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Information on EC 3.2.1.4 - cellulase and Organism(s) Caldicellulosiruptor saccharolyticus and UniProt Accession P22534

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EC Tree
     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.4 cellulase
IUBMB Comments
Will also hydrolyse 1,4-linkages in beta-D-glucans also containing 1,3-linkages.
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This record set is specific for:
Caldicellulosiruptor saccharolyticus
UNIPROT: P22534
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Word Map
The taxonomic range for the selected organisms is: Caldicellulosiruptor saccharolyticus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
cellulase, cel7a, cellobiohydrolase i, cel5a, cel6a, avicelase, endocellulase, celluclast, cel7b, cbhii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.5 cellulase
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-
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Abscission cellulase
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-
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alkali cellulase
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-
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Alkaline cellulase
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-
-
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avicelase
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-
-
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beta-1,4-endoglucan hydrolase
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-
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beta-1,4-glucanase
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-
-
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Carboxymethyl cellulase
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-
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Carboxymethyl-cellulase
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-
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carboxymethylcellulase
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CEL1
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cellobiohydrolase
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celluase A
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-
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celludextrinase
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-
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Cellulase
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cellulase A 3
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-
-
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Cellulase E1
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Cellulase E2
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-
-
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Cellulase E4
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-
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Cellulase E5
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-
-
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Cellulase SS
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-
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Cellulase V1
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cellulosin AP
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CMCase
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CX-cellulase
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EG1
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-
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EG2
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-
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EG3
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-
-
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EGA
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-
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EGB
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EGC
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EGCCA
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EGCCC
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EGCCD
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EGCCF
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EGCCG
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EGD
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EGE
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EGF
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EGH
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EGI
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EGIV
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EGM
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EGSS
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EGX
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EGY
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EGZ
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endo-1,4-beta-D-glucanase
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endo-1,4-beta-glucanase
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endo-1,4-beta-glucanase E1
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endo-1,4-beta-glucanase V1
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endocellulase E1
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endoglucanase
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endoglucanase D
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FI-CMCASE
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pancellase SS
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Thermoactive cellulase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
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-
-
-
PATHWAY SOURCE
PATHWAYS
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-
SYSTEMATIC NAME
IUBMB Comments
4-beta-D-glucan 4-glucanohydrolase
Will also hydrolyse 1,4-linkages in beta-D-glucans also containing 1,3-linkages.
CAS REGISTRY NUMBER
COMMENTARY hide
9012-54-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
carboxymethylcellulose + H2O
?
show the reaction diagram
-
-
-
?
cellulose + H2O
D-glucose + ?
show the reaction diagram
-
enzyme is able to degrade crystalline cellulose to glucose
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
-
-
?
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GUNA_CALSA
1742
0
193697
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Thermotoga sp. strain RQ2 and Escherichia coli
expression in Escherichia coli
expression in Thermotoga sp. strain RQ2 and Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team