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(carboxymethyl)cellulose + H2O
(carboxymethyl)cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
(carboxymethyl)cellulose + H2O
?
4-methylumbelliferyl cellopentaoside + H2O
cellotetraose + 4-methylumbelliferyl beta-D-glucopyranoside
-
Substrates: -
Products: -
?
4-methylumbelliferyl cellotetraoside + H2O
cellotriose + 4-methylumbelliferyl beta-D-glucopyranoside
-
Substrates: -
Products: -
?
4-methylumbelliferyl cellotrioside + H2O
cellobiose + 4-methylumbelliferyl beta-D-glucopyranoside
-
Substrates: -
Products: -
?
beta-glucan + H2O
?
-
Substrates: -
Products: -
?
carboxymethyl cellulose + H2O
?
Substrates: -
Products: -
?
carboxymethyl cellulose + H2O
carboxymethyl cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
carboxymethylcellulose + H2O
?
castor oil bean seed cake + H2O
?
H3PO4 -swollen cellulose + H2O
?
-
Substrates: -
Products: -
?
hydroxyethylcellulose + H2O
?
-
Substrates: -
Products: -
?
lichenan + H2O
?
-
Substrates: -
Products: -
?
pullulan + H2O
?
-
Substrates: 7.2% of the activity with (carboxymethyl)cellulose
Products: -
?
remazol brilliant blue R-carboxymethylcellulose + H2O
?
steam-exploded bagasse + H2O
?
-
Substrates: -
Products: -
?
xylan + H2O
?
-
Substrates: 6.8% of the activity with (carboxymethyl)cellulose
Products: -
?
additional information
?
-
(carboxymethyl)cellulose + H2O
(carboxymethyl)cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
-
Substrates: -
Products: -
?
(carboxymethyl)cellulose + H2O
(carboxymethyl)cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
-
Substrates: specific substrate
Products: -
?
(carboxymethyl)cellulose + H2O
(carboxymethyl)cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
-
Substrates: specific substrate
Products: -
?
(carboxymethyl)cellulose + H2O
(carboxymethyl)cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
-
Substrates: specific substrate
Products: -
?
(carboxymethyl)cellulose + H2O
(carboxymethyl)cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
-
Substrates: -
Products: -
?
(carboxymethyl)cellulose + H2O
?
-
Substrates: -
Products: -
?
(carboxymethyl)cellulose + H2O
?
-
Substrates: -
Products: -
?
(carboxymethyl)cellulose + H2O
?
-
Substrates: -
Products: -
?
(carboxymethyl)cellulose + H2O
?
-
Substrates: -
Products: -
?
(carboxymethyl)cellulose + H2O
?
-
Substrates: -
Products: -
?
(carboxymethyl)cellulose + H2O
?
-
Substrates: -
Products: -
?
(carboxymethyl)cellulose + H2O
?
-
Substrates: -
Products: -
?
(carboxymethyl)cellulose + H2O
?
-
Substrates: -
Products: -
?
avicel + H2O
?
-
Substrates: -
Products: -
?
avicel + H2O
?
-
Substrates: 29.8% of the activity with (carboxymethyl)cellulose
Products: -
?
carboxymethyl cellulose + H2O
carboxymethyl cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
Substrates: -
Products: -
?
carboxymethyl cellulose + H2O
carboxymethyl cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
Substrates: -
Products: -
?
carboxymethylcellulose + H2O
?
-
Substrates: enzyme is specific for carboxymethylcellulose
Products: -
?
carboxymethylcellulose + H2O
?
-
Substrates: enzyme is specific for carboxymethylcellulose
Products: -
?
carboxymethylcellulose + H2O
?
-
Substrates: enzyme is specific for carboxymethylcellulose
Products: -
?
castor oil bean seed cake + H2O
?
-
Substrates: -
Products: -
?
castor oil bean seed cake + H2O
?
-
Substrates: -
Products: -
?
filter paper + H2O
?
-
Substrates: -
Products: -
?
filter paper + H2O
?
-
Substrates: -
Products: -
?
filter paper + H2O
?
-
Substrates: 19.5% of the activity with (carboxymethyl)cellulose
Products: -
?
glucan + H2O
?
-
Substrates: highest activity
Products: -
?
glucan + H2O
?
-
Substrates: highest activity
Products: -
?
laminarin + H2O
?
-
Substrates: -
Products: -
?
laminarin + H2O
?
-
Substrates: -
Products: -
?
laminarin + H2O
?
-
Substrates: -
Products: -
?
remazol brilliant blue R-carboxymethylcellulose + H2O
?
-
Substrates: -
Products: -
?
remazol brilliant blue R-carboxymethylcellulose + H2O
?
-
Substrates: -
Products: -
?
remazol brilliant blue R-carboxymethylcellulose + H2O
?
-
Substrates: -
Products: -
?
additional information
?
-
-
Substrates: no activity with cellotriose and 4-methylumbelliferyl beta-D-glucopyranoside
Products: -
?
additional information
?
-
-
Substrates: the enzyme is specific for internal glycosidic bonds
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows negligible activity with crystalline substrate such as Avicel and filter paper
Products: -
?
additional information
?
-
-
Substrates: no activity with 2-nitrophenyl beta -D-galactopyranoside
Products: -
?
additional information
?
-
-
Substrates: no activity with 2-nitrophenyl beta -D-galactopyranoside
Products: -
?
additional information
?
-
-
Substrates: no substrates: cellobiose, 4-nitrophenyl-beta-D-glucopyranoside
Products: -
?
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(carboxymethyl)cellulose + H2O
(carboxymethyl)cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
(carboxymethyl)cellulose + H2O
?
(carboxymethyl)cellulose + H2O
(carboxymethyl)cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
-
Substrates: -
Products: -
?
(carboxymethyl)cellulose + H2O
(carboxymethyl)cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
-
Substrates: specific substrate
Products: -
?
(carboxymethyl)cellulose + H2O
(carboxymethyl)cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
-
Substrates: specific substrate
Products: -
?
(carboxymethyl)cellulose + H2O
(carboxymethyl)cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
-
Substrates: specific substrate
Products: -
?
(carboxymethyl)cellulose + H2O
?
-
Substrates: -
Products: -
?
(carboxymethyl)cellulose + H2O
?
-
Substrates: -
Products: -
?
(carboxymethyl)cellulose + H2O
?
-
Substrates: -
Products: -
?
(carboxymethyl)cellulose + H2O
?
-
Substrates: -
Products: -
?
(carboxymethyl)cellulose + H2O
?
-
Substrates: -
Products: -
?
(carboxymethyl)cellulose + H2O
?
-
Substrates: -
Products: -
?
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0.6 - 16.58
carboxymethyl cellulose
-
0.6
carboxymethyl cellulose
wild-type, pH 5.5, 60°C, calculated as amounts of reducing equivalents
-
0.68
carboxymethyl cellulose
mutant D468E, pH 5.5, 60°C, calculated as amounts of reducing equivalents
-
0.68
carboxymethyl cellulose
mutant D471V, pH 5.5, 60°C
-
0.72
carboxymethyl cellulose
mutant D471A, pH 5.5, 60°C, calculated as amounts of reducing equivalents
-
0.92
carboxymethyl cellulose
mutant D471E, pH 5.5, 60°C, calculated as amounts of reducing equivalents
-
1.31
carboxymethyl cellulose
mutant D468V, pH 5.5, 60°C, calculated as amounts of reducing equivalents
-
1.43
carboxymethyl cellulose
mutant D468A, pH 5.5, 60°C, calculated as amounts of reducing equivalents
-
1.43
carboxymethyl cellulose
mutant D469A, pH 5.5, 60°C, calculated as amounts of reducing equivalents
-
1.95
carboxymethyl cellulose
mutant F16S/Y95F, pH 5.0, 70°C
-
3.38
carboxymethyl cellulose
mutant D469V, pH 5.5, 60°C, calculated as amounts of reducing equivalents
-
3.98
carboxymethyl cellulose
wild-type, pH 5.0, 70°C
-
5.01
carboxymethyl cellulose
mutant D469E, pH 5.5, 60°C, calculated as amounts of reducing equivalents
-
7.98
carboxymethyl cellulose
mutant F16S, pH 5.0, 70°C
-
16.58
carboxymethyl cellulose
mutant Y95F, pH 5.0, 70°C
-
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D468A
calcium binding-site mutant, shows increased activity compared with the wild type with 0 mM or 10 mM Ca2+ added. The mutation triggers a conformational change similar to that induced by Ca2+ in the wild type. Mutant displays an increase in melting temperature by 5.9°C
D468E
calcium binding-site mutant, kinetic parameters similar to wild-type
D468V
calcium binding-site mutant, shows increased activity compared with the wild type with 0 mM or 10 mM Ca2+ added. Mutant displays an increase in melting temperature by 4.5°C
D469A
calcium binding-site mutant, results in decreased activity
D469V
calcium binding-site mutant, increase in kcat value
D471A
calcium binding-site mutant, results in decreased activity
D471E
calcium binding-site mutant, kinetic parameters similar to wild-type
D471V
calcium binding-site mutant, increase in km value
F16S
1.7fold increase in kcat and 1.5fold improvement in hydrolytic activity on cellulosic substrates, while maintaining thermostability
F16S/Y95F
60% reduction in catalytic efficiency
Y95F
4.0fold increase in kcat and 2.5fold improvement in hydrolytic activity on cellulosic substrates, while maintaining thermostability
F16S
-
1.7fold increase in kcat and 1.5fold improvement in hydrolytic activity on cellulosic substrates, while maintaining thermostability
-
F16S/Y95F
-
60% reduction in catalytic efficiency
-
Y95F
-
4.0fold increase in kcat and 2.5fold improvement in hydrolytic activity on cellulosic substrates, while maintaining thermostability
-
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Morana, A.; Esposito, A.; Maurelli, L.; Ruggiero, G.; Ionata, E.; Rossi, M.; La Cara, F.
A novel thermoacidophilic cellulase from Alicyclobacillus acidocaldarius
Protein Pept. Lett.
15
1017-1021
2008
Alicyclobacillus acidocaldarius, Alicyclobacillus acidocaldarius ATCC 27009, Alicyclobacillus acidocaldarius ATCC27009
brenda
Deka, D.; Jawed, M.; Goyal, A.
Purification and characterization of an alkaline cellulase produced by Bacillus subtilis (AS3)
Prep. Biochem. Biotechnol.
43
256-270
2013
Bacillus subtilis, Bacillus subtilis AS3
brenda
Wang, H.J.; Hsiao, Y.Y.; Chen, Y.P.; Ma, T.Y.; Tseng, C.P.
Polarity alteration of a calcium site induces a hydrophobic interaction network and enhances Cel9A endoglucanase thermostability
Appl. Environ. Microbiol.
82
1662-1674
2016
Alicyclobacillus acidocaldarius (Q9AJS0)
brenda
Bhat, S.; Goodenough, P.W.; Bhat, M.K.; Owen, E.
Isolation of four major subunits from Clostridium thermocellum cellulosome and their synergism in the hydrolysis of crystalline cellulose
Int. J. Biol. Macromol.
16
335-342
1994
Acetivibrio thermocellus
brenda
Kawamori, M.; Takayama, K.; Takasawa, S.
Production of cellulases by a thermophilic fungus, Thermoascus aurantiacus a-131f
Agric. Biol. Chem.
51
647-654
1987
Thermoascus aurantiacus, Thermoascus aurantiacus a-131f
-
brenda
Srikrishnan, S.; Randall, A.; Baldi, P.; Da Silva, N.A.
Rationally selected single-site mutants of the Thermoascus aurantiacus endoglucanase increase hydrolytic activity on cellulosic substrates
Biotechnol. Bioeng.
109
1595-1599
2012
Thermoascus aurantiacus (Q96UI5), Thermoascus aurantiacus IFO 9748 (Q96UI5)
brenda
Saraihom, S.; Kobayashi, D.; Lotrakul, P.; Prasongsuk, S.; Eveleigh, D.; Punnapayak, H.
First report of a tropical Lysobacter enzymogenes producing bifunctional endoglucanase activity towards carboxymethylcellulose and chitosan
Ann. Microbiol.
66
907-919
2016
Lysobacter enzymogenes, Lysobacter enzymogenes 521
-
brenda
Kim, M.; Kang, D.; Lee, J.
Construction of a recombinant Escherichia coli JM109/A-68 for production of carboxymethylcellulase and comparison of its production with its wild type, Bacillus velezensis A-68 in a pilot-scale bioreactor
Biotechnol. Bioprocess Eng.
21
601-611
2016
Bacillus velezensis, Bacillus velezensis A-68
-
brenda
Kim, M.; Gao, W.; Chung, C.; Lee, J.
Comparison of optimal conditions for mass production of carboxymethylcellulase by Escherichia coli JM109/A-68 with other recombinants in pilot-scale bioreactor
Biotechnol. Bioprocess Eng.
22
142-149
2017
Bacillus velezensis, Bacillus velezensis A-68
-
brenda
Abada, E.; Al-Fifi, Z.; Osman, M.
Bioethanol production with carboxymethylcellulase of Pseudomonas poae using castor bean (Ricinus communis L.) cake
Saudi J. Biol. Sci.
26
866-871
2018
Pseudomonas poae, Pseudomonas poae AB3
-
brenda
Duman, Y.; Yuzugullu Karakus, Y.; Sertel, A.; Polat, F.
Production, purification, and characterization of a thermo-alkali stable and metal-tolerant carboxymethylcellulase from newly isolated Bacillus methylotrophicus Y37
Turk. J. Chem.
40
802-815
2016
Bacillus velezensis, Bacillus velezensis Y37
-
brenda
Kang, D.U.; Lee, Y.S.; Lee, J.W.
Construction of Escherichia coli BL21/A-53 producing histidine-tagged carboxymethylcellulase and comparison of its characteristics with CMCase without histidine-tag
Prep. Biochem. Biotechnol.
49
167-175
2019
Escherichia coli
brenda