable, full-length and mutant enzyme forms
60
-
-
pH 5.5, 10 min, complete loss of activity
60
-
-
stable for 10 min
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
60
-
-
7 h, 90% remaining activity of the full-length enzyme form
60
-
-
retains 80% activity when incubated for 60 min in buffers at pH 3-8
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
65
-
-
stable for 5 min
65
-
-
60% loss of activity after 10 min /CBH I
65
-
-
3 h, 50% remaining activity of the full-length enzyme form
70
80
A4XIF7, -
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
70
-
-
CHB II: 40% loss of activity after 10 min
78
-
-
complete denaturation after 3 min
80
-
-
50% loss of activity after 3 hours
80
-
-
t1/2 CBHIA: 34 min, t1/2 CBHIB: 68 min, t1/2 CBHII: 38 min at pH 5
100
-
-
95% loss of activity after 10 min
100
-
-
5 min, loss of 50% of activity of the purified recombinant enzyme
additional information
-
-
the full-length enzyme form is more thermostable than the truncated mutant enzyme form
additional information
-
-
irreversible thermal unfolding kinetics of recombinant enzyme domains, overview
additional information
-
-
thermal unfolding kinetics of wild-type and mutant enzymes, overview
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)
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
glycerol stabilizes
-
freezing and thawing, stable
-
Ca2+ and cysteine stabilizes
-
bovine serum albumin stabilizes
-
ribonuclease stabilizes
-
dilute solutions, unstable
-
cellotetraose stabilizes the protein fold
-
freezing and thawing, stable
Penicillium funiculosum
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
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 ACCESSION NO.
LITERATURE
Ni2+ affinity column chromatography
-
on affinity column and by gel filtration
A7WNT9, A7WNU0
overexpressed in Escherichia coli
-
Ni2+-NTA column chromatography and HiTrap Q HP anion-exchange column chromatography
A4XIF7, -
gene cloned in Escherichia coli
-
Ni2+ affinity column chromatography
-
on affinity column and by gel filtration
A7WNU1
Source 15Q column chromatography
-
Ni-IDA resin column chromatography and Superdex 75pg 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
-
on NiNTA column
B7X9Z2, -
DEAE Sepharose column chromatography, Sephacryl S-300 gel filtration, and Mono Q column chromatography
-
-
Geotrichum sp.
Q8J0D2
homogeneity
-
CBH I and CBH II
-
cloned in Escherichia coli
-
DEAE Sepharose column chromatography
-
extracellular Cel5A, Cel6A, and Cel7A from culture medium
-
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
-
Ni2+ affinity column chromatography
-
on affinity column and by gel filtration
-
Q-Sepharose Fast-Flow column chromatography and Mono Q column chromatography
-
wild-type and mutants
-
HiTrap Q HP 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
-
DEAE Sepharose FF column chromatography
-
wild-type and mutants purified with one-step purification using gel filtration
-
homogeneity
Q8KKF7
-
Penicillium funiculosum
-
-
Penicillium pinophilum
-
DEAE-Sepharose column chromatography, Mono Q column chromatography, and Sephacryl S-300 gel filtration
-
nickel-NTA resin column chromatography
-
Ni2+ affinity column chromatography
-
three forms: CBHIA, CBHIB and CBHII, homogeneity
-
High Trap DEAE column chromatography
A9Q634, -
Ni2+ affinity column chromatography
-
on affinity column and by gel filtration
A7WNU2
recombinant wild-type Cel6B and mutant enzymes from Escherichia coli strain BL21(DE3) by hydrophobic interaction and anion exchange chromatography
-
Superdex 75 gel filtration and Mono-Q column chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Saccharomyces cerevisiae strain YDR483W
-
wild-type Cel7A expressed in Trichoderma reesei; wild-type Cel7B expressed in Trichoderma reesei
A7WNT9, A7WNU0
expressed in Escherichia coli
A4XIF7, -
cloned in Saccharomyces cerevisiae, cloned in Escherichia coli
-
expressed in Saccharomyces cerevisiae strain YDR483W
-
wild-type Cel7A expressed in Trichoderma reesei
A7WNU1
gene cbh1, DNA and amino acid sequence determination
-
3 truncated forms: Gh9, Gh9-Fn31,2, Gh9-Fn31,2-CBDIII
-
cloned in Escherichia coli
-
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 as a C-terminal His6-tag in Escherichia coli
B7X9Z2, -
expressed in Escherichia coli
Geotrichum sp.
Q8J0D2
expressed in Aspergillus oryzae
-
cloned in Escherichia coli
-
expressed in Escherichia coli
-
expressed in Fusarium venenatum
-
expressed in Saccharomyces cerevisiae strain YDR483W
-
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
-
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 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
-
functional expression of Cel9B and Cel48C in Escherichia coli
-
expressed in Saccharomyces cerevisiae strain H158
-, Q5S1P9
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 Escherichia coli
-
expressed in Saccharomyces cerevisiae strain YDR483W
-
expressed in Kluyveromyces lactis strain DELTActs1
A9Q634, -
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
A7WNU2
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
-
expression of wild-type Cel6B and mutant enzymes in Escherichia coli strain BL21(DE3)
-
expressed in Aspergillus niger
-
expressed in Escherichia coli XL-1 Blue cells; expressed in Escherichia coli XL-1 Blue cells; expressed in Escherichia coli XL-1 Blue cells
Q6E5B1, Q6E5B2, Q6E5B3
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D262A
-
site-directed mutagenesis, mutation of the the module interface residue affects the interaction of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
D264A
-
site-directed mutagenesis, mutation of the the module interface residue affects the interaction of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
T230A
-
site-directed mutagenesis, mutation of the module interface residue affects the final fold and stability of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
T230A/D262A
-
site-directed mutagenesis, mutation of the residues affects the interaction of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
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
-
Y466A
-, Q12621
the mutation greatly reduces the cellulose-binding ability
Y492A
-, Q12621
the mutation greatly reduces the cellulose-binding ability
Y493A
-, Q12621
the mutation greatly reduces the cellulose-binding ability
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
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
W272A
-
mutant
W272D
-
mutant
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
E217Q
Hypocrea jecorina ALKO2877
-
stability similar to wild-type enzyme, catalytically inactive
-
E223S/A224H/L225V/T226A/D262G
Hypocrea jecorina ALKO2877
-
mutant has a more alkaline pH optimum, mutation destabilizes the protein fold at both acidic and alkaline pH
-
D214N
Hypocrea jecorina CBH I
-
impaired catalytic activity
-
E212Q
Hypocrea jecorina CBH I
-
impaired catalytic activity
-
E217Q
Hypocrea jecorina CBH I
-
impaired catalytic activity
-
W272A
Hypocrea jecorina Cel6A
-
mutant
-
W272D
Hypocrea jecorina Cel6A
-
mutant
-
Y169F
Hypocrea jecorina Cel6A
-
mutant
-
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
Q7LIJ0
inactive mutant
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
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
-
isolation of the truncated catalytic core enzyme form 2 lacking the cellulose binding module and the major part of glycosylated linker from a mutant strain
E795Q
-
inactive mutant
additional information
-
elimination of the enzyme's immunoglobulin-like module leads to its complete inactivation
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
-
additional information
-
elimination of the enzyme's immunoglobulin-like module leads to its complete inactivation
-
M514Q
-
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
additional information
-
mixtures of the Cel6B mutant enzymes and Thermobifida fusca endocellulase Cel5A do not show increased synergism or processivity, and the mutant enzyme which has the highest processivity give the poorest synergism
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
refolding of recombinant enzyme, after solubilization and denaturation by 8 M urea from Escherichia coli inclusion bodies, by dialysis of enzyme in 10 mM DTT, PMSF, 2-mercaptoethanol, at 4C against 1 l of 50 mM Tris, pH 8.0, containing 5 mM CaCl2, for 2 days with 3times of buffer change
-
in 20 mM PIPES buffer [pH 6.8], 2.5% Triton X-100, 2 mM dithiothreitol, 2.5 mM CaCl2
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
detergent
-
usage in paper-, detergent- and textile industry
paper production
-
usage in paper-, detergent- and textile industry
industry
-
development of efficient degradation of cellulosic biomass using cellulolytic enzymes, e.g. Ex-4, of white rot fungi
industry
Irpex lacteus MC-2
-
development of efficient degradation of cellulosic biomass using cellulolytic enzymes, e.g. Ex-4, of white rot fungi
-
paper production
-
wild-type and recombinant endoglucanases Cel9B and Cel48C associated with endo- or exo-acting glucanases from Thermobifida fusca synergistically enhance the enzyme activity useful in pulpe and paper manufacturing, optimization, overview
biotechnology
-
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 yielding a robust, catalytically active product, biocatalyst system evaluation
additional information
-
ability to amplify a key fungal cellobiohydrolase I gene involved in plant litter decomposition has the potential to unlock the identity and dynamics of the cellulolytic fungal community in situ
textile production
-
usage in paper-, detergent- and textile industry
additional information
-
ability to amplify a key fungal cellobiohydrolase I gene involved in plant litter decomposition has the potential to unlock the identity and dynamics of the cellulolytic fungal community in situ
paper production
Paenibacillus sp. BP-23
-
wild-type and recombinant endoglucanases Cel9B and Cel48C associated with endo- or exo-acting glucanases from Thermobifida fusca synergistically enhance the enzyme activity useful in pulpe and paper manufacturing, optimization, overview
-
additional information
-
ability to amplify a key fungal cellobiohydrolase I gene involved in plant litter decomposition has the potential to unlock the identity and dynamics of the cellulolytic fungal community in situ