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Information on EC 3.2.1.4 - cellulase and Organism(s) Cryptopygus antarcticus and UniProt Accession D3GDK4

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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:
Cryptopygus antarcticus
UNIPROT: D3GDK4
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Word Map
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The taxonomic range for the selected organisms is: Cryptopygus antarcticus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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cellohexaose
+
H2O
=
2
cellotriose
+
=
2
Synonyms
cellulase, cel7a, cellobiohydrolase i, cel5a, cel6a, avicelase, endocellulase, celluclast, cel7b, cbhii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.5 cellulase
-
-
-
-
Abscission cellulase
-
-
-
-
alkali cellulase
-
-
-
-
Alkaline cellulase
-
-
-
-
avicelase
-
-
-
-
beta-1,4-endoglucan hydrolase
-
-
-
-
beta-1,4-glucanase
-
-
-
-
Carboxymethyl cellulase
-
-
-
-
Carboxymethyl-cellulase
-
-
-
-
carboxymethylcellulase
-
-
-
-
CEL1
-
-
-
-
cellobiohydrolase
-
-
-
-
celluase A
-
-
-
-
celludextrinase
-
-
-
-
Cellulase
-
-
-
-
cellulase A 3
-
-
-
-
Cellulase E1
-
-
-
-
Cellulase E2
-
-
-
-
Cellulase E4
-
-
-
-
Cellulase E5
-
-
-
-
Cellulase SS
-
-
-
-
Cellulase V1
-
-
-
-
cellulosin AP
-
-
-
-
CMCase
-
-
-
-
CX-cellulase
-
-
-
-
EG1
-
-
-
-
EG2
-
-
-
-
EG3
-
-
-
-
EGA
-
-
-
-
EGB
-
-
-
-
EGC
-
-
-
-
EGCCA
-
-
-
-
EGCCC
-
-
-
-
EGCCD
-
-
-
-
EGCCF
-
-
-
-
EGCCG
-
-
-
-
EGD
-
-
-
-
EGE
-
-
-
-
EGF
-
-
-
-
EGH
-
-
-
-
EGI
-
-
-
-
EGIV
-
-
-
-
EGM
-
-
-
-
EGSS
-
-
-
-
EGX
-
-
-
-
EGY
-
-
-
-
EGZ
-
-
-
-
endo-1,4-beta-D-glucanase
-
-
-
-
endo-1,4-beta-glucanase
-
-
-
-
endo-1,4-beta-glucanase E1
-
-
-
-
endo-1,4-beta-glucanase V1
-
-
-
-
endocellulase E1
-
-
-
-
endoglucanase
-
-
-
-
endoglucanase D
-
-
-
-
FI-CMCASE
-
-
-
-
pancellase SS
-
-
-
-
Thermoactive cellulase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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
barley beta-glucan + H2O
?
show the reaction diagram
-
-
-
?
carboxymethylcellulose + H2O
cellobiose + cellotriose + cellotetraose
show the reaction diagram
-
-
-
?
cellohexaose + H2O
cellotetraose + cellobiose
show the reaction diagram
-
-
-
?
cellopentaose + H2O
cellotriose + cellobiose
show the reaction diagram
-
-
-
?
cellotetraose + H2O
2 cellobiose
show the reaction diagram
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
?
additional information
?
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
13.9
substrate barley beta-glucan, pH 3.5, 40°C
20.5
substrate lichenan, pH 3.5, 40°C
35.8
substrate carboxymethylcellulose, pH 3.5, 40°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2 - 7
more than 60% of maximum activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 10
60% of maximum activity
80
40% of maximum activity
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?
GUN_CRYAT
225
0
23795
Swiss-Prot
Secretory Pathway (Reliability: 2)
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
molecular modeling of structure
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
8 h, no loss of activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
degradation
under acidic conditions at 50°C, the enzyme is effective in digesting the green algae Ulva pertusa
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Song, J.M.; Hong, S.K.; An, Y.J.; Kang, M.H.; Hong, K.H.; Lee, Y.H.; Cha, S.S.
Genetic and structural characterization of a thermo-tolerant, cold-active, and acidic endo-beta-1,4-glucanase from Antarctic springtail, Cryptopygus antarcticus
J. Agric. Food Chem.
65
1630-1640
2017
Cryptopygus antarcticus (D3GDK4), Cryptopygus antarcticus
Manually annotated by BRENDA team