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Information on EC 3.2.1.176 - cellulose 1,4-beta-cellobiosidase (reducing end)
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3.2.1.176 cellulose 1,4-beta-cellobiosidase (reducing end)IUBMB Comments
Some exocellulases, most of which belong to the glycoside hydrolase family 48 (GH48, formerly known as cellulase family L), act at the reducing ends of cellulose and similar substrates. The CelS enzyme from Clostridium thermocellum is the most abundant subunit of the cellulosome formed by the organism. It liberates cellobiose units from the reducing end by hydrolysis of the glycosidic bond, employing an inverting reaction mechanism . Different from EC 3.2.1.91, which attacks cellulose from the non-reducing end.
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Word Map
- 3.2.1.176
-
crew
-
subsystem
-
mission
-
hydroponic
- cellulosome
- thermocellum
-
bioregenerative
-
life-support
- cellulases
-
lunar
-
long-duration
-
inedible
- degradation
-
breadboard
- avicel
-
dockerin
-
moon
- synthesis
- biotechnology
- biofuel production
- analysis
- paper production
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
2
+
2
=
2
+
+
Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and similar substrates, releasing cellobiose from the reducing ends of the chains.
Synonyms
celss, cel48s, cbh-1, cbhi.1, cel48c, gh7 cbh, cbh7b, cellobiohydrolase cels, 1,4-beta-d-glucan cellobiohydrolase i, tr-cel7a, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,4-beta-D-glucan cellobiohydrolase I
1,4-beta-D-glucan-cellobiohydrolase I
CBH
CBH I
CBH1
Cbh7B
CbhA
CBHI
Cel48A
Cel48C
Cel48S
Cel7A
Cel7B
Cel7D
Cel9B
cellobiohydrolase
cellobiohydrolase CelS
-
-
-
-
cellobiohydrolase class I
cellobiohydrolase I
Cellulase SS
CelO
celS
CelSS
-
-
-
-
CelY
Ct-Cel5F
endoglucanase SS
-
-
-
-
exo-beta-1,4-glucanase
exoglucanase
GH7 CBH
reducing end acting processive exocellulase
reducing end-acting CBH
THITE_62596
additional information
Cel48A
-
-
-
-
Cel7A
-
-
cellobiohydrolase
-
-
cellobiohydrolase I
-
-
Cellulase SS
-
-
-
-
celS
-
-
-
-
additional information
-
the enzyme Cel7A probably belongs to the cellobiohydrolase family 7
additional information
the enzyme Cel7D belongs to the glycoside hydrolase family 7
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and similar substrates, releasing cellobiose from the reducing ends of the chains.
-
-
-
-
2 cellohexaose + 2 H2O = 2 cellotriose + cellotetraose + cellobiose
mechanism
2 cellohexaose + 2 H2O = 2 cellotriose + cellotetraose + cellobiose
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
-
2 cellohexaose + 2 H2O = 2 cellotriose + cellotetraose + cellobiose
substrate binding structure analysis of Cel7D
2 cellohexaose + 2 H2O = 2 cellotriose + cellotetraose + cellobiose
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
4-beta-D-glucan cellobiohydrolase (reducing end)
Some exocellulases, most of which belong to the glycoside hydrolase family 48 (GH48, formerly known as cellulase family L), act at the reducing ends of cellulose and similar substrates. The CelS enzyme from Clostridium thermocellum is the most abundant subunit of the cellulosome formed by the organism. It liberates cellobiose units from the reducing end by hydrolysis of the glycosidic bond, employing an inverting reaction mechanism [2]. Different from EC 3.2.1.91, which attacks cellulose from the non-reducing end.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(cellobiose)n + H2O
(cellobiose)n-1 + cellobiose
-
release of cellobiose from the reducing end. The enzyme uses a single displacement mechanism resulting in inversion of the anomeric configuration
-
-
?
2,4-dinitrophenyl beta-cellobioside + H2O
2,4-dinitrophenol + beta-cellobiose
-
-
-
-
?
2,4-dinitrophenyl beta-glucopyranoside + H2O
2,4-dinitrophenol + beta-D-glucose
-
-
-
-
?
2,4-dinitrophenyl beta-lactoside + H2O
2,4-dinitrophenol + beta-lactose
-
-
-
-
?
2-chloro-4-nitrophenyl beta-cellobioside + H2O
2-chloro-4-nitrophenol + beta-cellobiose
-
-
-
-
?
2-chloro-4-nitrophenyl beta-D-lactoside + H2O
2-chloro-4-nitrophenol + D-lactose
-
-
-
?
2-chloro-4-nitrophenyl beta-D-lactoside + H2O
2-chloro-4-nitrophenol + lactose
-
-
-
?
2-chloro-4-nitrophenyl beta-lactoside + H2O
2-chloro-4-nitrophenol + beta-lactose
-
-
-
-
?
2-chloro-4-nitrophenyl lactoside + H2O
2-chloro-4-nitrophenol + ?
-
-
-
?
2-chloro-4-nitrophenyl-beta-D-cellotrioside + H2O
2-chloro-4-nitrophenol + ?
-
-
-
?
2-chloro-4-nitrophenyl-beta-D-lactoside + H2O
2-chloro-4-nitrophenol + D-lactose
-
-
-
-
?
4-bromophenyl beta-cellobioside + H2O
4-bromophenol + beta-cellobiose
-
-
-
-
?
4-bromophenyl beta-glucopyranoside + H2O
4-bromophenol + beta-D-glucose
-
-
-
-
?
4-methylumbelliferyl beta-cellobioside + H2O
4-methylumbelliferone + cellobiose
-
-
-
-
?
4-methylumbelliferyl beta-cellopentaoside + H2O
4-methylumbelliferone + cellopentaose
-
-
-
-
?
4-methylumbelliferyl beta-cellotetraoside + H2O
4-methylumbelliferone + cellotetraose
-
-
-
-
?
4-methylumbelliferyl beta-cellotrioside + H2O
4-methylumbelliferone + cellotriose
-
-
-
-
?
4-methylumbelliferyl beta-lactoside + H2O
4-methylumbelliferone + lactose
-
-
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferone + lactose
-
-
-
-
?
4-nitrophenyl beta-cellobioside + H2O
4-nitrophenol + beta-cellobiose
-
-
-
-
?
4-nitrophenyl beta-D-cellopentaoside + H2O
4-nitrophenol + beta-D-cellopentaose
best substrate
-
-
?
4-nitrophenyl beta-D-cellotrioside + H2O
4-nitrophenol + cellobiose
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-D-lactopyranoside + H2O
4-nitrophenol + D-lactose
-
-
-
-
?
4-nitrophenyl beta-D-lactoside
4-nitrophenol + beta-D-lactose
-
-
-
?
4-nitrophenyl beta-D-lactoside + H2O
4-nitrophenol + beta-D-lactose
-
-
-
-
?
4-nitrophenyl beta-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl beta-lactoside + H2O
4-nitrophenol + beta-lactose
-
-
-
-
?
4-trifluoromethylumbelliferyl beta-cellobioside + H2O
4-trifluoromethylumbelliferone + cellobiose
-
-
-
-
?
4-trifluoromethylumbelliferyl beta-cellotrioside + H2O
4-trifluoromethylumbelliferone + cellotriose
-
-
-
-
?
Avicel PH 101 + H2O
?
cellobiose production is monitored by an amperometric enzyme biosensor based on cellobiose dehydrogenase from Phanerochaete chrysosporium adsorbed onto the surface of a benzoquinone-modified carbon paste electrode
-
-
?
bacterial cellulose + H2O
cellobiose + cellotriose
-
no release of D-.glucose is observed
-
?
barley straw + H2O
?
-
investigation of the action of the commercial cellulase product Celluclast 1.5 (a mixture of different cellulases), derived from Trichoderma reesei on barley straw
-
-
?
carboxymethylcellulose + H2O
glucose + cellobiose + cellutetraose
-
-
-
-
?
cellulose + H2O
alpha-cellobiose + beta-cellobiose
the enzyme hydrolyzes the beta-1,4 linkages of a cellulose chain from its reducing end via a retaining mechanism liberating the product, which consists of roughly 63% beta-cellobiose and 37% alpha-cellobiose
-
-
?
cellulose nanowhisker + H2O
cellobiose + ?
-
crystalline portion of cellulose
-
-
?
microcrystalline cellulose Ibeta + H2O
?
-
enzyme-substrate complex, computational simulations and molecular dynamics, modelling of the enzyme interacting with a model segment of a cellulose microfibril, detailed overview
-
-
?
p-nitrophenyl beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
-
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
-
-
-
-
?
phosphoric acid-swollen cellulose + H2O
cellobiose + ?
Thermochaetoides thermophila
-
-
-
-
?
phosphoric acid-swollen cellulose + H2O
cellobiose + cellotriose
-
no release of D-.glucose is observed
-
?
sigmacell + H2O
?
2% activity compared to phosphoric acid-swollen cellulose
-
-
?
2-chloro-4-nitrophenyl beta-D-cellobioside + H2O
2-chloro-4-nitrophenol + D-cellobiose
-
-
-
?
2-chloro-4-nitrophenyl beta-D-cellobioside + H2O
2-chloro-4-nitrophenol + D-cellobiose
-
-
-
?
2-chloro-4-nitrophenyl-beta-D-lactoside
2-chloro-4-nitrophenol + beta-D-lactose
-
-
-
?
2-chloro-4-nitrophenyl-beta-D-lactoside
2-chloro-4-nitrophenol + beta-D-lactose
-
-
-
?
2-chloro-4-nitrophenyl-beta-D-lactoside
2-chloro-4-nitrophenol + beta-D-lactose
-
-
-
?
2-chloro-4-nitrophenyl-beta-D-lactoside
2-chloro-4-nitrophenol + beta-D-lactose
-
-
-
?
2-chloro-4-nitrophenyl-beta-D-lactoside
2-chloro-4-nitrophenol + beta-D-lactose
Thermochaetoides thermophila
-
-
-
?
2-chloro-4-nitrophenyl-beta-D-lactoside
2-chloro-4-nitrophenol + beta-D-lactose
Thermochaetoides thermophila ALKO4265
-
-
-
?
2-chloro-4-nitrophenyl-beta-D-lactoside
2-chloro-4-nitrophenol + beta-D-lactose
-
-
-
-
?
2-chloro-4-nitrophenyl-beta-lactoside + H2O
2-chloro-4-nitrophenol + lactose
-
-
-
?
2-chloro-4-nitrophenyl-beta-lactoside + H2O
2-chloro-4-nitrophenol + lactose
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
4-methylumbelliferol + cellobiose
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
4-methylumbelliferol + cellobiose
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
4-methylumbelliferone + beta-D-cellobiose
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
4-methylumbelliferone + beta-D-cellobiose
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
4-methylumbelliferone + cellobiose
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
4-methylumbelliferone + cellobiose
-
-
-
-
?
4-methylumbelliferyl beta-D-lactopyranoside + H2O
4-methylumbelliferone + lactose
-
-
-
?
4-methylumbelliferyl beta-D-lactopyranoside + H2O
4-methylumbelliferone + lactose
-
-
-
?
4-methylumbelliferyl beta-D-lactopyranoside + H2O
4-methylumbelliferone + lactose
-
-
-
?
4-methylumbelliferyl beta-D-lactopyranoside + H2O
4-methylumbelliferone + lactose
-
-
-
-
?
4-methylumbelliferyl beta-D-lactopyranoside + H2O
4-methylumbelliferone + lactose
-
-
-
?
4-methylumbelliferyl beta-D-lactopyranoside + H2O
4-methylumbelliferone + lactose
-
-
-
-
?
4-methylumbelliferyl beta-D-lactoside + H2O
4-methylumbelliferol + D-lactose
-
-
-
?
4-methylumbelliferyl beta-D-lactoside + H2O
4-methylumbelliferol + D-lactose
-
-
-
-
?
4-methylumbelliferyl beta-D-lactoside + H2O
4-methylumbelliferol + D-lactose
-
-
-
?
4-methylumbelliferyl beta-D-lactoside + H2O
4-methylumbelliferol + D-lactose
-
-
-
-
?
4-methylumbelliferyl beta-lactoside + H2O
4-methylumbelliferol + beta-lactose
-
-
-
-
?
4-methylumbelliferyl beta-lactoside + H2O
4-methylumbelliferol + beta-lactose
-
-
-
?
4-methylumbelliferyl lactoside + H2O
4-methylumbelliferone + lactose
-
-
-
-
?
4-methylumbelliferyl lactoside + H2O
4-methylumbelliferone + lactose
-
-
-
-
?
4-methylumbelliferyl lactoside + H2O
4-methylumbelliferone + lactose
Thermochaetoides thermophila
-
-
-
-
?
4-methylumbelliferyl lactoside + H2O
4-methylumbelliferone + lactose
-
-
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferol + beta-D-lactose
-
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferol + beta-D-lactose
-
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferol + beta-D-lactose
-
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferol + beta-D-lactose
-
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferol + beta-D-lactose
Thermochaetoides thermophila
-
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferol + beta-D-lactose
Thermochaetoides thermophila ALKO4265
-
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferol + beta-D-lactose
-
-
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferol + D-lactose
-
-
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferol + D-lactose
-
-
-
?
4-methylumbelliferyl-beta-D-lactoside + H2O
4-methylumbelliferol + D-lactose
-
-
-
?
4-nitrophenyl beta-D-cellobioside
4-nitrophenol + D-cellobiose
-
-
-
?
4-nitrophenyl beta-D-cellobioside
4-nitrophenol + D-cellobiose
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + beta-D-cellobiose
-
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
-
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
very low activity
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
0.9% activity compared to phosphoric acid-swollen cellulose
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
Thermothelomyces thermophilus DSM 1799
0.9% activity compared to phosphoric acid-swollen cellulose
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
-
minimal activity
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + D-cellobiose
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + D-cellobiose
Thermochaetoides thermophila
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + D-cellobiose
-
-
-
?
4-nitrophenyl beta-D-cellotetraoside + H2O
?
enzyme activity starts from the reducing end in a processive mode after making random cuts
-
-
?
4-nitrophenyl beta-D-cellotetraoside + H2O
?
enzyme activity starts from the reducing end in a processive mode after making random cuts
-
-
?
4-nitrophenyl beta-D-lactopyranoside + H2O
4-nitrophenol + beta-D-lactopyranose
-
-
-
?
4-nitrophenyl beta-D-lactopyranoside + H2O
4-nitrophenol + beta-D-lactopyranose
-
-
-
-
?
4-nitrophenyl beta-D-lactopyranoside + H2O
4-nitrophenol + beta-D-lactose
-
-
-
?
4-nitrophenyl beta-D-lactopyranoside + H2O
4-nitrophenol + beta-D-lactose
-
-
-
?
4-nitrophenyl beta-D-lactoside + H2O
4-nitrophenol + D-lactose
-
-
-
-
?
4-nitrophenyl beta-D-lactoside + H2O
4-nitrophenol + D-lactose
-
-
-
-
?
4-nitrophenyl beta-D-lactoside + H2O
4-nitrophenol + D-lactose
-
-
-
?
4-nitrophenyl beta-D-lactoside + H2O
4-nitrophenol + D-lactose
-
-
-
-
?
4-nitrophenyl beta-D-lactoside + H2O
4-nitrophenol + D-lactose
-
-
-
?
4-nitrophenyl beta-D-lactoside + H2O
4-nitrophenol + lactose
-
-
-
?
4-nitrophenyl beta-D-lactoside + H2O
4-nitrophenol + lactose
-
-
-
?
4-nitrophenyl cellopentaoside + H2O
4-nitrophenyl-cellobioside + cellotriose
-
-
-
?
4-nitrophenyl cellopentaoside + H2O
4-nitrophenyl-cellobioside + cellotriose
-
-
-
?
4-nitrophenyl cellotetraoside + H2O
4-nitrophenyl cellobioside + cellobiose
-
-
-
?
4-nitrophenyl cellotetraoside + H2O
4-nitrophenyl cellobioside + cellobiose
-
-
-
?
4-nitrophenyl cellotrioside + H2O
cellobiose + 4-nitrophenyl beta-D-glucoside
-
-
-
?
4-nitrophenyl cellotrioside + H2O
cellobiose + 4-nitrophenyl beta-D-glucoside
-
-
-
?
4-nitrophenyl D-cellobioside + H2O
4-nitrophenol + D-cellobiose
-
-
-
?
4-nitrophenyl D-cellobioside + H2O
4-nitrophenol + D-cellobiose
-
-
-
?
avicel + H2O
?
4% activity compared to phosphoric acid-swollen cellulose
-
-
?
avicel + H2O
?
Thermothelomyces thermophilus DSM 1799
4% activity compared to phosphoric acid-swollen cellulose
-
-
?
avicel + H2O
cellobiose + D-glucose + cellotriose
absorption to avicel at 4°C is 87.5%
-
-
?
avicel + H2O
cellobiose + D-glucose + cellotriose
absorption to avicel at 4°C is 87.5%
-
-
?
avicel + H2O
cellobiose + D-glucose + cellotriose
-
-
-
?
avicel + H2O
cellobiose + D-glucose + cellotriose
Thermochaetoides thermophila
absorption to avicel at 4°C is 84%
-
-
?
avicel + H2O
cellobiose + D-glucose + cellotriose
Thermochaetoides thermophila ALKO4265
absorption to avicel at 4°C is 84%
-
-
?
avicel + H2O
cellobiose + D-glucose + cellotriose
-
absorption to avicel at 4°C is 95.5%
-
-
?
bacterial cellulose + H2O
?
-
from Acetobacter xylinum strain ATCC53582
-
-
?
bacterial cellulose + H2O
?
-
from Acetobacter xylinum strain ATCC53582
-
-
?
bacterial cellulose + H2O
?
13% activity compared to phosphoric acid-swollen cellulose
-
-
?
bacterial cellulose + H2O
?
Thermothelomyces thermophilus DSM 1799
13% activity compared to phosphoric acid-swollen cellulose
-
-
?
bacterial cellulose + H2O
?
-
from cetobacter xylinum strain ATCC53582
-
-
?
bacterial cellulose + H2O
?
-
binding of enzyme to bacterial cellulose is only partially reversible
-
-
?
bacterial cellulose + H2O
?
-
binding of enzyme to bacterial cellulose is only partially reversible
-
-
?
bacterial microcrystalline cellulose + H2O
?
best substrate
-
-
?
bacterial microcrystalline cellulose + H2O
?
best substrate
-
-
?
cellooligosaccharide + H2O
cellobiose
-
degree of polymerization is 25
-
-
?
cellopentaose + H2O
?
Acetivibrio thermocellus DSM1313
-
about 75% activity compared to Avicel
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
-
cellobiose is released from the reducing end by exocellulase E4 (89%), cellopentaose is labeled at the reducing end with (18)O, the products are analyzed by ionspray mass spectrometry. This value is approximate since IS-MS is unable to detect glucose under the conditions used. As a result, this value is based only on the amount of (18)O present in CTet (20% of that present in the unreacted starting material)
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
-
cellobiose is preferentially released from the reducing end by CBH I (72%), cellopentaose is labeled at the reducing end with (18)O, the products are analyzed by ionspray mass spectrometry. This value is approximate since IS-MS is unable to detect glucose under the conditions used. As a result, this value is based only on the amount of (18)O present in CTet (20% of that present in the unreacted starting material)
-
-
?
cellotetraose + H2O
?
Acetivibrio thermocellus DSM1313
-
about 20% activity compared to Avicel
-
-
?
cellulose + H2O
?
cellobiohydrolases are exo-active glycosyl hydrolases that processively convert cellulose to soluble sugars, typically cellobiose. Occuring opposite effects on binding and activity by the enzyme can be reconciled if the rate-limiting step is after the catalysis (i.e. in the dissociation process), analysis of the rate-limiting step for cellobiohydrolases, overview
-
-
?
cellulose + H2O
?
-
hydrolysis of amorphous cellulose by different concentrations of enzyme using a cellobiose dehydrogenase biosensor, the enzyme TrCel7A is a retaining cellulase and therefore produces solely the beta-anomer
-
-
?
cellulose + H2O
?
-
functionally based kinetic model for enzymatic hydrolysis of pure cellulose
-
-
?
cellulose + H2O
cellobiose + ?
the recombinant gene product is active on cellodextrins, barley beta-glucan, carboxymethylcellulose and insoluble cellulose. Cellobiose is the only product released from amorphic and crystalline cellulose, cellotetraose and higher cellooligosaccharides. The cleavage pattern of p-nitrophenyl beta-D-cellotetraoside, blockage of the hydrolysis of NaBH4-reduced cellopentaose and the reduction in substrate viscosity suggests activity from the reducing end in a processive mode after making random cuts. Binding to insoluble, i.e. amorphous, and crystalline cellulose is mediated by the carbohydrate-binding module CBM3b, with a preference for the crystalline substrate
-
-
?
cellulose + H2O
cellobiose + ?
the recombinant gene product is active on cellodextrins, barley beta-glucan, carboxymethylcellulose and insoluble cellulose. Cellobiose is the only product released from amorphic and crystalline cellulose, cellotetraose and higher cellooligosaccharides. The cleavage pattern of p-nitrophenyl beta-D-cellotetraoside, blockage of the hydrolysis of NaBH4-reduced cellopentaose and the reduction in substrate viscosity suggests activity from the reducing end in a processive mode after making random cuts. Binding to insoluble, i.e. amorphous, and crystalline cellulose is mediated by the carbohydrate-binding module CBM3b, with a preference for the crystalline substrate
-
-
?
cellulose + H2O
cellobiose + ?
-
cellulolytic enzyme, the enzyme is active on most cellulosic substrates
-
-
?
cellulose + H2O
cellobiose + ?
-
cellulolytic enzyme, the enzyme is active on most cellulosic substrates
-
-
?
cellulose + H2O
cellobiose + ?
-
-
-
-
?
cellulose + H2O
cellobiose + ?
-
the enzyme hydrolyzes beta-1,4-linkages
-
-
?
cellulose + H2O
cellobiose + ?
-
Cel7A acts on labelled bacterial cellulose, bacterial microcrystalline cellulose and endoglucanase-pretreated bacterial cellulose respectively
-
-
?
cellulose + H2O
cellobiose + ?
-
Cel7A acts on labelled bacterial cellulose, bacterial microcrystalline cellulose and endoglucanase-pretreated bacterial cellulose respectively
-
-
?
cellulose + H2O
cellobiose + ?
-
cellulose Ialpha from Cladophora sp. and cellulose Ibeta from Halocynthia roretzi
-
-
?
cellulose + H2O
cellobiose + ?
substrate acid-swollen cellulose
-
-
?
cellulose + H2O
cellobiose + D-glucose + cellotriose
acid-swollen cellulose, bacterial microcrystlline cellulose
-
-
?
cellulose + H2O
cellobiose + D-glucose + cellotriose
acid-swollen cellulose, bacterial microcrystlline cellulose
-
-
?
cellulose + H2O
cellobiose + D-glucose + cellotriose
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + D-glucose + cellotriose
-
-
different combinations and proportions of products depending on organism
?
cellulose Ialpha + H2O
cellobiose + ?
different susceptibilities of cellulose Ialpha and IIII are highly dependent on enzyme concentration, and at nanomolar enzyme concentration, Cel7A shows similar rates of hydrolysis against cellulose Ialpha and IIII. At picomolar enzyme concentration, Cel7A displays similar binding and dissociation rate constants for cellulose Ialpha and IIII and similar fractions of productive binding. Once productively bound, Cel7A processively hydrolyzes and moves along cellulose Ialpha and IIII with similar translational rates
-
-
?
cellulose Ialpha + H2O
cellobiose + ?
different susceptibilities of cellulose Ialpha and IIII are highly dependent on enzyme concentration, and at nanomolar enzyme concentration, Cel7A shows similar rates of hydrolysis against cellulose Ialpha and IIII. At picomolar enzyme concentration, Cel7A displays similar binding and dissociation rate constants for cellulose Ialpha and IIII and similar fractions of productive binding. Once productively bound, Cel7A processively hydrolyzes and moves along cellulose Ialpha and IIII with similar translational rates
-
-
?
cellulose IIII + H2O
cellobiose + ?
different susceptibilities of cellulose Ialpha and IIII are highly dependent on enzyme concentration, and at nanomolar enzyme concentration, Cel7A shows similar rates of hydrolysis against cellulose Ialpha and IIII. At picomolar enzyme concentration, Cel7A displays similar binding and dissociation rate constants for cellulose Ialpha and IIII and similar fractions of productive binding. Once productively bound, Cel7A processively hydrolyzes and moves along cellulose Ialpha and IIII with similar translational rates
-
-
?
cellulose IIII + H2O
cellobiose + ?
different susceptibilities of cellulose Ialpha and IIII are highly dependent on enzyme concentration, and at nanomolar enzyme concentration, Cel7A shows similar rates of hydrolysis against cellulose Ialpha and IIII. At picomolar enzyme concentration, Cel7A displays similar binding and dissociation rate constants for cellulose Ialpha and IIII and similar fractions of productive binding. Once productively bound, Cel7A processively hydrolyzes and moves along cellulose Ialpha and IIII with similar translational rates
-
-
?
crystalline cellulose + H2O
?
-
the enzyme hydrolyzes only the hydrophobic faces of cellulose
-
-
?
crystalline cellulose + H2O
?
the enzyme shows processive hydrolysis by the catalytic domain and a sliding movement of single enzyme molecules on a highly crystalline cellulose surface, the cellulose-binding domain is unnecessary for the sliding movement, real-time monitoring by high-speed atomic force microscope
-
-
?
filter paper + H2O
?
21% activity compared to phosphoric acid-swollen cellulose
-
-
?
p-nitrophenyl beta-D-cellobioside + H2O
p-nitrophenol + beta-D-cellobiose
-
-
-
-
?
p-nitrophenyl beta-D-cellobioside + H2O
p-nitrophenol + beta-D-cellobiose
-
-
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + ?
-
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + D-glucose + cellotriose
-
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + D-glucose + cellotriose
-
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + D-glucose + cellotriose
-
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + D-glucose + cellotriose
-
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + D-glucose + cellotriose
-
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + D-glucose + cellotriose
Thermochaetoides thermophila
-
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + D-glucose + cellotriose
Thermochaetoides thermophila ALKO4265
-
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + D-glucose + cellotriose
-
-
-
-
?
phosphoric acid-swollen cellulose + H2O
?
-
about 30% activity compared to Avicel
-
-
?
phosphoric acid-swollen cellulose + H2O
?
100% activity
-
-
?
phosphoric acid-swollen cellulose + H2O
?
Thermothelomyces thermophilus DSM 1799
100% activity
-
-
?
pretreated corn stover + H2O
?
-
14% conversion, 24 h, 65°C, best performance of the tested enzymes
-
?
additional information
?
-
-
role in the cellusome, an active cellulase system
-
-
?
additional information
?
-
role in the cellusome, an active cellulase system
-
-
?
additional information
?
-
-
enzyme is exclusively an exocellulase
-
-
?
additional information
?
-
-
rCelO completely lacks chromogenic activity on the p-nitrophenyl-cellodextrins from p-nitrophenyl glucoside to 4-nitrophenyl cellopentaoside
-
-
?
additional information
?
-
rCelO completely lacks chromogenic activity on the p-nitrophenyl-cellodextrins from p-nitrophenyl glucoside to 4-nitrophenyl cellopentaoside
-
-
?
additional information
?
-
-
no activity with pectin, xylan, cellobiose and cellotriose
-
-
?
additional information
?
-
Acetivibrio thermocellus DSM1313
-
no activity with pectin, xylan, cellobiose and cellotriose
-
-
?
additional information
?
-
-
rCelO completely lacks chromogenic activity on the p-nitrophenyl-cellodextrins from p-nitrophenyl glucoside to 4-nitrophenyl cellopentaoside
-
-
?
additional information
?
-
rCelO completely lacks chromogenic activity on the p-nitrophenyl-cellodextrins from p-nitrophenyl glucoside to 4-nitrophenyl cellopentaoside
-
-
?
additional information
?
-
no activity with 4-methylumbelliferyl-beta-D-lactoside
-
-
?
additional information
?
-
no activity with 4-methylumbelliferyl-beta-D-lactoside
-
-
?
additional information
?
-
no activity with 4-methylumbelliferyl-beta-D-lactoside
-
-
?
additional information
?
-
no activity with 4-methylumbelliferyl-beta-D-lactoside
-
-
?
additional information
?
-
-
the full-length and mutant enzyme forms show similar substrate specificities
-
-
?
additional information
?
-
no substrate: beechwood xylan
-
-
?
additional information
?
-
no substrate: beechwood xylan
-
-
?
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
?
-
inability of Cel7B to hydrolyze cellotriose
-
-
?
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
?
-
-
no substrates: starch, xylan, cellobiose. Filter paper is a very poor substrate
-
-
?
additional information
?
-
no activity on carboxymethyl cellulose, cellobiose, cellotriose or 4-methylumbelliferyl alpha-D-glucoside
-
-
?
additional information
?
-
no activity on carboxymethyl cellulose, cellobiose, cellotriose or 4-methylumbelliferyl alpha-D-glucoside
-
-
?
additional information
?
-
substrate binding structure analysis of Cel7D
-
-
?
additional information
?
-
-
the enzyme employs reducing-end exo- and endo-mode initiation in parallel
-
-
?
additional information
?
-
-
the enzyme employs reducing-end exo- and endo-mode initiation in parallel
-
-
?
additional information
?
-
-
no hydrolysis of a soluble cellulose derivative and barley (1-3),(1-4)-beta-D-glucan
-
-
?
additional information
?
-
no hydrolysis of a soluble cellulose derivative and barley (1-3),(1-4)-beta-D-glucan
-
-
?
additional information
?
-
-
no substrates: carboxymethyl cellulose, 4-nitrophenyl-beta-D-glucopyranoside and 4-nitrophenyl-beta-D-galactopyranoside
-
-
?
additional information
?
-
-
no activity with carboxymethyl cellulose, 4-nitrophenyl beta-D-glucopyranoside, and 4-nitrophenyl beta-D-galactopyranoside
-
-
?
additional information
?
-
Cel48A does not cleave cellotriose. No reaction at all with 4-methylumbelliferyl cellobioside and very low activity with 4-methylumbelliferyl cellotrioside
-
-
?
additional information
?
-
Thermochaetoides thermophila
-
enzyme degrades highly ordered crystalline forms of cellulose, i.e., cotton, microcrystalline cellulose, and Whatman CCAI cellulose, more readily than soluble polysaccharides such as lichenan, glucan, xylan and carboxymethylcellulose
-
-
?
additional information
?
-
no substrate: avicel
-
-
?
additional information
?
-
-
no detectable hydrolysis is observed with carboxymethylcellulose, laminarin and p-nitrophenyl beta-D-glucopyranoside
-
-
?
additional information
?
-
-
the enzyme is efficient in hydrolyzing crystalline cellulosic substrates, such as Avicel and Sigmacell 20, but is not effective in the hydrolysis of substituted substrates, such as caboxymethyl cellulose
-
-
?
additional information
?
-
the enzyme is efficient in hydrolyzing crystalline cellulosic substrates, such as Avicel and Sigmacell 20, but is not effective in the hydrolysis of substituted substrates, such as caboxymethyl cellulose
-
-
?
additional information
?
-
-
the enzyme is efficient in hydrolyzing crystalline cellulosic substrates, such as Avicel and Sigmacell 20, but is not effective in the hydrolysis of substituted substrates, such as caboxymethyl cellulose
-
-
?
additional information
?
-
the enzyme is efficient in hydrolyzing crystalline cellulosic substrates, such as Avicel and Sigmacell 20, but is not effective in the hydrolysis of substituted substrates, such as caboxymethyl cellulose
-
-
?
additional information
?
-
-
the enzyme employs reducing-end exo- and endo-mode initiation in parallel
-
-
?
additional information
?
-
-
the enzyme has the ability to degrade highly crystalline cellulose. The catalytic domain and the cellulose-binding domain are both necessary for full activity on crystalline substrates
-
-
?
additional information
?
-
the enzyme has the ability to degrade highly crystalline cellulose. The catalytic domain and the cellulose-binding domain are both necessary for full activity on crystalline substrates
-
-
?
additional information
?
-
binding properties between the cellulose binding module Cel7A and cellulose substrates, e.g. crystalline cellulose, microcrystalline cellulose Avicel PH101, partially crystalline cellulose, and phosphoric acid swollen amorphous cellulose, thermodynamics, overview. Binding between cellulose binding module CBMCel7A and cellulose to some extent relates to the crystallinity of cellulose
-
-
?
additional information
?
-
-
comparison of activities of the wild-type and mutangt W40A enzymes (with and without the cellulose-binding domain) for various substrates, overview
-
-
?
additional information
?
-
comparison of activities of the wild-type and mutangt W40A enzymes (with and without the cellulose-binding domain) for various substrates, overview
-
-
?
additional information
?
-
enzyme Cel7A hydrolyses the cellulose from the reducing chain end in a processive manner
-
-
?
additional information
?
-
use of an optical tweezers-based single-molecule motility assay for precision tracking of Cel7A. Direct observation of motility during degradation reveals processive runs and distinct steps on the scale of 1 nm. Cel7A is not mechanically limited, can work against 20 pN loads and speeds up when assisted. The fundamental stepping cycle likely includes energy from glycosidic bonds and other sources. The catalytic domain alone is sufficient for processive motion
-
-
?
additional information
?
-
-
binding constant to crystalline cellulose nanowhiskers is about 100000 per M for CBMCel7A. For Avicel, lower binding constants are observed, and weak binding to phosphoric acid swollen cellulose. No binding of cellooligosaccharides of less than two glucose units
-
-
?
additional information
?
-
-
the catalytic domain of CBMCel7A hydrolyzes cellulose from the reducing ends. When the whole enzyme is aligned with the cellulose chain, the binding domain may recognize and bind to the nonreducing end other than the reducing end, and help to accommodate catalytic module to the reducing ends
-
-
?
additional information
?
-
use of an optical tweezers-based single-molecule motility assay for precision tracking of Cel7A. Direct observation of motility during degradation reveals processive runs and distinct steps on the scale of 1 nm. Cel7A is not mechanically limited, can work against 20 pN loads and speeds up when assisted. The fundamental stepping cycle likely includes energy from glycosidic bonds and other sources. The catalytic domain alone is sufficient for processive motion
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
Avicel PH 101 + H2O
?
cellobiose production is monitored by an amperometric enzyme biosensor based on cellobiose dehydrogenase from Phanerochaete chrysosporium adsorbed onto the surface of a benzoquinone-modified carbon paste electrode
-
-
?
cellulose + H2O
alpha-cellobiose + beta-cellobiose
the enzyme hydrolyzes the beta-1,4 linkages of a cellulose chain from its reducing end via a retaining mechanism liberating the product, which consists of roughly 63% beta-cellobiose and 37% alpha-cellobiose
-
-
?
bacterial cellulose + H2O
?
-
from Acetobacter xylinum strain ATCC53582
-
-
?
bacterial cellulose + H2O
?
-
from Acetobacter xylinum strain ATCC53582
-
-
?
bacterial cellulose + H2O
?
-
from cetobacter xylinum strain ATCC53582
-
-
?
cellulose + H2O
?
cellobiohydrolases are exo-active glycosyl hydrolases that processively convert cellulose to soluble sugars, typically cellobiose. Occuring opposite effects on binding and activity by the enzyme can be reconciled if the rate-limiting step is after the catalysis (i.e. in the dissociation process), analysis of the rate-limiting step for cellobiohydrolases, overview
-
-
?
cellulose + H2O
cellobiose + ?
-
cellulolytic enzyme, the enzyme is active on most cellulosic substrates
-
-
?
cellulose + H2O
cellobiose + ?
-
cellulolytic enzyme, the enzyme is active on most cellulosic substrates
-
-
?
cellulose + H2O
cellobiose + ?
-
-
-
-
?
cellulose + H2O
cellobiose + ?
-
the enzyme hydrolyzes beta-1,4-linkages
-
-
?
additional information
?
-
-
role in the cellusome, an active cellulase system
-
-
?
additional information
?
-
role in the cellusome, an active cellulase system
-
-
?
additional information
?
-
-
the enzyme employs reducing-end exo- and endo-mode initiation in parallel
-
-
?
additional information
?
-
-
the enzyme employs reducing-end exo- and endo-mode initiation in parallel
-
-
?
additional information
?
-
-
the enzyme employs reducing-end exo- and endo-mode initiation in parallel
-
-
?
additional information
?
-
-
the enzyme has the ability to degrade highly crystalline cellulose. The catalytic domain and the cellulose-binding domain are both necessary for full activity on crystalline substrates
-
-
?
additional information
?
-
the enzyme has the ability to degrade highly crystalline cellulose. The catalytic domain and the cellulose-binding domain are both necessary for full activity on crystalline substrates
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,3-dimethylimidazolium dimethylphosphate
complete inhibition at 30% v/v, ionic liquids inactivate cellulases, the enzyme is sensitive against 1,3-dimethylimidazolium dimethylphosphate and 1-ethyl-3-methylimidazolium acetate, effects on cellulase substrate binding, overview
1-ethyl-3-methylimidazolium acetate
complete inhibition at 30% v/v, ionic liquids inactivate cellulases, the enzyme is sensitive against 1,3-dimethylimidazolium dimethylphosphate and 1-ethyl-3-methylimidazolium acetate, effects on cellulase substrate binding, overview
cellobioimidazole
i.e. (5R,6R,7S,8S)-6-(beta-D-glucopyranosyloxy)-5,6,7,8-tetrahydro-5-[(hydroxy)methyl]imidazol[1,2a] pyridine-7,8-diol, the disaccharide binds in the glycosyl-binding subsites +1 and +2 close to the exit of the cellulose-binding tunnel/cleft of Cel7D, binding structure analysis
methyl (4S)-beta-cellobiosyl-4-thio-beta-cellobioside
a thio-linked substrate analogue, the disaccharide binds in the glycosyl-binding subsites +1 and +2 close to the exit of the cellulose-binding tunnel/cleft of Cel7D, binding structure analysis
cellobiose
inhibits recombinant CelS activity on cellopentaose. Complete inhibition at 10 mg/ml cellobiose. Cellobiose appeared to inhibit the CelS activity through a competitive mechanism. The inhibition is relieved when beta-glucosidase is added, presumably because of the conversion of cellobiose into glucose
cellobiose
-
effectively inhibited by cellobiose at concentrations of 3000-12000 ppm
cellobiose
-
strong inhibitor for the hydrolysis of 4-nitrophenyl beta-D-lactoside
cellobiose
competitive with wild-type enzyme, mixed inhibition with mutant enzyme
cellobiose
-
strong inhibitor for the hydrolysis of 4-nitrophenyl beta-D-lactoside
cellobiose
competitive with respect to 4-nitrophenyl beta-D-lactoside, noncompetitive with respect to avicel
Fe2+
93% residual activity at 1 mM; % residual activity at 1 mM
lactose
inhibits recombinant CelS activity on cellopentaose, 81% inhibition at 20 mg/ml lactose
lactose
the disaccharide binds in the glycosyl-binding subsites +1 and +2 close to the exit of the cellulose-binding tunnel/cleft of Cel7D, binding structure analysis
lignin
-
increase in temperature from 45 to 65°C increases the inhibitory effect of lignin
-
lignin
-
increase in temperature from 45 to 65°C increases the inhibitory effect of lignin
-
additional information
-
the enzyme activity cannot be efficiently inhibited at low D-glucose concentrations
-
additional information
-
4-nitrophenyl beta-D-lactoside (0.5 mM) does not influence the hydrolysis of cellulose
-
additional information
-
Cel7A tends to be strongly inhibited by its reaction products, is only moderately stable, and has a narrow pH range for activity
-
additional information
-
4-nitrophenyl beta-D-lactoside (0.5 mM) does not influence the hydrolysis of cellulose
-
additional information
-
4-methylumbelliferyl beta-D-lactoside substrate inhibition
-
additional information
4-methylumbelliferyl beta-D-lactoside substrate inhibition
-
additional information
-
when the enzyme is supplemented with a mixture of inhibitors (0.5 mg/ml lignin, 0.5 mg/ml hemicelluloses, and 0.5 mM hemicellulose oligomers), 60% of the original cellobiohydrolase activity is lost
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
not influenced by 2-mercaptoethanol
-
additional information
-
overexpression of the protein disulfide isomerase Sc-PDI1 and the plasma membrane targeting soluble N-ethylmaleimide-sensitive factor attachment protein receptor Sc-SSO1, and disruption of the sorting receptor Sc-VPS10 and a Ca2D/Mn2D ATPase Sc-PMR1, improve respectively the extracellular Tr-Cel7A activities
-
additional information
overexpression of the protein disulfide isomerase Sc-PDI1 and the plasma membrane targeting soluble N-ethylmaleimide-sensitive factor attachment protein receptor Sc-SSO1, and disruption of the sorting receptor Sc-VPS10 and a Ca2D/Mn2D ATPase Sc-PMR1, improve respectively the extracellular Tr-Cel7A activities
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acquired Immunodeficiency Syndrome
Consideration in selecting crops for the human-rated life support system: a Linear Programming model.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.84
2-chloro-4-nitrophenyl beta-D-cellobioside
catalyticdomain, pH 5.0, 37°C
0.28
4-methylumbelliferyl beta-D-cellobioside
pH 5.0, 55°C
0.0125
4-trifluoromethylumbelliferyl beta-cellobioside
-
at pH 5.0 and 10°C
0.004
4-trifluoromethylumbelliferyl beta-cellotrioside
-
at pH 5.0 and 10°C
1.4
cellopentaose
pH 5.7, temperature not specified in the publication
0.62
2-chloro-4-nitrophenyl beta-D-lactoside
wild-type, pH 6.0, 22°C
0.75
2-chloro-4-nitrophenyl beta-D-lactoside
mutant G4C/M70C/S290T, pH 6.0, 22°C
1
2-chloro-4-nitrophenyl beta-D-lactoside
mutant G4C/M70C, pH 6.0, 22°C
1.16
2-chloro-4-nitrophenyl beta-D-lactoside
mutant S290T, pH 6.0, 22°C
3.7
2-chloro-4-nitrophenyl beta-D-lactoside
50 mM sodium acetate buffer, pH 5.0, at 50°C
0.46
2-chloro-4-nitrophenyl beta-lactoside
-
pH 5.7, 37°C, wild-type enzyme
0.52
2-chloro-4-nitrophenyl-beta-D-lactoside
-
in 50 mM sodium phosphate buffer, pH 5.7, at 22°C
0.62
2-chloro-4-nitrophenyl-beta-D-lactoside
-
Cel7B wild-type expressed in Trichoderma reesei, at 22°C, pH 6.0
0.75
2-chloro-4-nitrophenyl-beta-D-lactoside
-
Cel7B mutant S290T/G4C/M70C expressed in Saccharomyces cerevisiae, at 22°C, pH 6.0
0.8
2-chloro-4-nitrophenyl-beta-D-lactoside
-
Cel7B wild-type expressed in Saccharomyces cerevisiae, at 22°C, pH 6.0
0.99
2-chloro-4-nitrophenyl-beta-D-lactoside
in 50 mM sodium phosphate buffer, pH 5.7, at 22°C
1
2-chloro-4-nitrophenyl-beta-D-lactoside
-
Cel7B mutant G4C/M70C expressed in Saccharomyces cerevisiae, at 22°C, pH 6.0
1.16
2-chloro-4-nitrophenyl-beta-D-lactoside
-
Cel7B mutant S290T expressed in Saccharomyces cerevisiae, at 22°C, pH 6.0
2
2-chloro-4-nitrophenyl-beta-D-lactoside
Thermochaetoides thermophila
in 50 mM sodium phosphate buffer, pH 5.7, at 22°C
2.1
2-chloro-4-nitrophenyl-beta-D-lactoside
in 50 mM sodium phosphate buffer, pH 5.7, at 22°C
48
3,4-dinitrophenyl-cellobioside
25°C, pH 5, E223S/A224H/L225V/T226A/D262G mutant
161
3,4-dinitrophenyl-cellobioside
25°C, pH 7, E223S/A224H/L225V/T226A/D262G mutant
543
3,4-dinitrophenyl-lactoside
25°C, pH 5, E223S/A224H/L225V/T226A/D262G mutant
0.23
4-methylumbelliferyl beta-D-lactopyranoside
wild-type, pH 6.0, 22°C
0.28
4-methylumbelliferyl beta-D-lactopyranoside
mutant S290T, pH 6.0, 22°C
0.3
4-methylumbelliferyl beta-D-lactopyranoside
mutant G4C/M70C, pH 6.0, 22°C
0.3
4-methylumbelliferyl beta-D-lactopyranoside
mutant G4C/M70C/S290T, pH 6.0, 22°C
0.318
4-methylumbelliferyl beta-D-lactopyranoside
mutant enzyme W40A, at pH 5.0 and 27°C
0.358
4-methylumbelliferyl beta-D-lactopyranoside
wild type enzyme, at pH 5.0 and 27°C
0.293
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 27°C, recombinant mutant W40A enzyme catalytic domain
0.318
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 27°C, recombinant mutant W40A enzyme
0.335
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 27°C, recombinant wild-type enzyme catalytic domain
0.358
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 27°C, recombinant wild-type enzyme
0.56
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 22°C, fusion protein with CBM1 from Hypocrea jecorina Cel7A containing an additional S-S bridge in the catalytic module
0.88
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 22°C, wild-type
0.96
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 45°C, wild-type
1.1
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 45°C, fusion protein with CBM1 from Hypocrea jecorina Cel7A containing an additional S-S bridge in the catalytic module
2.1
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 60°C, wild-type
0.22
4-methylumbelliferyl-beta-D-lactoside
in 50 mM sodium acetate buffer, pH 5.0, at 22°C
0.221
4-methylumbelliferyl-beta-D-lactoside
Thermochaetoides thermophila
in 50 mM sodium acetate buffer, pH 5.0, at 22°C
0.23
4-methylumbelliferyl-beta-D-lactoside
-
Cel7B wild-type expressed in Trichoderma reesei, at 22°C, pH 6.0
0.268
4-methylumbelliferyl-beta-D-lactoside
in 50 mM sodium acetate buffer, pH 5.0, at 22°C
0.28
4-methylumbelliferyl-beta-D-lactoside
-
Cel7B mutant S290T expressed in Saccharomyces cerevisiae, at 22°C, pH 6.0
0.28
4-methylumbelliferyl-beta-D-lactoside
-
Cel7B wild-type expressed in Saccharomyces cerevisiae, at 22°C, pH 6.0
0.287
4-methylumbelliferyl-beta-D-lactoside
-
in 50 mM sodium acetate buffer, pH 5.0, at 22°C
0.3
4-methylumbelliferyl-beta-D-lactoside
-
Cel7B mutant G4C/M70C expressed in Saccharomyces cerevisiae, at 22°C, pH 6.0
0.3
4-methylumbelliferyl-beta-D-lactoside
-
Cel7B mutant S290T/G4C/M70C expressed in Saccharomyces cerevisiae, at 22°C, pH 6.0
0.57
4-nitrophenyl beta-D-cellobioside
at 50°C in 50 mM sodium acetate (pH 5.0)
0.76
4-nitrophenyl beta-D-cellobioside
pH 5.0, 50°C, presence of 1 mM mannotetraose
0.81
4-nitrophenyl beta-D-cellobioside
pH 5.0, 50°C, presence of 1 mM mannotriose
0.85
4-nitrophenyl beta-D-cellobioside
catalyticdomain, pH 5.0, 37°C
0.87
4-nitrophenyl beta-D-cellobioside
pH 5.0, 50°C, presence of 1 mM mannobiose
1.02
4-nitrophenyl beta-D-cellobioside
pH 5.0, 50°C, presence of 2 mM mannobiose
3.4
4-nitrophenyl beta-D-cellobioside
50 mM sodium acetate buffer, pH 5.0, at 50°C
1.07
4-nitrophenyl beta-D-lactoside
catalyticdomain, pH 5.0, 37°C
3.4
4-nitrophenyl beta-D-lactoside
pH 5.0, 45°C, recombinant protein carrying Hypocrea jecorina carbohydrate-binding module and linker
3.4
4-nitrophenyl beta-D-lactoside
pH 5.0, 45°C, recombinant protein carrying Hypocrea jecorina carbohydrate-binding module and linker
0.44
4-nitrophenyl D-cellobioside
-
in the presence of 1 mM Tween 80, at pH 5.0 and 50°C
0.81
4-nitrophenyl D-cellobioside
-
in the absence of Tween 80, at pH 5.0 and 50°C
additional information
Avicel
Km value of the full-length enzyme increases from 2.8 g/l, pH 5.0, 10°C, to 19 g/l, pH 5.0, 50°C
-
additional information
Avicel
Km value of the full-length enzyme increases from 2.8 g/l, pH 5.0, 10°C, to 29 g/l, pH 5.0, 50°C
-
additional information
Avicel
Km value of the isolated catalytic domain increases from 4.9 g/l, pH 5.0, 10°C, to 76 g/l, pH 5.0, 50°C
-
additional information
Avicel
Km value of the isolated catalytic domain increases from 7.1 g/l, pH 5.0, 10°C, to 122 g/l, pH 5.0, 50°C
-
additional information
additional information
-
Michaelis-Menten kinetic
-
additional information
additional information
Michaelis-Menten kinetic
-
additional information
additional information
-
detailed kinetic analysis of wild-type enzyme and mutants E212Q, D214N, and E217Q
-
additional information
additional information
-
bacterial cellulose binding at low nanomolar free enzyme concentrations is exclusively active site-mediated and is consistent with Langmuir's one binding site model, strongest binding observed with non-complexed cellulases, productive binding of te enzyme to cellulose chain ends on the hydrophobic face of bacterial cellulose microfibril. With increasing free TrCel7A concentrations the isotherm gradually deviates from the Langmuir's one binding site model caused by the increasing contribution of lower affinity binding modes that included both active site-mediated binding and non-productive binding with active site free from cellulose chain. The binding of enzyme to bacterial cellulose is only partially reversible. Measurement of binding kinetics and modelling, overview
-
additional information
additional information
comparative analysis of steady-state kinetics, adsorption, and processivity for wild-type enzyme and the W38A variant, full-length enzymes and catalytic domains with substrate Avicel PH 101, detailed overiew
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.11
2-chloro-4-nitrophenyl beta-D-cellobioside
catalyticdomain, pH 5.0, 37°C
0.35
4-methylumbelliferyl beta-D-cellobioside
pH 5.0, 55°C
2.4
bacterial microcrystalline cellulose
-
in 50 mM sodium acetate with 2 mM CaCl2 and pH 5.0 at 25°C
-
0.017
2-chloro-4-nitrophenyl beta-D-lactoside
wild-type, pH 6.0, 22°C
0.02
2-chloro-4-nitrophenyl beta-D-lactoside
mutant S290T, pH 6.0, 22°C
0.165
2-chloro-4-nitrophenyl beta-D-lactoside
mutant G4C/M70C/S290T, pH 6.0, 22°C
0.182
2-chloro-4-nitrophenyl beta-D-lactoside
mutant G4C/M70C, pH 6.0, 22°C
0.74
2-chloro-4-nitrophenyl beta-D-lactoside
50 mM sodium acetate buffer, pH 5.0, at 50°C
12.8
2-chloro-4-nitrophenyl beta-lactoside
-
pH 5.7, 37°C, wild-type enzyme
0.0153
2-chloro-4-nitrophenyl-beta-D-lactoside
-
Cel7B wild-type expressed in Saccharomyces cerevisiae, at 22°C, pH 6.0
0.0165
2-chloro-4-nitrophenyl-beta-D-lactoside
-
Cel7B mutant S290T/G4C/M70C expressed in Saccharomyces cerevisiae, at 22°C, pH 6.0
0.0167
2-chloro-4-nitrophenyl-beta-D-lactoside
-
Cel7B wild-type expressed in Trichoderma reesei, at 22°C, pH 6.0
0.01817
2-chloro-4-nitrophenyl-beta-D-lactoside
-
Cel7B mutant G4C/M70C expressed in Saccharomyces cerevisiae, at 22°C, pH 6.0
0.0205
2-chloro-4-nitrophenyl-beta-D-lactoside
-
Cel7B mutant S290T expressed in Saccharomyces cerevisiae, at 22°C, pH 6.0
0.0283
2-chloro-4-nitrophenyl-beta-D-lactoside
in 50 mM sodium phosphate buffer, pH 5.7, at 22°C
0.043
2-chloro-4-nitrophenyl-beta-D-lactoside
-
in 50 mM sodium phosphate buffer, pH 5.7, at 22°C
0.0467
2-chloro-4-nitrophenyl-beta-D-lactoside
in 50 mM sodium phosphate buffer, pH 5.7, at 22°C
0.3167
2-chloro-4-nitrophenyl-beta-D-lactoside
Thermochaetoides thermophila
in 50 mM sodium phosphate buffer, pH 5.7, at 22°C
0.08
4-methylumbelliferyl beta-D-lactopyranoside
mutant G4C/M70C, pH 6.0, 22°C
0.11
4-methylumbelliferyl beta-D-lactopyranoside
mutant S290T, pH 6.0, 22°C
0.12
4-methylumbelliferyl beta-D-lactopyranoside
mutant G4C/M70C/S290T, pH 6.0, 22°C
0.14
4-methylumbelliferyl beta-D-lactopyranoside
wild-type, pH 6.0, 22°C
0.33
4-methylumbelliferyl beta-D-lactopyranoside
mutant enzyme W40A, at pH 5.0 and 27°C
0.49
4-methylumbelliferyl beta-D-lactopyranoside
wild type enzyme, at pH 5.0 and 27°C
0.055
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 22°C, wild-type
0.31
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 45°C, wild-type
0.33
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 27°C, recombinant mutant W40A enzyme
0.361
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 27°C, recombinant mutant W40A enzyme catalytic domain
0.415
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 27°C, recombinant wild-type enzyme catalytic domain
0.435
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 45°C, fusion protein with CBM1 from Hypocrea jecorina Cel7A containing an additional S-S bridge in the catalytic module
0.492
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 27°C, recombinant wild-type enzyme
0.65
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 22°C, fusion protein with CBM1 from Hypocrea jecorina Cel7A containing an additional S-S bridge in the catalytic module
1.35
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 60°C, wild-type
0.083
4-methylumbelliferyl-beta-D-lactoside
-
Cel7B mutant G4C/M70C expressed in Saccharomyces cerevisiae, at 22°C, pH 6.0
0.1067
4-methylumbelliferyl-beta-D-lactoside
-
Cel7B wild-type expressed in Saccharomyces cerevisiae, at 22°C, pH 6.0
0.1083
4-methylumbelliferyl-beta-D-lactoside
-
Cel7B mutant S290T expressed in Saccharomyces cerevisiae, at 22°C, pH 6.0
0.12
4-methylumbelliferyl-beta-D-lactoside
-
Cel7B mutant S290T/G4C/M70C expressed in Saccharomyces cerevisiae, at 22°C, pH 6.0
0.143
4-methylumbelliferyl-beta-D-lactoside
-
Cel7B wild-type expressed in Trichoderma reesei, at 22°C, pH 6.0
0.1883
4-methylumbelliferyl-beta-D-lactoside
in 50 mM sodium acetate buffer, pH 5.0, at 22°C
0.325
4-methylumbelliferyl-beta-D-lactoside
in 50 mM sodium acetate buffer, pH 5.0, at 22°C
0.4783
4-methylumbelliferyl-beta-D-lactoside
-
in 50 mM sodium acetate buffer, pH 5.0, at 22°C
1.15
4-methylumbelliferyl-beta-D-lactoside
Thermochaetoides thermophila
in 50 mM sodium acetate buffer, pH 5.0, at 22°C
0.1
4-nitrophenyl beta-D-cellobioside
catalyticdomain, pH 5.0, 37°C
0.112
4-nitrophenyl beta-D-cellobioside
at 50°C in 50 mM sodium acetate (pH 5.0)
0.39
4-nitrophenyl beta-D-cellobioside
50 mM sodium acetate buffer, pH 5.0, at 50°C
0.19
4-nitrophenyl beta-D-lactoside
catalyticdomain, pH 5.0, 37°C
0.27
4-nitrophenyl beta-D-lactoside
pH 5.0, 45°C, recombinant protein carrying Hypocrea jecorina carbohydrate-binding module and linker
0.51
4-nitrophenyl beta-D-lactoside
pH 5.0, 45°C, recombinant protein carrying Hypocrea jecorina carbohydrate-binding module and linker
2
amorphous cellulose
-
in 50 mM sodium acetate, pH 5.0, at 30°C
-
5.1
amorphous cellulose
-
in 50 mM sodium acetate with 2 mM CaCl2 and pH 5.0 at 25°C
-
4.75
Avicel
-
in 50 mM sodium acetate with 2 mM CaCl2 and pH 5.0 at 25°C
-
2.6
bacterial cellulose
-
in 50 mM sodium acetate, pH 5.0, at 30°C
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.131
2-chloro-4-nitrophenyl beta-D-cellobioside
catalyticdomain, pH 5.0, 37°C
0.178
4-nitrophenyl beta-D-lactoside
catalyticdomain, pH 5.0, 37°C
0.017
2-chloro-4-nitrophenyl beta-D-lactoside
mutant G4C/M70C, pH 6.0, 22°C
0.017
2-chloro-4-nitrophenyl beta-D-lactoside
mutant S290T, pH 6.0, 22°C
0.022
2-chloro-4-nitrophenyl beta-D-lactoside
mutant G4C/M70C/S290T, pH 6.0, 22°C
0.027
2-chloro-4-nitrophenyl beta-D-lactoside
wild-type, pH 6.0, 22°C
0.27
4-methylumbelliferyl beta-D-lactopyranoside
mutant G4C/M70C, pH 6.0, 22°C
0.38
4-methylumbelliferyl beta-D-lactopyranoside
mutant S290T, pH 6.0, 22°C
0.4
4-methylumbelliferyl beta-D-lactopyranoside
mutant G4C/M70C/S290T, pH 6.0, 22°C
0.62
4-methylumbelliferyl beta-D-lactopyranoside
wild-type, pH 6.0, 22°C
1.03
4-methylumbelliferyl beta-D-lactopyranoside
mutant enzyme W40A, at pH 5.0 and 27°C
1.37
4-methylumbelliferyl beta-D-lactopyranoside
wild type enzyme, at pH 5.0 and 27°C
0.063
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 22°C, wild-type
0.12
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 22°C, fusion protein with CBM1 from Hypocrea jecorina Cel7A containing an additional S-S bridge in the catalytic module
0.32
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 45°C, wild-type
0.42
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 45°C, fusion protein with CBM1 from Hypocrea jecorina Cel7A containing an additional S-S bridge in the catalytic module
0.72
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 60°C, wild-type
1.03
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 27°C, recombinant mutant W40A enzyme
1.23
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 27°C, recombinant mutant W40A enzyme catalytic domain
1.23
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 27°C, recombinant wild-type enzyme catalytic domain
1.37
4-methylumbelliferyl beta-D-lactoside
pH 5.0, 27°C, recombinant wild-type enzyme
0.118
4-nitrophenyl beta-D-cellobioside
catalyticdomain, pH 5.0, 37°C
0.196
4-nitrophenyl beta-D-cellobioside
at 50°C in 50 mM sodium acetate (pH 5.0)
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
birchwood xylan
Kic 0.093 g/l, Kiu 0.18 g/l, pH 5.0, 37°C
-
0.0055
cellobiose
-
Cel7B mutant G4C/M70C expressed in Saccharomyces cerevisiae, at 22°C, pH 6.0
0.006
cellobiose
-
Cel7B wild-type expressed in Trichoderma reesei, at 22°C, pH 6.0
0.0063
cellobiose
-
Cel7B wild-type expressed in Saccharomyces cerevisiae, at 22°C, pH 6.0
0.0066
cellobiose
-
Cel7B mutant S290T expressed in Saccharomyces cerevisiae, at 22°C, pH 6.0
0.019
cellobiose
-
Cel7B mutant S290T/G4C/M70C expressed in Saccharomyces cerevisiae, at 22°C, pH 6.0
0.13
cellobiose
pH 5.0, 45°C, recombinant protein carrying Hypocrea jecorina carbohydrate-binding module and linker
0.183
cellobiose
pH 5.0, 45°C, fusion protein with CBM1 from Hypocrea jecorina Cel7A containing an additional S-S bridge in the catalytic module
0.295
cellobiose
pH 5.0, 45°C, recombinant protein carrying Hypocrea jecorina carbohydrate-binding module and linker
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.028
0.036
0.038
0.039
0.041
0.044
0.047
0.117
0.17
0.19
0.2
0.22
0.51
pH 5.0, 22°C, fusion protein with CBM1 from Hypocrea jecorina Cel7A
0.52
pH 5.0, 22°C, fusion protein with CBM3 derived from Clostridium thermocellum cellulosomal-scaffolding protein CipA
0.53
pH 5.0, 22°C, fusion protein with CBM1 from Hypocrea jecorina Cel7A containing an additional S-S bridge in the catalytic module
0.56
pH 5.0, 22°C, fusion protein with CBM2 from Cellulomonas fimi xylanase 10A
0.57
pH 5.0, 22°C, fusion protein with CBM3 derived from Clostridium thermocellum cellulosomal-scaffolding protein CipA containing an additional S-S bridge in the catalytic module
275000
substrate phosphoric acid swollen cellulose, pH 5.0, 37°C
additional information
0.028
-
substrate 4-nitrophenyl beta-D-lactoside, wild-type, pH 5, 50°C
0.028
-
wild type enzyme, with 4-nitrophenyl beta-D-lactoside as substrate, at pH 4.0 and 40°C
0.036
-
substrate 4-nitrophenyl beta-D-lactoside, mutant N194A, pH 5, 50°C
0.036
-
mutant enzyme N194A, with 4-nitrophenyl beta-D-lactoside as substrate, at pH 4.0 and 40°C
0.038
-
substrate 4-nitrophenyl beta-D-lactoside, mutant N45A, pH 5, 50°C
0.038
-
mutant enzyme N45A, with 4-nitrophenyl beta-D-lactoside as substrate, at pH 4.0 and 40°C
0.039
-
substrate 4-nitrophenyl beta-D-lactoside, mutant N388A, pH 5, 50°C
0.039
-
mutant enzyme N388A, with 4-nitrophenyl beta-D-lactoside as substrate, at pH 4.0 and 40°C
0.041
-
mutant enzyme N388A, with beta-glucan as substrate, at pH 4.0 and 40°C
0.044
-
mutant enzyme N194A, with beta-glucan as substrate, at pH 4.0 and 40°C
0.047
-
wild type enzyme, with beta-glucan as substrate, at pH 4.0 and 40°C
0.117
-
mutant enzyme N45A, with beta-glucan as substrate, at pH 4.0 and 40°C
0.17
-
mutant enzyme N194A, with Avicel as substrate, at pH 4.0 and 40°C
0.19
-
mutant enzyme N388A, with Avicel as substrate, at pH 4.0 and 40°C
0.2
-
wild type enzyme, with Avicel as substrate, at pH 4.0 and 40°C
0.22
-
mutant enzyme N45A, with Avicel as substrate, at pH 4.0 and 40°C
additional information
-
melting temperatures, recombinant expression in Saccharomyces cerevisiae and in Neurospora crassa. The Cel7A expressed in Neurospora crassa has a by 10°C higher melting temperature and higher specific activity than the Cel7A expressed in Saccharomyces cerevisiae
additional information
-
the processive action of reducing-end-specific Trichoderma reesei cellobiohydrolase Cel7A on derivatized cellulose model substrates allows to perform an active-site titration, which in turn can be used to quantify the processivity of the enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 6.5
4 - 8
5 - 6
5.7
5
recombinant protein carrying Hypocrea jecorina carbohydrate-binding module and linker
5
recombinant protein carrying Hypocrea jecorina carbohydrate-binding module and linker
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 6
4.5 - 7
-
more than 85% activity between pH 4.5 and 6.5, about 75% activity at pH 7.0
5 - 9
pH 5: about 45% of maximal activity, pH 9.0: about 45% of maximal activity
3 - 6
about 65% activity at pH 3.0, 71% activity at pH 5.0, 23% activityat pH 6.0
3 - 6
recombinant enzyme, activity range, 76% of maximal activity at pH 3..0, inactive at pH 7.0, profile overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
45
50
55
60
65
70
45
recombinant protein carrying Hypocrea jecorina carbohydrate-binding module and linker
55
recombinant protein carrying Hypocrea jecorina carbohydrate-binding module and linker
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 50
about 45% activity at 30°C, about 19% activity at 50°C
50 - 65
the activity is highest at 53°C and slightly lower at 65°C, whereas the enzyme is practically inactive at 75°C
additional information
additional information
the maximal rate increases strongly with temperature, whereas the affinity for the insoluble substrate decreases, and as a result, the effect of temperature depends strongly on the substrate load. Temperature has little or no effect on the hydrolytic rate in dilute substrate suspensions, whereas strong temperature activation is observed at saturating substrate loads
additional information
the maximal rate increases strongly with temperature, whereas the affinity for the insoluble substrate decreases, and as a result, the effect of temperature depends strongly on the substrate load. Temperature has little or no effect on the hydrolytic rate in dilute substrate suspensions, whereas strong temperature activation is observed at saturating substrate loads
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.2
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene cbh1, wild-type and mutant industrial strain, full-length and mutant enzyme forms
-
-
brenda
Thermochaetoides thermophila
White Rot fungus, Cel7D is the major cellulase
Uniprot
brenda
-
-
-
brenda
an anamorph of the fungus Hypocrea jecorina, gene cel7A
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the amount of CelS in the supernatant fluids of cellobiose-grown cultures is lower than that of cellulose-grown cultures
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the glycoside hydrolase family 7, GH7
malfunction
metabolism
physiological function
additional information
malfunction
-
CelS knockout strains show reduced growth rate and cell yield on cellulose
malfunction
-
family 48 glycoside hydrolases are not necessary for growth of Clostridium thermocellum on crystalline cellulose. Creation of knockout mutants for Cel48S, the most abundant cellulosome subunit. The cellulose hydrolysis rate of the S mutant strain is 60% lower than the parent strain, with the S mutant strain also exhibiting a 40% reduction in cell yield. Although most cellulolytic bacteria have one family 48 cellulase, Clostridium thermocellum has two, Cel48S and Cel48Y. Cellulose solubilization by a Cel48S and Cel48Y double knockout is essentially the same as that of the Cel48S single knockout. Solubilization of crystalline cellulose by Clostridium thermocellum can proceed to completion without expression of a family 48 cellulase
malfunction
mutation of Trp40 at the entrance of the catalytic tunnel drastically decreases the ability to degrade crystalline cellulose. Inactive mutant enzyme does not slide on a cellulose surface
metabolism
cellulosomal enzyme systems utilize self-assembled scaffolded multimodule enzymes to deconstruct biomass, structure-function relationships governing the action of the large cellulosomal enzyme complex
metabolism
the cellobiohydrolase Cel7A is the major component of total extract produced by Trichoderma and is the key enzyme for efficient degradation of crystalline cellulose
metabolism
Trichoderma harzianum secretes an effective and well-balanced enzymatic system that is able to completely hydrolyze cellulosic substrates into monomeric glucose
metabolism
-
Trichoderma harzianum secretes an effective and well-balanced enzymatic system that is able to completely hydrolyze cellulosic substrates into monomeric glucose
-
physiological function
CelS is the exoglucanase component of the Clostridium thermocellum cellulosome multicomponent cellulase complex
physiological function
-
CelS is the major enzymatic component of the Clostridium thermocellum cellulosome
physiological function
the enzyme was a component of the cellulosome complex
physiological function
model of synergistic cooperation between endocellulase Cel9A and exocellulase Cel48a. Endocellulase Cel9A is most effective on fresh bacterial cellulose with a presumably uniform surface at the molecular level. Its processive activity likely erodes the surface and thus reduces its own activity. Cel48A is able to hydrolyze the Cel9A-modified substrate efficiently and replenish the uniform surface required by Cel9A, creating a feedback mechanism
physiological function
-
comparison of the binding isotherm to cellulose of cellobiose dehydrogenase (CDH) from Phanerochaete chrysosporium with that of cellobiohydrolase 1 (CBH 1) from Trichoderma reesei. The binding of both enzymes decreases in the presence of ethylene glycol, increases in the presence of ammonium sulfate and is unaffected by sodium chloride
physiological function
-
the enzyme was a component of the cellulosome complex
-
additional information
-
bacterial cellulose binding at low nanomolar free enzyme concentrations is exclusively active site-mediated and is consistent with Langmuir's one binding site model, strongest binding observed with non-complexed cellulases, productive binding of te enzyme to cellulose chain ends on the hydrophobic face of bacterial cellulose microfibril. With increasing free TrCel7A concentrations the isotherm gradually deviates from the Langmuirs one binding site model caused by the increasing contribution of lower affinity binding modes that includes both active site-mediated binding and non-productive binding with active site free from cellulose chain. The binding of enzyme to bacterial cellulose is only partially reversible
additional information
-
cellobiohydrolase I has a shortened loop at the entrance of the cellulose-binding tunnel, the flexibility of Tyr260 is enhanced as a result of the short side-chains of adjacent Val216 and Ala384 residues and creates an additional gap at the side face of the catalytic tunnel. A larger flexibility in this region might facilitate the entry of the substrate into the tight binding tunnel of the enzyme. Structure analysis and molecular dynamics simulations, overview
additional information
cellobiohydrolase I has a shortened loop at the entrance of the cellulose-binding tunnel, the flexibility of Tyr260 is enhanced as a result of the short side-chains of adjacent Val216 and Ala384 residues and creates an additional gap at the side face of the catalytic tunnel. A larger flexibility in this region might facilitate the entry of the substrate into the tight binding tunnel of the enzyme. Structure analysis and molecular dynamics simulations, overview
additional information
crystal structures of the two X1 modules from the enzyme CbhA
additional information
enzyme and catalytic tunnel structure, overview
additional information
tertiary structure analysis at different pH values, small-angle X-ray scattering, overview
additional information
the core domain is able to bind tightly to cellulose, even in absence of the carbohydrate-binding module. Family 1 carbohydrate-binding modules are small wedge-shaped domains with a rough and a flat face. Carbohydrate-binding module interaction with crystalline cellulose surfaces takes place through three tyrosine residues aligned on the flat face forming hydrogen bonds with the cellulose substrate
additional information
-
three-dimensional structure of the catalytic domain of TrCel7A cellobiohydrolase, Trp40 is involved in recruiting individual substrate chains into the active site tunnel to initiate processive hydrolysis, molecular dynamics simulation study, overview. The reducing end glucose unit is effectively loaded into the active site ofWTcat, but not into that of W40Acat, when the simulation is started from subsite-7
additional information
three-dimensional structure of the catalytic domain of TrCel7A cellobiohydrolase, Trp40 is involved in recruiting individual substrate chains into the active site tunnel to initiate processive hydrolysis, molecular dynamics simulation study, overview. The reducing end glucose unit is effectively loaded into the active site ofWTcat, but not into that of W40Acat, when the simulation is started from subsite-7
additional information
-
cellobiohydrolase I has a shortened loop at the entrance of the cellulose-binding tunnel, the flexibility of Tyr260 is enhanced as a result of the short side-chains of adjacent Val216 and Ala384 residues and creates an additional gap at the side face of the catalytic tunnel. A larger flexibility in this region might facilitate the entry of the substrate into the tight binding tunnel of the enzyme. Structure analysis and molecular dynamics simulations, overview
-
additional information
-
bacterial cellulose binding at low nanomolar free enzyme concentrations is exclusively active site-mediated and is consistent with Langmuir's one binding site model, strongest binding observed with non-complexed cellulases, productive binding of te enzyme to cellulose chain ends on the hydrophobic face of bacterial cellulose microfibril. With increasing free TrCel7A concentrations the isotherm gradually deviates from the Langmuirs one binding site model caused by the increasing contribution of lower affinity binding modes that includes both active site-mediated binding and non-productive binding with active site free from cellulose chain. The binding of enzyme to bacterial cellulose is only partially reversible
-
Show AA Sequence and Transmembrane Helices (155 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45000
46000
x * 75000, full-length enzyme, x * 46000, catalytic domain, SDS-PAGE
47500
50000
52000
53000
61000
native enzyme produced in Trichoderma reesei, glycosylated form (without Endo H treatment), SDS-PAGE
63000
65000
-
x * 65000, full-length enzyme form 1, SDS-PAGE, x * 52000, truncated catalytic core enzyme form 2, SDS-PAGE
66000
75000
52000
-
x * 65000, full-length enzyme form 1, SDS-PAGE, x * 52000, truncated catalytic core enzyme form 2, SDS-PAGE
52000
native enzyme produced in Trichoderma reesei, deglycosylated form (with Endo H treatment), SDS-PAGE
53000
Trichoderma reesei/Talatomyces emersonii chimeric cellobiohydrolase I containing the catalytic domain from Talaromyces emersonii and the linker and carbohydrate-binding module from Trichoderma reesei, deglycosylated form (with Endo H treatment), SDS-PAGE
53000
Trichoderma reesei/Talatomyces emersonii chimeric cellobiohydrolase I containing the catalytic domain from Talaromyces emersonii and the linker and carbohydrate-binding module from Trichoderma reesei, deglycosylated form (with Endo H treatment), SDS-PAGE
63000
Trichoderma reesei/Talatomyces emersonii chimeric cellobiohydrolase I containing the catalytic domain from Talaromyces emersonii and the linker and carbohydrate-binding module from Trichoderma reesei, glycosylated form (without Endo H treatment), SDS-PAGE
63000
Trichoderma reesei/Talatomyces emersonii chimeric cellobiohydrolase I containing the catalytic domain from Talaromyces emersonii and the linker and carbohydrate-binding module from Trichoderma reesei, glycosylated form (without Endo H treatment), SDS-PAGE
75000
x * 75000, full-length enzyme, x * 46000, catalytic domain, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
?
-
x * 74268, His12-tagged GH domain, calculated from amino acid sequence
?
Acetivibrio thermocellus DSM1313
-
x * 74268, His12-tagged GH domain, calculated from amino acid sequence
-
?
-
x * 65000, full-length enzyme form 1, SDS-PAGE, x * 52000, truncated catalytic core enzyme form 2, SDS-PAGE
?
x * 75000, full-length enzyme, x * 46000, catalytic domain, SDS-PAGE
?
x * 47500, calculated, x * 50000, SDS-PAGE, x * 65000, SDS-PAGE of recombinant protein carrying a cellulose-binding module
?
x * 80000, SDS-PAGE, recombinant protein fused to glutathione S-transferase
additional information
Thermochaetoides thermophila
mature protein CBH3 only comprises a catalytic domain and lacks cellulose-binding domain and a hinge region
additional information
-
enzyme molecular surface and structure analysis, overview
additional information
enzyme molecular surface and structure analysis, overview
additional information
-
enzyme molecular surface and structure analysis, overview
-
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
-
three-dimensional structure of the catalytic domain of TrCel7A cellobiohydrolase, overview
additional information
three-dimensional structure of the catalytic domain of TrCel7A cellobiohydrolase, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
additional information
glycoprotein
the crystal structures show attached N-glycans at two of the predicted N-glycosylation sites (Asn57 and Asn206) and also at Asn432 near the C terminus of the catalytic domain. O-glycosylation at Ser196 is indicated by electron density, on a loop where the glycan probably influences loop contacts across the active site and interactions with the cellulose surface
glycoprotein
-
the crystal structures show attached N-glycans at two of the predicted N-glycosylation sites (Asn57 and Asn206) and also at Asn432 near the C terminus of the catalytic domain. O-glycosylation at Ser196 is indicated by electron density, on a loop where the glycan probably influences loop contacts across the active site and interactions with the cellulose surface
-
glycoprotein
-
sequence shows four potential N-glycosylation sites at the catalytic module: Asn45, Asn194, Asn388, and Asn430. The N-linked glycans represent variable high-mannose oligosaccharides and the products of their sequential enzymatic trimming, according to the formula (Man)0-13(GlcNAc)2, or a single GlcNAc residue. Mutations in the glycosylation sites have no notable effect on pH-optimum of activity and enzyme thermostability but influence both the enzyme adsorption ability on Avicel and its activity against natural and synthetic substrates
glycoprotein
-
the enzyme has four potential N-glycosylation sites at its catalytic module: Asn45, Asn194, Asn388, and Asn430
glycoprotein
predicted N-glycosylation sites at N126, N283 and N397 and the O-glycosylated linker, structure, overview
glycoprotein
-
predicted N-glycosylation sites at N126, N283 and N397 and the O-glycosylated linker, structure, overview
-
glycoprotein
in the case of Trichoderma reesei/Talatomyces emersonii chimeric cellobiohydrolase I containing the catalytic domain from Talaromyces emersonii and the linker and carbohydrate-binding module from Trichoderma reesei which is expressed from Yarrowia, the overall magnitude of glycosylation is similar or only slightly higher than that for native cellobiohydrolase I produced in Trichoderma reesei
glycoprotein
-
there are four N-glycosylation sites at N270, N384, N45 and N64. N45 and N64 are N-glycosylated with high mannose type glycans. The catalytic domain of the enzyme is extensively O-glycosylated with hexoses and N-acetylhexosamines. There are several glycosylation sites (such as T383, S8, and S46) at the openings of the substrate-binding tunnel, and potentially involve in the binding of cellulose
glycoprotein
-
there are four N-glycosylation sites at N270, N384, N45 and N64. N45 and N64 are N-glycosylated with high mannose type glycans. The catalytic domain of the enzyme is extensively O-glycosylated with hexoses and N-acetylhexosamines. There are several glycosylation sites (such as T383, S8, and S46) at the openings of the substrate-binding tunnel, and potentially involve in the binding of cellulose
-
glycoprotein
-
there are four N-glycosylation sites at N270, N384, N45 and N64. N45 and N64 are N-glycosylated with high mannose type glycans. The catalytic domain of the enzyme is extensively O-glycosylated with hexoses and N-acetylhexosamines. There are several glycosylation sites (such as T383, S8, and S46) at the openings of the substrate-binding tunnel, and potentially involve in the binding of cellulose
-
proteolytic modification
the encoded preprotein consists of 535 amino acids, divided into a 17-residue signal peptide followed by a GH7 catalytic module of about 436 residues, a Ser/Thr-rich linker region of about 47 residues, and finally a C-terminal CBM1 of about 35 residues
proteolytic modification
-
the encoded preprotein consists of 535 amino acids, divided into a 17-residue signal peptide followed by a GH7 catalytic module of about 436 residues, a Ser/Thr-rich linker region of about 47 residues, and finally a C-terminal CBM1 of about 35 residues
-
additional information
-
N-terminal glutamine cyclization in the Cel7A improves the properties of the enzyme concering thermal stability and enzyme activity
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystals of truncated CelS in complex with cellobiose are obtained by ammonium sulfate precipitation, crystal structure of the catalytic domain of Clostridium thermocellum CelS in complex with oligosaccharides
Ig-GH9 CbhA: immunoglobulin-like module and the catalytic module, and Ig-GH9 CbhA-(E795Q) mutant in complex with cellotetraose
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purified recombinant enzyme, sitting drop vapor diffusion method, mixing of 0.001 ml each of 80 mg/ml protein, in 20 mM Tris, pH 7.0, with 100 mM NaCl, and 1.9 M sodium malonate, pH 6.0, or with 1.9 M sodium malonate, pH 6.5, 20% v/v ethylene glycol, 50 mM KI. In a second method, 15 mg/ml protein in 20 mM acetic acid buffer, pH 5.0, with 100 mM NaCl is mixed with 0.2 M ammonium iodide, 20% w/v PEG 3350, pH 6.2, X-ray diffraction structure determination and analysis at 1.7 A resolution, single isomorphous replacement with anomalous signal from iodine and molecular-replacement
crystal structures in complex with cellobiose, cellotetraose and triethylene glycol molecules. The product cellobiose occupies subsites +1 and +2 in the open active-site cleft of the enzyme-cellotetraose complex structure, and three triethylene glycol molecules and one pentaethylene glycol molecule are located at active-site subsites -2 to -6 in the structure of the ExgS-triethylene glycol complex. Glu50 acts as a proton donor and Asp222 plays a nucleophilic role
sitting drop vapor diffusion method, using 12.5% (w/v) polyethylene glycol 1000, 12.5% (w/v) PEG 3350, 12.5% (v/v) 2-methyl-2,4-pentanediol, 0.1 M sodium HEPES-MOPS pH 7.5, 0.03 M MgCl2, and 0.03 M CaCl2
to 2.1 A resolution. Protein natively consists of a catalytic domain and does not exhibit a carbohydrate-binding module. Strucutre is homologous to those of other GH7 CBHs with an enclosed active-site tunnel
sitting drop vapor diffusion method, using 0.1 M sodium malonate, pH 7.0 and 12% (w/v) PEG 3350
to 1.8 A resolution. Protein natively consists of a catalytic domain and does not exhibit a carbohydrate-binding module. Structure is homologous to those of other GH7 CBHs with an enclosed active-site tunnel
structures, with and without bound thio-oligosaccharides, show conformational diversity of tunnel-enclosing loops, including a form with partial tunnel collapse at subsite -4
hanging drop vapor diffusion method, apoenzyme using 20 mM MgCl2, 0.1 M HEPES, pH 7.5, 22% (w/v) polyacrylic acid 5100 sodium salt, or in complex with thio-beta-D-xylopentaose using 20mM MgCl2, 0.1 M HEPES, pH 7.7, 15-22% (w/v) polyethylene glycol 3350
apo form at 1.6 A resolution, and three ligand bound complexes ranging from 1.9 A to 1.14 A resolution. Enzyme exhibits an extended substrate-binding motif at the tunnel entrance, which may aid in substrate acquisition and processivity. Enzyme stability and activity remain unchanged, or increase at high salt concentration
vapor diffusion method, using 0.1 M CH3CO2Na pH 4.5, 15% (w/v) PEG 6000 and 0.5 M CaCl2
Cel7B free and in complex with cellobiose, cellotriose, and cellotetraose, at high resolution (1.6-2.1 A). Cel7B crystals are pseudo-merohedrally twinned and belong to space group P21, with unit cell dimensions of a=50.9 A, b=94.5 A, c=189.8 A, beta=90.0°. The loops extending from the core beta-sandwich structure form a long tunnel composed of multiple subsites for the binding of the glycosyl units of a cellulose chain
free and in complex with cellobiose, cellotriose, and cellotetraose, at 1.6-2.1 A resolution. Four molecules in the asymmetric unit, with characteristic fold of a glycoside hydrolase family 7 cellobiohydrolase. The catalytic residues at the reducing end of the tunnel are conserved, and the mechanism is expected to be retaining. Enzyme shows large variations in the amino acid side chain conformations and in the positions of glycosyl units in the different cellooligomer complexes. In each complex structure, all glycosyl residues are in the chair conformation
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 -173°C and 1.7-1.8 A resolution
sitting drop vapor diffusion method, using sodium phosphate monobasic monohydrate and 1.53 M potassium phosphate dibasic pH 4.0
3D structural modeling of the Cel7A catalytic module with N-linked glucans attached to Asn45, Asn194, and Asn388 glycosylation sites. Residue Asn45 is located near the entrance to the enzyme active site tunnel, while the two other N-glycosylation sites are located on the loops forming the tunnel, Asn194 being closer to the entrance and Asn388 being closer to the exit of the tunnel
-
mutant D224N, to 1.6 A resolution. There is one molecule in the asymmetric unit in complex with a cellobiose and a cellohexaose molecule. The active site tunnel entrance is enriched in aromatic residues. Only the aromatic residues located around the tunnel entrance appear to be important for the ability of Cel48A to access individual cellulose chains on bacterial cellulose
hanging drop vapor diffusion method, using 25% (w/v) PEG 8K and 2.5 mM CaCl2
catalytic domain, cocrystallized with the (S)-enantiomer of the beta-blocker propranolol
sitting drop vapor diffusion method, using 25.5% (w/v) PEG 4000, 0.17 M ammonium sulfate, and 15% (v/v) glycerol
structures in complex with xylotriose, xylotetraose and xylopentaose reveal a predominant binding mode at the entrance of the substrate-binding tunnel of the enzyme, in which each xylose residue is shifted about 2.4 A towards the catalytic center compared with binding of cellooligosaccharides. Partial occupancy of two consecutive xylose residues at subsites -2 and -1 suggests an alternative binding mode for xylooligosaccharides in the vicinity of the catalytic center
protein lacking the C-terminal linker-CBM1 part, yielding crystals of space group P212121 with two protein molecules, chains A and B, in the asymmetric unit, to 1.8 A resolution. The catalytic triad consisting of Glu213 (nucleophile), Asp215 and Glu218 (acid/base), and the tryptophan platforms at subsites -7, -4, -2 and +1 are highly conserved
structure of catalytic module, 1.8 A resolution. The crystal structure of the enzyme reveals considerable flexibility of the active-site-defining loop regions
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A30T
-
mutant shows improved unfolding temperature by 1.5°C compared to the wild type enzyme (64.5°C)
G184D
-
mutant has higher specific activity and shows wild type unfolding temperature (64.5°C)
G4C/M70C
G4C/M70C/S290T
S290T
A201P
-
predicted from structure fold, calculation of the thermostability of the mutant
A329G
-
predicted from structure fold, calculation of the thermostability of the mutant
A383Y
D300K
-
predicted from structure fold, calculation of the thermostability of the mutant
D354V
D52T
-
predicted from structure fold, calculation of the thermostability of the mutant
E325P
-
predicted from structure fold, calculation of the thermostability of the mutant
H208Y
H358K
-
predicted from structure fold, calculation of the thermostability of the mutant
H358R
-
predicted from structure fold, calculation of the thermostability of the mutant
H358V
-
predicted from structure fold, calculation of the thermostability of the mutant
L113M
-
predicted from structure fold, calculation of the thermostability of the mutant
N126G
-
predicted from structure fold, calculation of the thermostability of the mutant
N439G
-
predicted from structure fold, calculation of the thermostability of the mutant, the mutation results in loss of expression
N93K
P399G
-
predicted from structure fold, calculation of the thermostability of the mutant
Q345M
-
predicted from structure fold, calculation of the thermostability of the mutant
S130T
-
predicted from structure fold, calculation of the thermostability of the mutant
S13P
-
predicted from structure fold, calculation of the thermostability of the mutant
S13P/Y60L7S324P/A383Y7Y43
-
predicted from structure fold, calculation of the thermostability of the mutant, the mutant is the most thermostable variant
S222K
-
predicted from structure fold, calculation of the thermostability of the mutant
S324P
S57D
-
predicted from structure fold, calculation of the thermostability of the mutant
S5T
-
predicted from structure fold, calculation of the thermostability of the mutant
T164K
-
predicted from structure fold, calculation of the thermostability of the mutant
T257 V
-
predicted from structure fold, calculation of the thermostability of the mutant
T257I
-
predicted from structure fold, calculation of the thermostability of the mutant
T257K
-
predicted from structure fold, calculation of the thermostability of the mutant
T273K
-
predicted from structure fold, calculation of the thermostability of the mutant
T273P
-
predicted from structure fold, calculation of the thermostability of the mutant
T339P
-
predicted from structure fold, calculation of the thermostability of the mutant
T339Q
-
predicted from structure fold, calculation of the thermostability of the mutant
T392I
T395P
-
predicted from structure fold, calculation of the thermostability of the mutant, the mutation results in loss of expression
T408D
-
predicted from structure fold, calculation of the thermostability of the mutant
T41V
-
predicted from structure fold, calculation of the thermostability of the mutant
V110L
-
predicted from structure fold, calculation of the thermostability of the mutant
V217I
-
predicted from structure fold, calculation of the thermostability of the mutant
V227L
-
predicted from structure fold, calculation of the thermostability of the mutant
V331M
-
predicted from structure fold, calculation of the thermostability of the mutant
V404A
-
predicted from structure fold, calculation of the thermostability of the mutant
Y430F
Y60I
-
predicted from structure fold, calculation of the thermostability of the mutant
Y60L
N194A
N388A
N45A
F195A
mutagenesis of active site tunnel residues, moderate reduction in activity
Y213A
mutagenesis of active site tunnel residues, moderate reduction in activity
Y213A/S311A
mutagenesis of active site tunnel residues, moderate reduction in activity
Y213A/W313A
mutagenesis of active site tunnel residues, moderate reduction in activity
Y97A
mutagenesis of active site tunnel residues, moderate reduction in activity
D214N
E212Q
E217Q
E223S/A224H/L225V/T226A/D262G
G22D/N49S/A68T/P227L/S278P/T296P
the mutant shows an increase in melting temperature and a greater half-life compared with the wild type enzyme
S128C
mutant generated for single-molecule fluorescence imaging analysis, shows hydrolysis activity comparable with those of the wild-type against cellulose Ialpha and IIII and similar dependence on the enzyme concentration
S8P/G22D/T41I/N49S/A68T/S113N/P227L /D249K/S278P/T296P/N301R
the mutant shows an increase in melting temperature and a greater half-life compared with the wild type enzyme
S8P/T41I/N49S/A68T/N89D/S92T/S113N /S196T/P227L/D249K/T255P/S278P/E295K /T296P/T332Y/V403D/S411F/T462I
the mutant, which is active up to 75°C, shows a 10.4°C increase in melting temperature and a 44fold greater half-life compared with the wild type enzyme
W38A
W40A
E223S/A224H/L225V/T226A/D262G
-
mutant has a more alkaline pH optimum, mutation destabilizes the protein fold at both acidic and alkaline pH
-
W38A
-
the mutant shows an increased Km value for Avicel compared to the wild type enzyme
-
S128C
-
mutant generated for single-molecule fluorescence imaging analysis, shows hydrolysis activity comparable with those of the wild-type against cellulose Ialpha and IIII and similar dependence on the enzyme concentration
-
additional information
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 2.5°C compared to that of the wild-type. The mutant has increased activity towards microcrystalline cellulose (avicel) at 75°C
G4C/M70C
introduction of disulfide bridge, improvement of thermostability by 2.5 degrees and increased activity towards microcrystalline cellulose at 75°C
G4C/M70C/S290T
-
thermostability-increasing mutation together with disulfide bridge mutation, the unfolding temperature is increased by 4°C compared to that of the wild-type, additive effect on thermostability. The mutant has increased activity towards microcrystalline cellulose (avicel) at 75°C
G4C/M70C/S290T
improvement of thermostability by 4.0 degrees and increased activity towards microcrystalline cellulose at 75°C
S290T
-
mutant has slightly lower specific activity and shows improved unfolding temperature by 3.5°C compared to the wild type enzyme (64.5°C)
S290T
-
can hydrolyse crystalline cellulose at 70°C 2fold more effectively than the wild-type, the unfolding temperature is increased by 1.5°C compared to that of the wild-type
A383Y
-
predicted from structure fold, calculation of the thermostability of the mutant, stabilizing mutation
A383Y
-
the mutation increases stability and results in a 10°C increase in the optimal temperature for activity, to 65°C, and a 50% increase in total sugar production from crystalline cellulose compared to the wild type
D354V
-
predicted from structure fold, calculation of the thermostability of the mutant, stabilizing mutation
D354V
-
the mutation increases stability and results in a 10°C increase in the optimal temperature for activity, to 65°C, and a 50% increase in total sugar production from crystalline cellulose compared to the wild type
H208Y
-
predicted from structure fold, calculation of the thermostability of the mutant, stabilizing mutation
H208Y
-
the mutation increases stability and results in a 10°C increase in the optimal temperature for activity, to 65°C, and a 50% increase in total sugar production from crystalline cellulose compared to the wild type
N93K
-
predicted from structure fold, calculation of the thermostability of the mutant, increased thermotability compared to the wild-type enzyme
N93K
-
the mutation increases stability and results in a 10°C increase in the optimal temperature for activity, to 65°C, and a 50% increase in total sugar production from crystalline cellulose compared to the wild type
S324P
-
predicted from structure fold, calculation of the thermostability of the mutant, stabilizing mutation
S324P
-
the mutation increases stability and results in a 10°C increase in the optimal temperature for activity, to 65°C, and a 50% increase in total sugar production from crystalline cellulose compared to the wild type
T392I
-
predicted from structure fold, calculation of the thermostability of the mutant, stabilizing mutation
T392I
-
the mutation increases stability and results in a 10°C increase in the optimal temperature for activity, to 65°C, and a 50% increase in total sugar production from crystalline cellulose compared to the wild type
Y430F
-
predicted from structure fold, calculation of the thermostability of the mutant, increased thermotability compared to the wild-type enzyme
Y430F
-
the mutation increases stability and results in a 10°C increase in the optimal temperature for activity, to 65°C, and a 50% increase in total sugar production from crystalline cellulose compared to the wild type
Y60L
-
predicted from structure fold, calculation of the thermostability of the mutant, increased thermotability compared to the wild-type enzyme
Y60L
-
the mutation increases stability and results in a 10°C increase in the optimal temperature for activity, to 65°C, and a 50% increase in total sugar production from crystalline cellulose compared to the wild type
N194A
-
mutation in glycosylation site, has no notable effect on pH-optimum of activity and enzyme thermostability, leads to decrease in substrate digestion rates
N194A
-
the substrate digestion rates of the mutant are notably lower relative to the wild type enzyme
N388A
-
mutation in glycosylation site, has no notable effect on pH-optimum of activity and enzyme thermostability, leads to decrease in substrate digestion rates
N388A
-
the substrate digestion rates of the mutant are notably lower relative to the wild type enzyme
N45A
-
mutation in glycosylation site, has no notable effect on pH-optimum of activity and enzyme thermostability, but leads to a significant increase in the rate of avicel and milled aspen wood hydrolysis
N45A
-
the mutation leads to a significant increase in the rate of Avicel and milled aspen wood hydrolysis compared to the wild type enzyme
D214N
-
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
D214N
the mutant shows slightly reduced activity compared to the wild type enzyme
E212Q
-
site-directed mutagenesis, the mutant shows reduced activity and altered kinetics compared to the wild-type enzyme
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
W38A
site-directed mutagenesis, Trp38 in the middle of the active tunnel is replaced with an alanine. This mutation weakens complex formation, and the population of substrate-bound W38A is only about half of the wild-type. Nevertheless, the maximal, steady-state rate is twice as high for the variant enzyme compared to the wild-type enzyme
W38A
-
the mutant shows an increased Km value for Avicel compared to the wild type enzyme
W40A
mutation of Trp40 at the entrance of the catalytic tunnel drastically decreases the ability to degrade crystalline cellulose. Comparison of activities of the wild-type and mutant W40A enzymes (with and without the cellulose-binding domain) for various substrates, overview
W40A
the mutation causes a loss of crystalline cellulose-degrading ability. The mutant shows reduced specific activity for crystalline cellulose and diffused the cellulose chain from the entrance of the active site tunnel
W40A
-
the mutation causes a loss of crystalline cellulose-degrading ability. The mutant shows reduced specific activity for crystalline cellulose and diffused the cellulose chain from the entrance of the active site tunnel
-
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
additional information
protein natively consists of a catalytic domain and does not exhibit a carbohydrate-binding module. Upon addition of the family 1 Hypocrea jecorina Cel7A carbohydrate-binding module and linker to the C terminus of the Dictyostelium enzymes, the recombinant Cel7ACBM hydrolyzes avicel, pretreated corn stover, and phosphoric acid-swollen cellulose as efficiently as Hypocrea jecorina Cel7A when hydrolysis is compared at their temperature optima. The Ki of cellobiose is significantly higher for the Dictyostelium Cel7ACBM
additional information
protein natively consists of a catalytic domain and does not exhibit a carbohydrate-binding module. Upon addition of the family 1 Hypocrea jecorina Cel7A carbohydrate-binding module and linker to the C terminus of the Dictyostelium enzyme, the recombinant Cel7ACBM hydrolyzes avicel, pretreated corn stover, and phosphoric acid-swollen cellulose as efficiently as Hypocrea jecorina Cel7A when hydrolysis is compared at their temperature optima. The Ki of cellobiose is significantly higher for the Dictyostelium Cel7ACBM
additional information
linking of a cellulose-binding module improves the thermostability by 2.5 degrees and causes a clear increase in the hydrolysis activity towards Avicel at 70°C
additional information
-
prediction of point mutations to increase the thermostability of the enzyme, overview
additional information
addition of different types of carbohydrate-binding modules (CBM) to cellobiohydrolase Cel7A and construction of chimeric cellobiohydrolases with an additional S-S bridge in the catalytic module. All the fusion proteins are secreted in active form and in good yields by Saccharomyces cerevisiae. The purified chimeric enzymes bind to cellulose clearly better than the catalytic module alone and demonstrate high thermal stability. Fusions with CBM1 from Hypocrea jecorina Cel7A, CBM2 from Cellulomonas fimi xylanase 10A and CBM3 derived from Clostridium thermocellum cellulosomal-scaffolding protein CipA are highly active
additional information
the carbohydrate-binding module has a dual effect on the activity, it diminishes the tendency of heat-induced desorption, but also has a pronounced negative effect on the maximal rate, which was 2fold larger in variants without carbohydrate-binding module throughout the investigated temperature range. Although the carbohydrate-binding module is beneficial for affinity it slows down the catalytic process
additional information
expression of Trichoderma reesei/Talatomyces emersonii chimeric cellobiohydrolase I containing the catalytic domain from Talaromyces emersonii and the linker and carbohydrate-binding module from Trichoderma reesei in Yarrowia lipolytica
additional information
-
secretory pathway engineering, including protein folding, disulfide bond formation, and protein trafficking and sorting, enhances secretion of cellobiohydrolase I, with its native signal peptide, from Trichoderma reesei in Saccharomyces cerevisiae. Overexpression of the protein disulfide isomerase Sc-PDI1 and the plasma membrane targeting soluble N-ethylmaleimide-sensitive factor attachment protein receptor Sc-SSO1, and disruption of the sorting receptor Sc-VPS10 and a Ca2+/Mn2+ ATPase Sc-PMR1, improve respectively the extracellular Tr-Cel7A activities. The extracellular activities of the quadruple-modified strain using 4-nitrophenyl-beta-D-cellobioside and phosphoric acid swollen cellulose as the substrates, respectively, are 3.9fold and 1.3fold higher than that of the reference cel7AF strain, detailed overview
additional information
secretory pathway engineering, including protein folding, disulfide bond formation, and protein trafficking and sorting, enhances secretion of cellobiohydrolase I, with its native signal peptide, from Trichoderma reesei in Saccharomyces cerevisiae. Overexpression of the protein disulfide isomerase Sc-PDI1 and the plasma membrane targeting soluble N-ethylmaleimide-sensitive factor attachment protein receptor Sc-SSO1, and disruption of the sorting receptor Sc-VPS10 and a Ca2+/Mn2+ ATPase Sc-PMR1, improve respectively the extracellular Tr-Cel7A activities. The extracellular activities of the quadruple-modified strain using 4-nitrophenyl-beta-D-cellobioside and phosphoric acid swollen cellulose as the substrates, respectively, are 3.9fold and 1.3fold higher than that of the reference cel7AF strain, detailed overview
additional information
the carbohydrate-binding module has a dual effect on the activity, it diminishes the tendency of heat-induced desorption, but also has a pronounced negative effect on the maximal rate, which was 2fold larger in variants without carbohydrate-binding module throughout the investigated temperature range. Although the carbohydrate-binding module is beneficial for affinity it slows down the catalytic process
additional information
expression of Trichoderma reesei/Talatomyces emersonii chimeric cellobiohydrolase I containing the catalytic domain from Talaromyces emersonii and the linker and carbohydrate-binding module from Trichoderma reesei in Yarrowia lipolytica
additional information
-
the carbohydrate-binding module has a dual effect on the activity, it diminishes the tendency of heat-induced desorption, but also has a pronounced negative effect on the maximal rate, which was 2fold larger in variants without carbohydrate-binding module throughout the investigated temperature range. Although the carbohydrate-binding module is beneficial for affinity it slows down the catalytic process
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 7
enzyme is stable at pH 3-7 at 37°C, but loses 90% of activity at pH 2 after 20 min
654486
3.5 - 5.6
-
optimal stability, gradual decrease in stability at more alkaline pH values
655473
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
50 - 60
-
unstable at temperatures lower than 50°C, retains about 80% of its activity after a 30 min incubation at 50°C and is completely inactivated after a 30 min pre-incubation at or above 60°C
50 - 65
-
the enzyme is stable at 50°C at least for 3 h. At 60 and 65°C, the enzyme half-life times are in the range of 40-43 min and 11-13 min, respectively
50 - 70
the enzyme has a half-life of 60 min at 70°C and after incubation for 72 h retains more than 80% of enzymatic activity at 60°C and 100% at 50°C, respectively
53
55 - 70
thermal unfolding behavior of Th Cel7A is found to be a two-step process at pH 5.0. The first step leads to the formation of molten globule-like states between 55°C and 65°C, followed by a second step that was due to the unfolding of the molten globule-like state at temperatures above 70°C
60
62 - 69
the melting temperature is 62.5°C. The wild type enzyme shows half-lives of 19.9, 9.3 and 8.6 min at 62°C, 66°C, and 69°C, respectively
64.2 - 74.7
-
melting tempeartures, recombinant expression in Saccharomyces cerevisiae and in Neurospora crassa. The Cel7A expressed in Neurospora crassa has a by 10°C higher melting temperature and higher specific activity than the Cel7A expressed in Saccharomyces cerevisiae
65
70
70.5
melting temperature, mutant carrying a cellulose-binding module
72
melting temperature, fusion protein with CBM2 from Cellulomonas fimi xylanase 10A
72.5
74
melting temperature, fusion protein with CBM1 from Hypocrea jecorina Cel7A
75
melting temperature, fusion protein with CBM3 derived from Clostridium thermocellum cellulosomal-scaffolding protein CipA
75.5
melting temperature, fusion protein with CBM1 from Hypocrea jecorina Cel7A containing an additional S-S bridge in the catalytic module
77
melting temperature, fusion protein with CBM3 derived from Clostridium thermocellum cellulosomal-scaffolding protein CipA containing an additional S-S bridge in the catalytic module
80
additional information
50
enzyme retains full activity between pH 4 and 6, but is rapidly inactivated at lower pH values
53
melting temperature, recombinant protein carrying Hypocrea jecorina carbohydrate-binding module and linker
53
melting temperature, recombinant protein carrying Hypocrea jecorina carbohydrate-binding module and linker
additional information
-
the full-length enzyme form is more thermostable than the truncated mutant enzyme form
additional information
-
the Trichoderma reesei produced fusion protein Cel7B-CBM has 2.5°C improved unfolding temperature when compared to the Trichoderma reesei produced catalytic module (Cel7B wild-type)
additional information
cellobiose-binding influences the enzyme's thermal stability
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation and phenyl Sepharose resin column chromatography
ammonium sulfate precipitation and Source 15Phe column chromatography
ammonium sulfate precipitation, phenyl Sepharose 6 column chromatography Source 15Q resin column chromatography, and Superdex 75 gel filtration
-
ammonium sulfate precipitation, phenyl Sepharose column chromatography, Source 15Q column chromatography, and Superdex 75 gel filtration
ammonium sulfate precipitation, Source 15Q column chromatography, and Source 15 isopropyl column chromatography
-
Bio-Gel P-6 gel filtration, DEAE-Sepharose column chromatography and phenyl Sepharose column chromatography
HiTrap phenyl column chromatography and Superdex 200 gel filtration
homogeneity
Ni2+ affinity column chromatography
Ni2+ Sepharose column chromatography and Superdex S200 gel filtration
-
on affinity column and by gel filtration
phenyl Sepharose column chromatography, Source 15Q column chromatography, and Sephadex G-25 gel filtration
-
Q Sepharose column chromatography and DEAE-Sephadex gel filtration
Q-Sepharose Fast-Flow column chromatography and Mono Q column chromatography
-
recombinant -type and mutant W40A enzymes from Trichoderma reesei strain ALKO 3413 culture filtrate by gel filtration, anion exchange, hydrophobic interaction, and affinity chromatography
recombinant C-terminally His6-tagged enzyme from Saccharomyces cerevisiae by anion exchange chromaatography and dialysis, recombinant enzyme from Neurospora crassa by ammonium sulfate fractionation, gel filtration, anion exchange chromatography and dialysis
-
recombinant His6-tagged enzyme from Escherichia coli (BL21) by cation exchange and hydrophobic interaction chromatography, followed by another step of cation exchange and anion exchange chromatography and gel filtration
the enzyme and catalytic domain alone are each expressed in and purified from Streptomyces lividans
wild-type and mutants purified with one-step purification using gel filtration
-
ammonium sulfate precipitation and Source 15Phe column chromatography
ammonium sulfate precipitation, phenyl Sepharose column chromatography, Source 15Q column chromatography, and Superdex 75 gel filtration
ammonium sulfate precipitation, phenyl Sepharose column chromatography, Source 15Q column chromatography, and Superdex 75 gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as an endoglucanase-cellobiohydrolase fusion protein in Saccharomyces cerevisiae, Yarrowia lipolytica, and Lipomyces starkeyi
-
expressed in Aspergillus oryzae
expressed in Saccharomyces cerevisiae
expressed in Saccharomyces cerevisiae strain YDR483W
expressed in Trichoderma reesei
expression in Escherichia coli
expression in Pichia pastoris
folding and/or post-translation modification of heterologous enzyme in Yarrowia lipolytica cannot completely mimic that in the original source strain. Trichoderma reesei/Talatomyces emersonii chimeric cellobiohydrolase I containing the catalytic domain from Talaromyces emersonii and the linker and carbohydrate-binding module from Trichoderma reesei
gene cel7A, heterologous expression of wild-type and mutant enzymes in Aspergillus oryzae
gene cel7A, recombinant expression of wild-type and mutant W40A enzymes under the control of its own promoter in Trichoderma reesei strain ALKO 3413 lacking the genes encoding for endogenous Cel7A and Cel7B
gene cel7AF, recombinant expression of extracellular C-terminally FLAG-tagged enzyme with its native signal peptide in Saccharomyces cerevisiae strain CEN.PK102-3, the enzyme is secreted to the culture medium
recombinant expression of C-terminally His6-tagged enzyme in Saccharomyces cerevisiae, and expression in Neurospora crassa using an Neurospora crassa codon bias and Neurospora crassa CBHI signal peptide and cloned in pCSR1:GPD vector, which directs gene integration to the csr-1 locus. Gene expression is promoted by the constitutive Myceliophthora thermophila gpdA promoter. The Cel7A expressed in Neurospora crassa has a higher melting temperature and higher specific activity than the Cel7A expressed in Saccharomyces cerevisiae. The underlying cause of this disparity is the lack of N-terminal glutamine cyclization in the Cel7A expressed in Saccharomyces cerevisiae. Treating the enzyme in vitro with glutaminyl cyclase improves the properties of Cel7A expressed in Saccharomyces cerevisiae to match those of Cel7A expressed in Neurospora crassa
-
recombinant expression of His6-tagged enzyme in Escherichia coli (BL21)
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
-
wild-type Cel7A expressed in Trichoderma reesei
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
folding and/or post-translation modification of heterologous enzyme in Yarrowia lipolytica cannot completely mimic that in the original source strain. Trichoderma reesei/Talatomyces emersonii chimeric cellobiohydrolase I containing the catalytic domain from Talaromyces emersonii and the linker and carbohydrate-binding module from Trichoderma reesei
folding and/or post-translation modification of heterologous enzyme in Yarrowia lipolytica cannot completely mimic that in the original source strain. Trichoderma reesei/Talatomyces emersonii chimeric cellobiohydrolase I containing the catalytic domain from Talaromyces emersonii and the linker and carbohydrate-binding module from Trichoderma reesei
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
celS appears to be regulated at the transcriptional level, and its expression is modulated by growth rate both under conditions of cellobiose and nitrogen limitation. The amount of celS mRNA transcripts per cell is about 180 for cells grown under carbon limitation at growth rates of 0.04 to 0.21 per h and 80 and 30 transcripts per cell for batch cultures at growth rates of 0.23 and 0.35 per hour, respectively. Under nitrogen limitation, the corresponding levels were 110, 40, and 30 transcripts/cell for growth rates of 0.07, 0.11, and 0.14 per hour, respectively. Two major transcriptional start sites are detected at positions 140 and 145 bp, upstream of the translational start site of the celS gene. The relative activity of the two promoters remains constant under the conditions studied and is in agreement with the results of the RNase protection assay, in which the observed transcriptional activity is inversely proportional to the growth rate
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
biofuel production
biotechnology
degradation
paper production
synthesis
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
analysis
development of an optical tweezers-based single-molecule motility assay for precision tracking of Cel7A. Direct observation of motility during degradation reveals processive runs and distinct steps on the scale of 1 nm. Cel7A is not mechanically limited, can work against 20 pN loads and speeds up when assisted. The fundamental stepping cycle likely includes energy from glycosidic bonds and other sources. The catalytic domain alone is sufficient for processive motion
analysis
-
polymerization-based assay for determining the potency of cellulolytic enzyme formulations on pretreated biomass substrates by monitoring the autofluorescence of cellulose. The one-pot method is label-free, rapid, highly sensitive, and requires only a single pipetting step. Using model enzyme formulations derived from Trichoderma reesei, Trichoderma longibrachiatum, Talaromyces emersonii and recombinant bacterial minicellulosomes from Clostridium thermocellum, enzyme performance based on differences in thermostability, cellulose-binding domain targeting, and endo/exoglucanase synergy can be differentiated
analysis
-
development of an optical tweezers-based single-molecule motility assay for precision tracking of Cel7A. Direct observation of motility during degradation reveals processive runs and distinct steps on the scale of 1 nm. Cel7A is not mechanically limited, can work against 20 pN loads and speeds up when assisted. The fundamental stepping cycle likely includes energy from glycosidic bonds and other sources. The catalytic domain alone is sufficient for processive motion
-
biofuel production
successful expression of a chimeric cellobiohydrolase I with essentially full native activity in Yarrowia lipolytica. Yarrowia lipolytica strains can be genetically engineered, ultimately by heterologous expression of fungal cellulases and other enzymes, to directly convert lignocellulosic substrates to biofuels
biofuel production
successful expression of a chimeric cellobiohydrolase I with essentially full native activity in Yarrowia lipolytica. Yarrowia lipolytica strains can be genetically engineered, ultimately by heterologous expression of fungal cellulases and other enzymes, to directly convert lignocellulosic substrates to biofuels
biotechnology
recombination of the catalytic domains of three glycoside hydrolase family 48 bacterial cellulases (Cel48), i.e. Clostridium cellulolyticum CelF, Clostridium stercorarium CelY, and Clostridium thermocellum CelS, to create a diverse library of Cel48 enzymes with an average of 106 mutations from the closest native enzyme. The library is based on the Clostridium thermocellum CelS architecture, which consists of a 70-kDa catalytic domain connected to the organism's respective dockerin domain. Large variations in properties such as the functional temperature range, stability, and specific activity on crystalline cellulose are found. Functional status and stability are predictable from simple linear models of the sequence-property data. Recombined protein fragments contribute additively to these properties in a given chimera
biotechnology
recombination of the catalytic domains of three glycoside hydrolase family 48 bacterial cellulases (Cel48), i.e. Clostridium cellulolyticum CelF, Clostridium stercorarium CelY, and Clostridium thermocellum CelS, to create a diverse library of Cel48 enzymes with an average of 106 mutations from the closest native enzyme. The library is based on the Clostridium thermocellum CelS architecture, which consists of a 70-kDa catalytic domain connected to the organism's respective dockerin domain. Two of the most stabilizing blocks are predicted to be from the parent CelS at blocks located in the C-terminus of the catalytic domain, close to where the dockerin attaches. Two of the highly stable chimeras also hydrolyze more cellulose than the most active parental enzyme
biotechnology
Acetivibrio thermocellus DSM 1237
-
recombination of the catalytic domains of three glycoside hydrolase family 48 bacterial cellulases (Cel48), i.e. Clostridium cellulolyticum CelF, Clostridium stercorarium CelY, and Clostridium thermocellum CelS, to create a diverse library of Cel48 enzymes with an average of 106 mutations from the closest native enzyme. The library is based on the Clostridium thermocellum CelS architecture, which consists of a 70-kDa catalytic domain connected to the organism's respective dockerin domain. Two of the most stabilizing blocks are predicted to be from the parent CelS at blocks located in the C-terminus of the catalytic domain, close to where the dockerin attaches. Two of the highly stable chimeras also hydrolyze more cellulose than the most active parental enzyme
-
biotechnology
-
recombination of the catalytic domains of three glycoside hydrolase family 48 bacterial cellulases (Cel48), i.e. Clostridium cellulolyticum CelF, Clostridium stercorarium CelY, and Clostridium thermocellum CelS, to create a diverse library of Cel48 enzymes with an average of 106 mutations from the closest native enzyme. The library is based on the Clostridium thermocellum CelS architecture, which consists of a 70-kDa catalytic domain connected to the organism's respective dockerin domain. Large variations in properties such as the functional temperature range, stability, and specific activity on crystalline cellulose are found. Functional status and stability are predictable from simple linear models of the sequence-property data. Recombined protein fragments contribute additively to these properties in a given chimera
-
degradation
commercial cellulases contain mannan hydrolysing enzymes. Addition of 10 mg/ml mannan reduces the glucose yield of avicel (at 20 g/l) from 40.1 to 24.3%. The inhibitory effect is at least partly attributed to the inhibition of Cel7A(CBHI), but not on beta-glucosidase
degradation
comparison of the activity w ith Humicola jecorina Cel7A reveals a much higher hydrolytic rate for Humicola grisea Cel7A at both 65°C (4.8fold higher initial rate) and 38°C (3.3fold higher)
degradation
-
construction of a consolidated bioprocessing-enabling yeast by constitutive expression of genes Cbh1 from Aspergillus aculeatus, Cbh1 and Cbh2 from Hypocrea jecorina. Additionally, Hypocrea jecorina Eg2, Aspergillus aculeatus Bgl1 are integrated into the Saccharomyces cerevisiae chromosome. The resultant strains expressing uni-, bi-, and trifunctional cellulases, respectively, exhibit corresponding cellulase activities and both the activities and glucose producing activity ascends. Evaluation in acid- and alkali-pretreated corncob containing media with 5 FPU exogenous cellulase/g biomass loading shows that compared with the control strains, the engineered strains efficiently ferment pretreated corncob to ethanol
degradation
construction of a consolidated bioprocessing-enabling yeast by constitutive expression of genes Cbh1 from Aspergillus aculeatus, Cbh1 and Cbh2 from Hypocrea jecorina. Additionally, Hypocrea jecorina Eg2, Aspergillus aculeatus Bgl1 are integrated into the Saccharomyces cerevisiae chromosome. The resultant strains expressing uni-, bi-, and trifunctional cellulases, respectively, exhibit corresponding cellulase activities and both the activities and glucose producing activity ascends. Evaluation in acid- and alkali-pretreated corncob containing media with 5 FPU exogenous cellulase/g biomass loading shows that compared with the control strains, the engineered strains efficiently ferment pretreated corncob to ethanol
degradation
development of optimal enzyme mixtures of six Trichoderma reesei enzymes and five thermostable enzyme for the hydrolysis of hydrothermally pretreated wheat straw, alkaline oxidised sugar cane bagasse and steam-exploded bagasse by statistically designed experiments. The composition of optimal enzyme mixtures depends clearly on the substrate and on the enzyme system studied. The optimal enzyme mixture of thermostable enzymes is dominated by Cel7A and requires a relatively high amount of xylanase, whereas with Hypocrea jecorina enzymes, the high proportion of Cel7B appears to provide the required xylanase activity
degradation
enzyme works synergistically with the commercial enzyme cocktail Cellic R CTec2 to enhance saccharification by 39% when added to a reaction mixture containing 0.25% alkaline pretreated oil palm empty fruit bunch
degradation
-
a fungal consortium of Aspergillus nidulans, Mycothermus thermophilus, and Humicola sp. composts a mixture (1:1) of silica rich paddy straw and lignin rich soybean trash during summer period in North India, results in a product with C:N ratio 9.5:1, available phosphorus 0.042% and fungal biomass 6.512 mg of N-acetyl glucosamine/100 mg of compost. A C:N ratio of 10.2:1 and highest humus content of 3.3% is achieved with 1:1 mixture of paddy straw and soybean trash. The consortium shows showed high cellobiase, carboxymethyl cellulase, xylanase, and FPase activities
degradation
-
a fungal consortium of Aspergillus nidulans, Mycothermus thermophilus, and Humicola sp. composts a mixture (1:1) of silica rich paddy straw and lignin rich soybean trash during summer period in North India, results in a product with C:N ratio 9.5:1, available phosphorus 0.042% and fungal biomass 6.512 mg of N-acetyl glucosamine/100 mg of compost. A C:N ratio of 10.2:1 and highest humus content of 3.3% is achieved with 1:1 mixture of paddy straw and soybean trash. The consortium shows showed high cellobiase, carboxymethyl cellulase, xylanase, and FPase activities
degradation
-
a fungal consortium of Aspergillus nidulans, Mycothermus thermophilus, and Humicola sp. composts a mixture (1:1) of silica rich paddy straw and lignin rich soybean trash during summer period in North India, results in a product with C:N ratio 9.5:1, available phosphorus 0.042% and fungal biomass 6.512 mg of N-acetyl glucosamine/100 mg of compost. A C:N ratio of 10.2:1 and highest humus content of 3.3% is achieved with 1:1 mixture of paddy straw and soybean trash. The consortium shows showed high cellobiase, carboxymethyl cellulase, xylanase, and FPase activities
degradation
-
enzyme works synergistically with the commercial enzyme cocktail Cellic R CTec2 to enhance saccharification by 39% when added to a reaction mixture containing 0.25% alkaline pretreated oil palm empty fruit bunch
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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
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
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synthesis
heterologous expression in Bacillus subtilis combined with customized signal peptides for secretion from a random libraries with 173 different signal peptides originating from the Bacillus subtilis genome. The customized signal peptide does not affect enzyme performance when assayed on carboxymethyl cellulose, phosphoric acid swollen cellulose, and microcrystalline cellulose
synthesis
recombinant enzyme expressed in Zea mays is glycosylated and 6 kDa smaller than the native fungal protein. The cellobiohydrolase performs as well as or better than its fungal counterpart in releasing sugars from complex substrates such as pretreated corn stover or wood
synthesis
Acetivibrio thermocellus DSM 1237
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heterologous expression in Bacillus subtilis combined with customized signal peptides for secretion from a random libraries with 173 different signal peptides originating from the Bacillus subtilis genome. The customized signal peptide does not affect enzyme performance when assayed on carboxymethyl cellulose, phosphoric acid swollen cellulose, and microcrystalline cellulose
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Release 2023.1 (January 2023)
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