We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments Will also hydrolyse 1,4-linkages in beta-D-glucans also containing 1,3-linkages.
The taxonomic range for the selected organisms is: Caldicellulosiruptor saccharolyticus The enzyme appears in selected viruses and cellular organisms
Synonyms
cellulase, cel7a, cellobiohydrolase i, cel5a, cel6a, avicelase, endocellulase, celluclast, cel7b, cbhii,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Abscission cellulase
-
-
-
-
Alkaline cellulase
-
-
-
-
beta-1,4-endoglucan hydrolase
-
-
-
-
beta-1,4-glucanase
-
-
-
-
Carboxymethyl cellulase
-
-
-
-
Carboxymethyl-cellulase
-
-
-
-
carboxymethylcellulase
-
-
-
-
cellobiohydrolase
-
-
-
-
endo-1,4-beta-D-glucanase
-
-
-
-
endo-1,4-beta-glucanase
-
-
-
-
endo-1,4-beta-glucanase E1
-
-
-
-
endo-1,4-beta-glucanase V1
-
-
-
-
Thermoactive cellulase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
hydrolysis of O-glycosyl bond
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4-beta-D-glucan 4-glucanohydrolase
Will also hydrolyse 1,4-linkages in beta-D-glucans also containing 1,3-linkages.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
carboxymethylcellulose + H2O
?
-
-
-
?
cellulose + H2O
D-glucose + ?
-
enzyme is able to degrade crystalline cellulose to glucose
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GUNA_CALSA
1742
0
193697
Swiss-Prot
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
the exoglucanase activity is located in the amino-terminal domain of the enzyme and the endoglucanase activity is located in the carboxy-terminal domain
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
additional information
construction of deletion mutants expressing solely the carboxyterminal domain containing the endoglucanase activity. Temperature optimum and stability of the deletion mutants are the same as wild-type
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
70
-
half-life: 7.5 h
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expression in Thermotoga sp. strain RQ2 and Escherichia coli
expression in Escherichia coli
expression in Thermotoga sp. strain RQ2 and Escherichia coli
expression in Escherichia coli
-
expression in Escherichia coli
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
synthesis
expression of enzyme in Escherichia coli and Thermotoga sp. after fusion to the signal peptides of TM1840 (amyA) or TM0070 (xynB). Expressed in Escherichia coli and Thermotoga sp. renders the hosts with increased endoglucanase activities. In Escherichia coli, the recombinant enzymes are mainly bound to the bacterial cells, whereas in Thermotoga sp., about half of the enzyme activities are observed in the culture supernatants. However, the cellulase activities are lost in Thermotoga sp. after three consecutive transfers
synthesis
expression of enzyme in Escherichia coli and Thermotoga sp. after fusion to the signal peptides of TM1840 (amyA) or TM0070 (xynB). Expressed in Escherichia coli and Thermotoga sp. renders the hosts with increased endo- and exoglucanase activities. In Escherichia coli, the recombinant enzymes are mainly bound to the bacterial cells, whereas in Thermotoga sp., about half of the enzyme activities are observed in the culture supernatants. However, the cellulase activities are lost in Thermotoga sp. after three consecutive transfers
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Patchett, M.L.; Neal, T.L.; Schofield, L.R.; Strange, R.C.; Daniel, R.M.; Morgan, H.W.
Heat treatment purification of thermostable cellulase and hemicellulase enzymes expressed in E. coli
Enzyme Microb. Technol.
11
113-115
1989
Caldicellulosiruptor saccharolyticus
-
brenda
Saul, D.J.; Williams, L.C.; Grayling, R.A.; Chamley, L.W.; Love, D.R.; Bergquist, P.L.
celB, a gene coding for a bifunctional cellulase from the extreme thermophile "Caldocellum saccharolyticum"
Appl. Environ. Microbiol.
56
3117-3124
1990
Caldicellulosiruptor saccharolyticus (P10474)
brenda
Xu, H.; Han, D.; Xu, Z.
Expression of heterologous cellulases in Thermotoga sp. strain RQ2
Biomed Res. Int.
2015
304523
2015
Caldicellulosiruptor saccharolyticus (P10474), Caldicellulosiruptor saccharolyticus (P22534), Caldicellulosiruptor saccharolyticus
brenda
Transporter Classification Database (TCDB):
4.D.3.1.6