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2,4-dinitrophenyl cellobiose + H2O
2,4-dinitrophenol + cellobiose
-
-
-
-
?
2-chloro-4-nitrophenyl-beta-D-cellotrioside + H2O
2-chloro-4-nitrophenol + ?
-
-
-
-
?
2-chloronitrophenyl-beta-D-lactoside + H2O
?
-
-
-
-
?
4-methylumbelliferyl beta-cellobioside + H2O
4-methylumbelliferol + cellobiose
-
substrate binding analysis of wild-type enzyme and mutant D274A, mutant D274A binds 4-methylumbelliferyl beta-cellobioside to approximately the same extent as the wild-type, overview
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
4-methylumbelliferol + 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-methylumbelliferyl beta-D-lactopyranoside + H2O
4-methylumbelliferone + lactose
4-methylumbelliferyl beta-D-lactoside + H2O
4-methylumbelliferol + beta-D-lactose
-
-
-
?
4-methylumbelliferyl-beta-D-cellobioside + H2O
4-methylumbelliferol + cellobiose
-
-
-
-
?
4-methylumbelliferyl-beta-D-cellobioside + H2O
?
-
-
-
-
?
4-methylumbelliferyl-beta-D-cellohexaoside + H2O
?
-
-
-
-
?
4-methylumbelliferyl-beta-D-cellopentaoside + H2O
?
-
-
-
-
?
4-methylumbelliferyl-beta-D-cellotetraoside + H2O
?
-
-
-
-
?
4-methylumbelliferyl-beta-D-cellotrioside + H2O
?
-
-
-
-
?
4-methylumbelliferyl-beta-D-oligoglucosides + H2O
?
-
enzyme preferentially cleaves the second or the fourth glycosidic bond, cleaves the second bond between putative sub-sites -2 and -1 or +1 and +2, cleaves the fourth bond between putative sub-sites -1 and +1
-
-
?
4-nitrophenyl beta-cellobioside + H2O
4-nitrophenol + beta-cellobiose
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + beta-D-cellobiose
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + D-cellobiose
-
-
-
?
4-nitrophenyl beta-D-galactopyranoside + H2O
4-nitrophenol + D-galactopyranose
-
0.26% activity compared to 4-nitrophenyl beta-D-cellobioside
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
4-nitrophenyl beta-D-lactopyranoside + H2O
4-nitrophenol + beta-D-lactopyranose
4-nitrophenyl beta-D-lactoside + H2O
4-nitrophenol + lactose
4-nitrophenyl beta-D-mannopyranoside + H2O
4-nitrophenol + D-mannopyranose
-
0.64% activity compared to 4-nitrophenyl beta-D-cellobioside
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + D-xylopyranose
-
0.64% activity compared to 4-nitrophenyl beta-D-cellobioside
-
-
?
4-nitrophenyl beta-lactoside + H2O
4-nitrophenol + ?
-
-
-
?
4-nitrophenyl beta-lactoside + H2O
4-nitrophenol + beta-lactose
-
-
-
?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
4-nitrophenyl cellopentaoside + H2O
4-nitrophenol + cellobiose + D-glucose
-
-
-
?
4-nitrophenyl cellopentaoside + H2O
cellobiose + 4-nitrophenyl cellotrioside
-
-
-
?
4-nitrophenyl cellotetraoside + H2O
cellobiose + 4-nitrophenyl cellobioside
4-nitrophenyl cellotrioside + H2O
4-nitrophenol + cellobiose + D-glucose
-
-
-
?
4-nitrophenyl lactoside + H2O
4-nitrophenol + lactose
-
-
-
?
4-nitrophenyl-beta-D-lactoside
4-nitrophenol + lactose
-
-
-
-
?
acid-swollen avicel + H2O
cellobiose + cellotriose
alpha-cellobiosyl fluoride + H2O
fluoride + cellobiose
avicel + H2O
cellobiose + ?
avicel + H2O
D-glucose + ?
microcrystalline cellulose, Avicel PH-101, at 2%
-
-
?
Avicel PH101 + H2O
cellobiose + ?
-
-
-
-
?
barley beta-glucan + H2O
?
barley straw + H2O
?
-
-
-
-
?
beta-cellobiosyl fluoride + H2O
fluoride + cellobiose
beta-glucan + H2O
cellobiose
low activity
-
-
?
carboxymethyl cellulose + H2O
?
carboxymethyl cellulose + H2O
cellobiose
97% activity compared to Avicel
-
-
?
carboxymethyl cellulose + H2O
cellobiose + ?
carboxymethylcellulose + H2O
?
-
0.26% activity compared to 4-nitrophenyl beta-D-cellobioside
-
-
?
carboxymethylcellulose + H2O
cellobiose + ?
carboxymethylcellulose + H2O
glucose + cellobiose + cellutetraose
cello-oligosaccharides + H2O
?
-
natural and derivatized cello-oligosaccharides, H3PO4-swollen cellulose, Avicel, laminarin, lichenan, barley glucan
-
-
?
cellobiose + H2O
?
-
0.11% activity compared to 4-nitrophenyl beta-D-cellobioside
-
-
?
cellodextrins + H2O
cellobiose + D-glucose + cellotriose
-
-
-
?
cellohexaose + 3 H2O
3 cellobiose
cellohexaose + H2O
?
-
-
-
?
cellohexaose + H2O
cellobiose + cellotetraose
-
-
-
-
?
cellohexaose + H2O
cellobiose + cellotetraose + cellotriose
-
-
-
?
cellohexaose + H2O
cellobiose + cellotriose + cellotetraose
cellohexaose + H2O
cellotriose + cellobiose + cellotetraose
celloligosaccharides + H2O
cellobiose + H2O
-
-
-
?
cellooligosaccharide + H2O
cellobiose
-
degree of polymerization is 25
-
-
?
cellopentaose + H2O
?
-
-
-
?
cellopentaose + H2O
cellobiose + ?
cellopentaose + H2O
cellobiose + cellotriose
cellopentaose + H2O
cellobiose + D-glucose
-
-
-
?
cellopentaose + H2O
cellobiose + D-glucose + cellotriose
cellopentaose + H2O
cellotriose + cellobiose
cellotetraose + H2O
2 cellobiose
cellotetraose + H2O
?
-
-
-
?
cellotetraose + H2O
cellobiose + ?
cellotetraose + H2O
cellobiose + D-glucose + cellotriose
cellotriitol + H2O
cellobiose + sorbitol
-
-
-
?
cellotriose + H2O
?
-
-
-
?
cellotriose + H2O
cellobiose + D-glucose
cellotriose + H2O
cellobiose + glucose
cellotriose + H2O
glucose + cellobiose
-
-
-
?
Celluclast-treated Avicel + H2O
cellobiose + ?
-
the recombinant enzyme is inactive with Avicel, but can digest Celluclast-treated Avicel producing cellobiose
-
-
?
cellulose + H2O
beta-cellobiose + ?
cellulose + H2O
cellobiose + ?
cellulose + H2O
cellobiose + cellohexaose
hydrolyzes Avicel and filter paper, efficiency of hydrolysis increases in the following order: Gh9, Gh9-Fn31,2, Gh9-Fn31,2-CBDIII
-
-
?
cellulose + H2O
cellobiose + D-glucose + cellotriose
cellulose nanowhisker + H2O
cellobiose + ?
-
crystalline portion of cellulose
-
-
?
chito-oligosaccharide + H2O
?
chitosan + H2O
N-acetyl-D-glucosamine + ?
corn stover + H2O
cellobiose + ?
-
-
-
?
crystalline cellulose + H2O
?
-
-
-
-
?
melibiose + H2O
?
about 4% activity compared to Avicel
-
-
?
methylumbelliferyl-lactoside + H2O
methylumberlliferone + lactose
-
-
-
-
?
microcrystalline cellulose + H2O
?
-
-
-
?
oat spelt xylan + H2O
?
about 2% activity compared to Avicel
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + beta-D-cellobiose
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
p-nitrophenyl-lactoside + H2O
p-nitrophenol + lactose
phosphoric acid swollen cellulose + H2O
?
phosphoric acid swollen cellulose + H2O
cellobiose + ?
phosphoric acid swollen cellulose + H2O
cellobiose + cellotriose + ?
phosphoric acid-swollen Avicel + H2O
cellobiose
-
low specific activity
-
-
?
phosphoric acid-swollen cellulose + H2O
cellobiose + ?
Thermochaetoides thermophila
-
-
-
-
?
pretreated corn-stover + H2O
?
-
-
-
?
pretreated rice straw + H2O
?
-
-
-
?
regenerated amorphous cellulose + H2O
?
-
On amorphous cellulose, the enzyme is able to initiate hydrolysis on about 4% of the sites to which it could adsorb
-
-
?
sodium hydroxide pretreated corn stover + H2O
?
sulforhodamine-conjugated cellohexaose + H2O
cellotetraose + cellotriose
-
-
-
-
?
xylan + H2O
xylobiose + xylotetraose + xylohexaose
additional information
?
-
4-methylumbelliferyl beta-D-cellobioside + H2O
4-methylumbelliferone + cellobiose
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
4-methylumbelliferone + cellobiose
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
4-methylumbelliferone + cellobiose
-
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
4-methylumbelliferone + cellobiose
Thermochaetoides thermophila
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
4-methylumbelliferone + cellobiose
-
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
4-methylumbelliferone + cellobiose
-
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
?
-
-
-
-
?
4-methylumbelliferyl beta-D-cellobioside + H2O
?
-
-
-
-
?
4-methylumbelliferyl beta-D-lactopyranoside + H2O
4-methylumbelliferone + lactose
-
-
-
?
4-methylumbelliferyl beta-D-lactopyranoside + H2O
4-methylumbelliferone + lactose
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + beta-D-cellobiose
substrate of wild-type enzyme and recombinant Cex-RsaA fusion mutant
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + beta-D-cellobiose
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + beta-D-cellobiose
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + beta-D-cellobiose
-
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + beta-D-cellobiose
-
-
-
-
?
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
-
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
-
100% activity, highly preferred substrate
-
-
?
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
-
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
-
best substrate
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
-
best substrate
-
-
?
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
-
-
-
-
?
4-nitrophenyl beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
0.11% activity compared to 4-nitrophenyl beta-D-cellobioside
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
0.11% activity compared to 4-nitrophenyl beta-D-cellobioside
-
-
?
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-lactopyranose
-
-
-
-
?
4-nitrophenyl beta-D-lactoside + H2O
4-nitrophenol + lactose
-
42.1% activity compared to 4-nitrophenyl beta-D-cellobioside
-
-
?
4-nitrophenyl beta-D-lactoside + H2O
4-nitrophenol + lactose
-
-
-
-
?
4-nitrophenyl beta-D-lactoside + H2O
4-nitrophenol + lactose
-
-
-
-
?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
?
4-nitrophenyl cellobioside + H2O
4-nitrophenol + cellobiose
-
-
-
?
4-nitrophenyl cellotetraoside + H2O
cellobiose + 4-nitrophenyl cellobioside
-
-
-
?
4-nitrophenyl cellotetraoside + H2O
cellobiose + 4-nitrophenyl cellobioside
-
-
-
?
acid-swollen avicel + H2O
cellobiose + cellotriose
-
-
-
-
?
acid-swollen avicel + H2O
cellobiose + cellotriose
-
-
-
-
?
agarose + H2O
?
low activity
-
-
?
agarose + H2O
?
about 40% activity compared to Avicel
-
-
?
alpha-cellobiosyl fluoride + H2O
fluoride + cellobiose
-
-
-
-
?
alpha-cellobiosyl fluoride + H2O
fluoride + cellobiose
-
-
-
-
?
avicel + H2O
?
-
-
-
?
avicel + H2O
?
-
26.9% activity compared to 4-nitrophenyl beta-D-cellobioside
-
-
?
avicel + H2O
?
microcrystalline cellulose
-
-
?
avicel + H2O
?
-
shows a synergistic effect in the degradation of avicel when the enzyme acts together with either cellobiohydrolase I (Ex-1) or endoglucanase (En-1) produced by Irpex lacteus MC-2
-
-
?
avicel + H2O
?
-
shows a synergistic effect in the degradation of avicel when the enzyme acts together with either cellobiohydrolase I (Ex-1) or endoglucanase (En-1) produced by Irpex lacteus MC-2
-
-
?
avicel + H2O
?
-
microcrystalline cellulose
-
-
?
avicel + H2O
?
microcrystalline cellulose
-
-
?
avicel + H2O
?
microcrystalline cellulose
-
-
?
avicel + H2O
?
-
cellobiohydrolase I when acting on Avicel, is not perfectly processive, the cellulose chain is released from the active site after 5-10 cellobiose units have been cleaved off. Adsorption of endoglucanase II and cellobiohydrolase I iss mutually negatively affected by the presence of the other enzyme. This can be the result of (i) depletion (hydrolysis) of common binding sites or (ii) competition for (occupation of) common adsorption sites. Importance of competition is shown by the concentration dependence of the observed decrease in adsorption. Cellobiohydrolase I is competing more efficiently for the binding sites than endoglucanase II. Adsorption results indicate that, besides common adsorption sites (for which endoglucanase II and cellobiohydrolase I compete), the enzymes have specific sites as well
-
-
?
avicel + H2O
cellobiose
-
-
-
-
?
avicel + H2O
cellobiose
-
-
-
-
?
avicel + H2O
cellobiose
-
-
-
-
?
avicel + H2O
cellobiose
-
-
-
?
avicel + H2O
cellobiose
-
-
-
?
avicel + H2O
cellobiose
-
-
-
-
?
avicel + H2O
cellobiose
-
-
plus traces of cellotriose
?
avicel + H2O
cellobiose
-
low specific activity
-
-
?
avicel + H2O
cellobiose
-
low specific activity
-
-
?
avicel + H2O
cellobiose
-
-
-
?
avicel + H2O
cellobiose
-
191% activity compared to cellulose
-
-
?
avicel + H2O
cellobiose
highest activity
-
-
?
avicel + H2O
cellobiose
high activity
-
-
?
avicel + H2O
cellobiose
-
-
-
-
?
avicel + H2O
cellobiose
-
-
-
?
avicel + H2O
cellobiose + ?
-
-
-
?
avicel + H2O
cellobiose + ?
-
-
-
?
avicel + H2O
cellobiose + ?
-
-
-
?
avicel + H2O
cellobiose + ?
-
-
-
-
?
avicel + H2O
cellobiose + ?
-
-
-
-
?
avicel + H2O
cellobiose + ?
-
-
-
-
?
avicel + H2O
cellobiose + ?
-
-
-
-
?
avicel + H2O
cellobiose + ?
Thermochaetoides thermophila
-
-
-
-
?
avicel + H2O
cellobiose + ?
-
-
-
?
avicel + H2O
cellobiose + ?
-
-
-
-
?
Avicel PH-101 + H2O
?
-
-
-
?
Avicel PH-101 + H2O
?
-
-
-
?
barley beta-glucan + H2O
?
-
highest specific activity
-
-
?
barley beta-glucan + H2O
?
-
highest specific activity
-
-
?
barley beta-glucan + H2O
?
-
-
-
-
?
barley beta-glucan + H2O
?
-
-
-
-
?
beechwood xylan + H2O
?
low activity
-
-
?
beechwood xylan + H2O
?
about 20% activity compared to Avicel
-
-
?
beta-cellobiosyl fluoride + H2O
fluoride + cellobiose
-
-
-
-
?
beta-cellobiosyl fluoride + H2O
fluoride + cellobiose
-
-
-
-
?
beta-D-glucan + H2O
?
Thermochaetoides thermophila
highest activity
-
-
?
beta-D-glucan + H2O
?
Thermochaetoides thermophila DSM 1495
highest activity
-
-
?
beta-glucan + H2O
?
-
227% activity compared to cellulose
-
-
?
beta-glucan + H2O
?
low activity
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
low specific activity
-
-
?
carboxymethyl cellulose + H2O
?
-
low specific activity
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
Thermochaetoides thermophila
lowest activity
-
-
?
carboxymethyl cellulose + H2O
?
Thermochaetoides thermophila DSM 1495
lowest activity
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
?
-
-
-
?
carboxymethyl cellulose + H2O
cellobiose + ?
-
-
-
?
carboxymethyl cellulose + H2O
cellobiose + ?
-
-
-
?
carboxymethyl cellulose + H2O
cellobiose + ?
high activity
-
-
?
carboxymethylcellulose + H2O
cellobiose + ?
-
-
-
-
?
carboxymethylcellulose + H2O
cellobiose + ?
-
-
-
-
?
carboxymethylcellulose + H2O
cellobiose + ?
Thermochaetoides thermophila
-
-
-
-
?
carboxymethylcellulose + H2O
cellobiose + ?
-
-
-
?
carboxymethylcellulose + H2O
cellobiose + ?
-
-
-
-
?
carboxymethylcellulose + H2O
cellobiose + ?
-
-
-
-
?
carboxymethylcellulose + H2O
cellobiose + ?
-
little activity
-
-
?
carboxymethylcellulose + H2O
cellobiose + ?
-
-
-
-
?
carboxymethylcellulose + H2O
cellobiose + ?
-
-
CBH I, exo-glucanase
?
carboxymethylcellulose + H2O
glucose + cellobiose + cellutetraose
-
-
-
-
?
carboxymethylcellulose + H2O
glucose + cellobiose + cellutetraose
-
-
-
-
?
carboxymethylcellulose + H2O
glucose + cellobiose + cellutetraose
-
-
-
-
?
carboxymethylcellulose + H2O
glucose + cellobiose + cellutetraose
-
-
CBH II, endo-glucanase
?
cellohexaose + 3 H2O
3 cellobiose
complete degradation within 30 min, 50°C
-
-
?
cellohexaose + 3 H2O
3 cellobiose
complete degradation within 30 min, 50°C
-
-
?
cellohexaose + H2O
cellobiose + cellotriose + cellotetraose
-
-
enzyme does not release D-glucose
-
?
cellohexaose + H2O
cellobiose + cellotriose + cellotetraose
-
-
enzyme does not release D-glucose
-
?
cellohexaose + H2O
cellotriose + cellobiose + cellotetraose
-
-
-
-
?
cellohexaose + H2O
cellotriose + cellobiose + cellotetraose
-
-
-
?
cellohexaose + H2O
cellotriose + cellobiose + cellotetraose
-
-
-
-
?
cellopentaose + H2O
cellobiose + ?
-
-
-
-
?
cellopentaose + H2O
cellobiose + ?
-
-
cellobiose is the major product
-
?
cellopentaose + H2O
cellobiose + ?
-
-
cellobiose is the major product
-
?
cellopentaose + H2O
cellobiose + cellotriose
-
good substrate
-
-
?
cellopentaose + H2O
cellobiose + cellotriose
-
-
-
?
cellopentaose + H2O
cellobiose + D-glucose + cellotriose
-
-
-
?
cellopentaose + H2O
cellobiose + D-glucose + cellotriose
-
-
-
?
cellopentaose + H2O
cellobiose + D-glucose + cellotriose
-
-
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
-
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
-
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
-
cellobiose is preferentialls released from the nonreducing end by exocellulase E3, cellopentaose is labeled at the reducing end with (18)O, the products are analyzed by ionspray mass spectrometry, 61% of the (18)O is found in cellotriose
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
complete degradation within 30 min, 50°C
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
complete degradation within 30 min, 50°C
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
-
cellobiose is preferentially released from the nonreducing end by CBH II, cellopentaose is labeled at the reducing end with (18)O, the products are analyzed by ionspray mass spectrometry, 63% of the (18)O is found in cellotriose
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
?
cellotetraose + H2O
2 cellobiose
-
-
-
?
cellotetraose + H2O
2 cellobiose
complete degradation within 30 min, 50°C
-
-
?
cellotetraose + H2O
2 cellobiose
complete degradation within 30 min, 50°C
-
-
?
cellotetraose + H2O
cellobiose + ?
-
good substrate
-
-
?
cellotetraose + H2O
cellobiose + ?
-
-
cellobiose is the major product
-
?
cellotetraose + H2O
cellobiose + D-glucose + cellotriose
-
-
different combinations and proportions of products
?
cellotetraose + H2O
cellobiose + D-glucose + cellotriose
-
-
preferably cellobiose
?
cellotetraose + H2O
cellobiose + D-glucose + cellotriose
-
-
-
-
?
cellotetraose + H2O
cellobiose + D-glucose + cellotriose
-
-
-
?
cellotetraose + H2O
cellobiose + D-glucose + cellotriose
-
-
different combinations and proportions of products
?
cellotetraose + H2O
cellobiose + D-glucose + cellotriose
-
-
-
-
?
cellotetraose + H2O
cellobiose + D-glucose + cellotriose
-
-
-
?
cellotriose + H2O
cellobiose + D-glucose
-
-
-
-
?
cellotriose + H2O
cellobiose + D-glucose
complete degradation within 30 min, 50°C
-
-
?
cellotriose + H2O
cellobiose + D-glucose
complete degradation within 30 min, 50°C
-
-
?
cellotriose + H2O
cellobiose + glucose
-
-
-
-
?
cellotriose + H2O
cellobiose + glucose
-
-
-
-
?
cellotriose + H2O
cellobiose + glucose
-
-
-
?
cellotriose + H2O
cellobiose + glucose
-
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
?
-
cellobiohydrolases act from one end of a cellulose chain and processively cleave off cellobiose as the main product. Processivity and synergism are important properties of cellulases, particularly for hydrolysis of crystalline substrates
-
-
?
cellulose + H2O
?
-
substrates are phosphoric acid-treated cotton, carboxymethylcellulose, bacterial microcrystalline cellulose, and phosphoric acid-swollen cellulose, as well as 8-mg/ml Whatman no. 1 filter paper, substrate specificity of wild-type and mutant enzymes, overview
-
-
?
cellulose + H2O
?
-
-
-
?
cellulose + H2O
?
-
-
-
-
?
cellulose + H2O
beta-cellobiose + ?
-
-
-
-
?
cellulose + H2O
beta-cellobiose + ?
-
-
-
-
?
cellulose + H2O
cellobiose + ?
-
-
-
?
cellulose + H2O
cellobiose + ?
-
-
-
?
cellulose + H2O
cellobiose + ?
-
-
-
?
cellulose + H2O
cellobiose + ?
-
-
-
?
cellulose + H2O
cellobiose + ?
cellulolytic enzyme
-
-
?
cellulose + H2O
cellobiose + ?
-
-
-
-
?
cellulose + H2O
cellobiose + ?
-
-
-
?
cellulose + H2O
cellobiose + ?
the enzyme hydrolyzes beta-1,4-linkages
-
-
?
cellulose + H2O
cellobiose + ?
-
100% activity with 5 mg cellulose, 30% activity with 0.5 mg cellulose as substrate
-
-
?
cellulose + H2O
cellobiose + ?
-
-
-
-
?
cellulose + H2O
cellobiose + ?
the enzyme acts on nonreducing end of cellulose
-
-
?
cellulose + H2O
cellobiose + ?
-
-
-
-
?
cellulose + H2O
cellobiose + ?
-
-
-
?
cellulose + H2O
cellobiose + ?
-
activity with bacterial microcrystalline cellulose, phosphoric acid-treated swollen cellulose, phosphoric acid-treated cotton, and carboxymethyl cellulose
-
-
?
cellulose + H2O
cellobiose + ?
Thermochaetoides thermophila
-
-
-
-
?
cellulose + H2O
cellobiose + ?
Thermochaetoides thermophila
-
-
-
?
cellulose + H2O
cellobiose + ?
-
hydrolyses pure cellulose, either as highly crystalline native cotton or as highly hydrated amorphous cellulose. No activity with carboxymethylcellulose
-
-
?
cellulose + H2O
cellobiose + ?
-
hydrolyses pure cellulose, either as highly crystalline native cotton or as highly hydrated amorphous cellulose. No activity with carboxymethylcellulose
-
-
?
cellulose + H2O
cellobiose + ?
-
-
-
-
?
cellulose + H2O
cellobiose + ?
-
hydrolysis of filter paper by intact cellobiohydrolase I in the presence of additional cellulose binding domains has a synergistic effect, leading to an increase of the sugar production of up to 30%
-
-
?
cellulose + H2O
cellobiose + ?
-
the enzyme acts on anthranilic-acid-labelled bacterial cellulose, bacterial microcrystalline cellulose, and endoglucanase-pretreated bacterial cellulose, preparation, overview
-
-
?
cellulose + H2O
cellobiose + ?
-
-
-
-
?
cellulose + H2O
cellobiose + ?
-
the enzyme acts on anthranilic-acid-labelled bacterial cellulose, bacterial microcrystalline cellulose, and endoglucanase-pretreated bacterial cellulose, preparation, overview
-
-
?
cellulose + H2O
cellobiose + ?
-
-
-
-
?
cellulose + H2O
cellobiose + D-glucose + cellotriose
-
-
-
-
?
cellulose + H2O
cellobiose + D-glucose + cellotriose
-
-
-
-
?
cellulose + H2O
cellobiose + D-glucose + cellotriose
-
-
-
-
?
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 + 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 + 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 + H2O
cellobiose + D-glucose + cellotriose
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + D-glucose + cellotriose
-
Cel6A is a more endo-processive enzyme, whereas Cel7A is essentially a processive enzyme, both forms show a synergistic effect in the digestion of bacterial cellulose
-
-
?
cellulose + H2O
cellobiose + 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 + H2O
cellobiose + D-glucose + cellotriose
-
-
only cellobiose
?
cellulose + H2O
cellobiose + D-glucose + cellotriose
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + D-glucose + cellotriose
-
-
-
-
?
cellulose + H2O
cellobiose + D-glucose + cellotriose
-
-
-
-
?
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 + 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 + H2O
cellobiose + D-glucose + cellotriose
-
-
different combinations and proportions of products depending on organism
?
cellulose + H2O
cellobiose + D-glucose + cellotriose
-
-
-
?
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 + H2O
cellobiose + D-glucose + cellotriose
-
-
-
-
?
cellulose + H2O
cellobiose + D-glucose + cellotriose
-
-
-
-
?
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 + H2O
cellobiose + D-glucose + cellotriose
-
-
-
-
?
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 + 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 + 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 + H2O
cellobiose + D-glucose + cellotriose
-
-
-
-
?
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 + 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 + H2O
cellobiose + D-glucose + cellotriose
-
-
different combinations and proportions of products depending on organism
?
chito-oligosaccharide + H2O
?
oligosaccharides with a degree of polymerization between three and six units, product analysis by analyzed by mass and NMR spectrometry
-
-
?
chito-oligosaccharide + H2O
?
oligosaccharides with a degree of polymerization between three and six units, product analysis by analyzed by mass and NMR spectrometry
-
-
?
chito-oligosaccharide + H2O
?
oligosaccharides with a degree of polymerization between three and six units, product analysis by analyzed by mass and NMR spectrometry
-
-
?
chito-oligosaccharide + H2O
?
oligosaccharides with a degree of polymerization between three and six units, product analysis by analyzed by mass and NMR spectrometry
-
-
?
chito-oligosaccharide + H2O
?
oligosaccharides with a degree of polymerization between three and six units, product analysis by analyzed by mass and NMR spectrometry
-
-
?
chito-oligosaccharide + H2O
?
oligosaccharides with a degree of polymerization between three and six units, product analysis by analyzed by mass and NMR spectrometry
-
-
?
chito-oligosaccharide + H2O
?
oligosaccharides with a degree of polymerization between three and six units, product analysis by analyzed by mass and NMR spectrometry
-
-
?
chitosan + H2O
N-acetyl-D-glucosamine + ?
DA13
-
-
?
chitosan + H2O
N-acetyl-D-glucosamine + ?
DA13
-
-
?
chitosan + H2O
N-acetyl-D-glucosamine + ?
DA13
-
-
?
chitosan + H2O
N-acetyl-D-glucosamine + ?
DA13
-
-
?
chitosan + H2O
N-acetyl-D-glucosamine + ?
DA13
-
-
?
chitosan + H2O
N-acetyl-D-glucosamine + ?
DA13
-
-
?
chitosan + H2O
N-acetyl-D-glucosamine + ?
DA13
-
-
?
corncob residue + H2O
?
-
-
-
?
corncob residue + H2O
?
-
-
-
?
filter paper + H2O
?
low activity
-
-
?
filter paper + H2O
?
about 18% activity compared to Avicel
-
-
?
filter paper + H2O
?
-
-
-
-
?
filter paper + H2O
?
-
-
-
-
?
filter paper + H2O
?
-
-
-
-
?
galactan + H2O
?
low activity
-
-
?
galactan + H2O
?
about 30% activity compared to Avicel
-
-
?
galactan + H2O
?
-
about 30% activity compared to Avicel
-
-
?
laminarin + H2O
?
-
1.5% activity compared to 4-nitrophenyl beta-D-cellobioside
-
-
?
laminarin + H2O
?
-
1.5% activity compared to 4-nitrophenyl beta-D-cellobioside
-
-
?
lichenan + H2O
?
-
-
-
-
?
lichenan + H2O
?
-
-
-
-
?
lichenan + H2O
?
-
33.8% activity compared to 4-nitrophenyl beta-D-cellobioside
-
-
?
lichenan + H2O
?
-
33.8% activity compared to 4-nitrophenyl beta-D-cellobioside
-
-
?
lichenan + H2O
?
-
high specific activity
-
-
?
lichenan + H2O
?
-
high specific activity
-
-
?
lichenan + H2O
?
Thermochaetoides thermophila
-
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + beta-D-cellobiose
-
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + beta-D-cellobiose
-
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
-
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
-
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
-
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
-
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
-
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
-
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
-
-
-
-
?
p-nitrophenyl-beta-D-cellobioside + H2O
p-nitrophenol + cellobiose
-
-
-
-
?
p-nitrophenyl-lactoside + H2O
p-nitrophenol + lactose
-
-
-
-
?
p-nitrophenyl-lactoside + H2O
p-nitrophenol + lactose
-
-
-
-
?
p-nitrophenyl-lactoside + H2O
p-nitrophenol + lactose
-
-
-
-
?
p-nitrophenyl-lactoside + H2O
p-nitrophenol + lactose
-
-
-
-
?
phosphoric acid swollen cellulose + H2O
?
-
217% activity compared to cellulose
-
-
?
phosphoric acid swollen cellulose + H2O
?
Thermochaetoides thermophila
-
-
-
?
phosphoric acid swollen cellulose + H2O
?
Thermochaetoides thermophila DSM 1495
-
-
-
?
phosphoric acid swollen cellulose + H2O
?
-
-
-
?
phosphoric acid swollen cellulose + H2O
?
-
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + ?
-
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + ?
Thermochaetoides thermophila
-
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + ?
-
-
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + ?
-
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + cellotriose + ?
-
shows 9fold higher activity toward phosphoric acid swollen cellulose than toward avicel
-
-
?
phosphoric acid swollen cellulose + H2O
cellobiose + cellotriose + ?
-
shows 9fold higher activity toward phosphoric acid swollen cellulose than toward avicel
-
-
?
sodium hydroxide pretreated corn stover + H2O
?
-
-
-
-
?
sodium hydroxide pretreated corn stover + H2O
?
-
-
-
-
?
stachyose + H2O
?
about 18% activity compared to Avicel
-
-
?
stachyose + H2O
?
-
about 18% activity compared to Avicel
-
-
?
xylan + H2O
?
-
1.13% activity compared to 4-nitrophenyl beta-D-cellobioside
-
-
?
xylan + H2O
?
-
1.13% activity compared to 4-nitrophenyl beta-D-cellobioside
-
-
?
xylan + H2O
xylobiose + xylotetraose + xylohexaose
-
-
-
-
?
xylan + H2O
xylobiose + xylotetraose + xylohexaose
-
-
-
?
xylan + H2O
xylobiose + xylotetraose + xylohexaose
-
-
-
?
xyloglucan + H2O
?
low activity
-
-
?
xyloglucan + H2O
?
about 37% activity compared to Avicel
-
-
?
xyloglucan + H2O
?
-
about 37% activity compared to Avicel
-
-
?
additional information
?
-
-
no substrates: Avicel, cotton, cellulose powder. Enzyme splits off strictly cellobiose units from the nonreducing end of the cellulose chain with an exowise mechanism
-
-
?
additional information
?
-
no activity with 4-methylumbelliferyl beta-D-lactopyranoside or 4-methylumbelliferyl beta-D-cellobioside
-
-
?
additional information
?
-
no activity with 4-methylumbelliferyl beta-D-lactopyranoside or 4-methylumbelliferyl beta-D-cellobioside
-
-
?
additional information
?
-
no activity with 4-methylumbelliferyl beta-D-lactopyranoside or 4-methylumbelliferyl beta-D-cellobioside
-
-
?
additional information
?
-
no activity with 4-methylumbelliferyl beta-D-lactopyranoside or 4-methylumbelliferyl beta-D-cellobioside
-
-
?
additional information
?
-
4-nitrophenyl beta-D-glucopyranoside is not a substrate
-
-
?
additional information
?
-
-
4-nitrophenyl beta-D-glucopyranoside is not a substrate
-
-
?
additional information
?
-
-
not: cellobiose
-
-
?
additional information
?
-
-
no activity with cellotriose, and cellotetraose
-
-
?
additional information
?
-
-
no activity with cellotriose, and cellotetraose
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
not: cellobiose
-
-
?
additional information
?
-
-
hydrolyses internal glucosidic linkages of beta-1,3, 1,4-D-glucan
-
-
?
additional information
?
-
-
has a multi domain structure composed of a cellulose-binding domain, a Ser/Thr/Pro-rich linker, and a catalytic domain belonging to family 6 of glycosyl hydrolases, from the N-terminus
-
-
?
additional information
?
-
-
has a multi domain structure composed of a cellulose-binding domain, a Ser/Thr/Pro-rich linker, and a catalytic domain belonging to family 6 of glycosyl hydrolases, from the N-terminus
-
-
?
additional information
?
-
-
no detectable activity on laminarin, 4-nitrophenyl-beta-D-glucopyranoside, oat spelt xylan, and birch wood xylan
-
-
?
additional information
?
-
-
no detectable activity on laminarin, 4-nitrophenyl-beta-D-glucopyranoside, oat spelt xylan, and birch wood xylan
-
-
?
additional information
?
-
-
no substrates: avicel, soluble oat spelt xylan, Pachyman, 4-nitrophenyl-beta-D-cellobioside, 4-nitrophenyl-beta-D-galactopyranoside
-
-
?
additional information
?
-
-
no substrates: avicel, soluble oat spelt xylan, Pachyman, 4-nitrophenyl-beta-D-cellobioside, 4-nitrophenyl-beta-D-galactopyranoside
-
-
?
additional information
?
-
substrate specificity, overview
-
-
?
additional information
?
-
-
the enzyme liberates cellobiose and cellotriose from the nonreducing ends and requires at least four contiguous beta-1,4-linked glucosyl units for a substrate but does not recognize sulforhodamine-conjugated 1-amino-1-deoxyglucitol. ulforhodamine-conjugated cellotetraose, carboxymethylcellulose, hydroxyethyl cellulose, xylan, and mannan are no substrates
-
-
?
additional information
?
-
-
no hydrolysis of a soluble cellulose derivative and barley (1-3),(1-4)-beta-D-glucan
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
the enzyme completely lacks chromogenic activity on the 4-nitrophenyl-cellodextrins from 4-nitrophenyl glucoside to 4-nitrophenyl cellobioside
-
-
?
additional information
?
-
the enzyme completely lacks chromogenic activity on the 4-nitrophenyl-cellodextrins from 4-nitrophenyl glucoside to 4-nitrophenyl cellobioside
-
-
?
additional information
?
-
-
no activity with cellotriose, alpha-cellulose, cellobiose, and raffinose. The enzyme completely lacks chromogenic activity on the 4-nitrophenyl cellodextrins from 4-nitrophenyl glucoside to 4-nitrophenyl cellobioside
-
-
?
additional information
?
-
no activity with cellotriose, alpha-cellulose, cellobiose, and raffinose. The enzyme completely lacks chromogenic activity on the 4-nitrophenyl cellodextrins from 4-nitrophenyl glucoside to 4-nitrophenyl cellobioside
-
-
?
additional information
?
-
-
no activity with cellotriose, alpha-cellulose, cellobiose, and raffinose. The enzyme completely lacks chromogenic activity on the 4-nitrophenyl cellodextrins from 4-nitrophenyl glucoside to 4-nitrophenyl cellobioside
-
-
?
additional information
?
-
-
does not hydrolyze carboxymethylcellulose
-
-
?
additional information
?
-
-
does not hydrolyze carboxymethylcellulose
-
-
?
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
?
-
-
not: cellobiose
-
-
?
additional information
?
-
no substrates: avicel, 4-methylumbelliferyl beta-D-cellobioside, 4-nitrophenyl beta-D-cellobioside, 4-nitrophenyl beta-D-lactopyranoside
-
-
?
additional information
?
-
-
no substrates: avicel, 4-methylumbelliferyl beta-D-cellobioside, 4-nitrophenyl beta-D-cellobioside, 4-nitrophenyl beta-D-lactopyranoside
-
-
?
additional information
?
-
-
TTCBH6B is active against shorter oligosaccharides rather than polysaccharides
-
-
?
additional information
?
-
no substrates: avicel, 4-methylumbelliferyl beta-D-cellobioside, 4-nitrophenyl beta-D-cellobioside, 4-nitrophenyl beta-D-lactopyranoside
-
-
?
additional information
?
-
comparison of activities on chitosan by cellobiohydrolases, chitosanases, and lysozyme, oligomer pattern, overview. The different enzymes produce chito-oligosaccharides (COSs) with varying acetylation, NMR spectrometric analysis. The preferred cleavage site of enzyme CBH is between GlcN and GlcN
-
-
?
additional information
?
-
comparison of activities on chitosan by cellobiohydrolases, chitosanases, and lysozyme, oligomer pattern, overview. The different enzymes produce chito-oligosaccharides (COSs) with varying acetylation, NMR spectrometric analysis. The preferred cleavage site of enzyme CBH is between GlcN and GlcN
-
-
?
additional information
?
-
-
cellobiose slightly
-
-
?
additional information
?
-
-
Cel5A treated cellulose is no longer a substrate for Cel6A or Cel7A
-
-
?
additional information
?
-
no activity on oat spelt xylan, carboxymethylcellulose, xylobiose, cellobiose, 4-nitrophenyl-cellobiose, and 4-nitrophenyl derivatives of other disaccharides, overview
-
-
?
additional information
?
-
no activity on oat spelt xylan, carboxymethylcellulose, xylobiose, cellobiose, 4-nitrophenyl-cellobiose, and 4-nitrophenyl derivatives of other disaccharides, overview
-
-
?
additional information
?
-
no activity on oat spelt xylan, carboxymethylcellulose, xylobiose, cellobiose, and 4-nitrophenyl derivatives of other disaccharides, overview
-
-
?
additional information
?
-
no activity on oat spelt xylan, carboxymethylcellulose, xylobiose, cellobiose, and 4-nitrophenyl derivatives of other disaccharides, overview
-
-
?
additional information
?
-
-
binding constant to crystalline cellulose nanowhiskers is about 1000000 per M for Cel6A. 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
?
-
-
Cel6A hydrolyzes cellulose chain from the nonreducing end, while the binding module (CBMCel6A) is likely binding to the reducing end
-
-
?
additional information
?
-
-
compared to cellobiohydrolase Cel7A, cellobiohydrolase Cel6A is catalytically more efficient but less capable of attacking a broad range of structurally distinct sites on the cellulose surface
-
-
?
additional information
?
-
comparison of activities on chitosan by cellobiohydrolases, chitosanases, and lysozyme, oligomer pattern, overview. The different enzymes produce chito-oligosaccharides (COSs) with varying acetylation, NMR spectrometric analysis
-
-
?
additional information
?
-
comparison of activities on chitosan by cellobiohydrolases, chitosanases, and lysozyme, oligomer pattern, overview. The different enzymes produce chito-oligosaccharides (COSs) with varying acetylation, NMR spectrometric analysis
-
-
?
additional information
?
-
comparison of activities on chitosan by cellobiohydrolases, chitosanases, and lysozyme, oligomer pattern, overview. The different enzymes produce chito-oligosaccharides (COSs) with varying acetylation, NMR spectrometric analysis
-
-
?
additional information
?
-
comparison of activities on chitosan by cellobiohydrolases, chitosanases, and lysozyme, oligomer pattern, overview. The different enzymes produce chito-oligosaccharides (COSs) with varying acetylation, NMR spectrometric analysis
-
-
?
additional information
?
-
-
Cel5A treated cellulose is no longer a substrate for Cel6A or Cel7A
-
-
?
additional information
?
-
comparison of activities on chitosan by cellobiohydrolases, chitosanases, and lysozyme, oligomer pattern, overview. The different enzymes produce chito-oligosaccharides (COSs) with varying acetylation, NMR spectrometric analysis
-
-
?
additional information
?
-
-
-
-
-
?
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D262A
site-directed mutagenesis, mutation of the the module interface residue affects the interaction of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
D264A
site-directed mutagenesis, mutation of the the module interface residue affects the interaction of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
T230A
site-directed mutagenesis, mutation of the module interface residue affects the final fold and stability of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
T230A/D262A
site-directed mutagenesis, mutation of the residues affects the interaction of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
W678G
the binding free energies between the substrate and the mutant are higher than those of the wild type enzyme. The pull forces and energy barrier in the mutant is also reduced significantly
Y555S
the binding free energies between the substrate and the mutant are higher than those of the wild type enzyme. The pull forces and energy barrier in the mutant is also reduced significantly
D262A
-
site-directed mutagenesis, mutation of the the module interface residue affects the interaction of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
-
D264A
-
site-directed mutagenesis, mutation of the the module interface residue affects the interaction of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
-
T230A
-
site-directed mutagenesis, mutation of the module interface residue affects the final fold and stability of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
-
T230A/D262A
-
site-directed mutagenesis, mutation of the residues affects the interaction of immunoglobulin-like module and the catalytic module, the mutant shows similar activity, but reduced stability and an altered mechanism in thermal unfolding compared to the wild-type enzyme
-
A385P
-
the mutant shows a T50 value of 64.7°C
C313S
random mutagenesis, the mutation causes increased thermostability of the mutant enzyme compared to the wild-type, with decreased inactivation, increased maximum Avicel hydrolysis temperature, and improved long time hydrolysis performance
D405A
about 1% enzyme activity
D405N
only small structural changes, about 1% enzyme activity
M235P
-
the mutant shows a T50 value of 63.1°C
Q390P
-
the mutant shows a T50 value of 66.1°C
S215P
-
the mutant shows a T50 value of 65.6°C
C313S
-
random mutagenesis, the mutation causes increased thermostability of the mutant enzyme compared to the wild-type, with decreased inactivation, increased maximum Avicel hydrolysis temperature, and improved long time hydrolysis performance
A401P
-
the mutant enzyme shows improved thermostability compared to the wild type enzyme
A426P
-
the mutant shows 86.9% of wild type activity
S273P
-
the mutant enzyme shows improved thermostability compared to the wild type enzyme
S298P
-
the mutant shows 88% of wild type activity
T237G
-
the mutant enzyme shows improved thermostability compared to the wild type enzyme
T262G
-
the mutant shows 94.4% of wild type activity
T262G /S298P /A426P
-
the mutant shows 95.7% of wild type activity
D226A
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme. The D226A enzyme has a very low activity on insoluble cellulose, not improved by sodium azide
D226A/S232A
-
site-directed mutagenesis, the mutant is almost inactive and shows slightly decreased ligand binding compared to the wild-type enzyme
D274A
-
site-directed mutagenesis, the mutant shows altered and highly reduced substrate specificity compared to the wild-type enzyme
D497A
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
D512A
-
site-directed mutagenesis, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
E495A
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme
L230A
-
site-directed mutagenesis, the mutation causes slightly increased processivity and increased activity with phosphoric acid-treated cotton over 250%, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
M514A
-
site-directed mutagenesis, the mutation alters the secondary structure of the enzyme, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
M514Q
-
site-directed mutagenesis, the mutation alters the secondary structure of the enzyme, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
N282A
-
site-directed mutagenesis, mutation in residue near the tunnel entrance causes a twofold increase in processivity, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
N282D
-
site-directed mutagenesis, mutation in residue near the tunnel entrance causes a twofold increase in processivity, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
R180A
-
site-directed mutagenesis, mutation in residue near the tunnel exit causes a twofold increase in processivity, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
R180K
-
site-directed mutagenesis, mutation in residue near the tunnel exit causes a twofold increase in processivity, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
S232A
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme. The S232A enzyme retains near wild-type activity on most substrates, but carboxymethylcellulose activity is drastically reduced
W464A
-
site-directed mutagenesis, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
W464Y
-
site-directed mutagenesis, the mutant shows altered polysaccharide substrate specificity compared to the wild-type enzyme
Y220A
-
site-directed mutagenesis, the mutant shows altered substrate specificity compared to the wild-type enzyme, alomost inactive mutant
S131W
Thermochaetoides thermophila
the mutant with reduced activity exhibits effectively enhanced heat resistance to elevated temperatures. The half-life of this mutant enzyme is increased 1.42 and 2.40fold at 80°C and 90°C, respectively, compared to the wild type
W221R
Thermochaetoides thermophila
the mutant shows significantly declined activity compared to the wild type enzyme
W315R
Thermochaetoides thermophila
the mutant shows significantly declined activity compared to the wild type enzyme
Y119F
Thermochaetoides thermophila
the mutation increases the catalytic activity 1.82, 1.65 and 1.43fold against beta-D-glucan, phosphoric acid swollen cellulose and carboxymethyl cellulose, respectively, compared to the wild type enzyme
S131W
Thermochaetoides thermophila DSM 1495
-
the mutant with reduced activity exhibits effectively enhanced heat resistance to elevated temperatures. The half-life of this mutant enzyme is increased 1.42 and 2.40fold at 80°C and 90°C, respectively, compared to the wild type
-
W221R
Thermochaetoides thermophila DSM 1495
-
the mutant shows significantly declined activity compared to the wild type enzyme
-
W315R
Thermochaetoides thermophila DSM 1495
-
the mutant shows significantly declined activity compared to the wild type enzyme
-
Y119F
Thermochaetoides thermophila DSM 1495
-
the mutation increases the catalytic activity 1.82, 1.65 and 1.43fold against beta-D-glucan, phosphoric acid swollen cellulose and carboxymethyl cellulose, respectively, compared to the wild type enzyme
-
Y466A
the mutation greatly reduces the cellulose-binding ability
Y492A
the mutation greatly reduces the cellulose-binding ability
Y493A
the mutation greatly reduces the cellulose-binding ability
C313S
random mutagenesis, the mutation causes increased thermostability of the mutant enzyme compared to the wild-type, with decreased inactivation, increased maximum Avicel hydrolysis temperature, and improved long time hydrolysis performance. The C313S mutation increases total Humicola jecorina CBH II activity secreted by the Saccharomyces cerevisiae expression host more than 10fold
D175A
mutant retains some activity on longer oligosaccharides
D221A
almost complete loss of activity
D241C/D249C
thermostability similar to wild-type enzyme
DELTAG245-Y252
reduced thermostability
E107Q
mutant enzyme is destabilized at acidic pH and stabilized at alkaline pH
E107Q/D170N/D366N
mutant enzyme is destabilized at acidic pH and stabilized at alkaline pH
E212Q
site-directed mutagenesis, catalytic residue, inactive mutant
E217Q
site-directed mutagenesis, catalytic residue, inactive mutant
M134L
-
the mutant shows a T50 value of 62°C
Q276L
-
the mutant shows a T50 value of 58.6°C
S30F
-
the mutant shows a T50 value of 60.3°C
S316P
-
the mutant shows a T50 value of 61.9°C
S406P
-
the mutant shows a T50 value of 61.5°C
S413P
-
the mutant shows a T50 value of 63.8°C
Y247F
slight reduction of kcat on 4-nitrophenyl lactoside, but only a small effect on cellulose hydrolysis
Y31A
-
structural role minor, but does not bind strongly to cellulose
Y32A
-
structural role minor, but does not bind strongly to cellulose
Y5A
-
complete loss of binding affinity to cellulose
D416A
active center N-terminal loop has a more open conformation
D416A
crystal structure similar to wild-type enzyme, mutant retains about 10% of wild-type activity
D131A
the mutant protein displays the enzymatic activity of a typical endoglucanase. The mutant is as proficient as wild type enzyme in inducing rice immune responses, but is deficient in virulence-promoting activity
D131A
-
the mutant protein displays the enzymatic activity of a typical endoglucanase. The mutant is as proficient as wild type enzyme in inducing rice immune responses, but is deficient in virulence-promoting activity
-
additional information
elimination of the enzyme's immunoglobulin-like module leads to its complete inactivation
additional information
-
elimination of the enzyme's immunoglobulin-like module leads to its complete inactivation
-
additional information
construction of deletion mutants expressing solely the aminoterminal domain containing the exoglucanase activity. Temperature optimum and stability of the deletion mutants are the same as wild-type
additional information
construction of the recombinant Cex-RsaA fusion mutant by fusion of the C-terminus of Caulobacter crescentus surface (S)-layer protein RsaA with the beta-1,4-glycanase Cex from the cellulolytic bacterium Cellulomonas fimi, the RsaA C-terminus causes a spontaneous unstructured aggregation of the recombinant protein
additional information
-
construction of the recombinant Cex-RsaA fusion mutant by fusion of the C-terminus of Caulobacter crescentus surface (S)-layer protein RsaA with the beta-1,4-glycanase Cex from the cellulolytic bacterium Cellulomonas fimi, the RsaA C-terminus causes a spontaneous unstructured aggregation of the recombinant protein
additional information
-
CelC7 is insoluble when expressed in Escherichia coli. Deletion of 17 or 105 residues from the N-terminus significantly improves its solubility
additional information
-
CelC7 is insoluble when expressed in Escherichia coli. Deletion of 17 or 105 residues from the N-terminus significantly improves its solubility
-
additional information
-
mixtures of the Cel6B mutant enzymes and Thermobifida fusca endocellulase Cel5A do not show increased synergism or processivity, and the mutant enzyme which has the highest processivity give the poorest synergism
additional information
-
the enzyme from overexpressing line C10 performs better than the wild-type from ZU-02 in enzymatic hydrolysis because the exoexo-synergism plays a role, overview
additional information
-
the enzyme from overexpressing line C10 performs better than the wild-type from ZU-02 in enzymatic hydrolysis because the exoexo-synergism plays a role, overview
-
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