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Information on EC 3.2.1.4 - cellulase and Organism(s) Ruminiclostridium cellulolyticum and UniProt Accession P37698

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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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Ruminiclostridium cellulolyticum
UNIPROT: P37698
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The taxonomic range for the selected organisms is: Ruminiclostridium cellulolyticum
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
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 Cel9M
-
shortest variant of family 9 cellulases which contains only the catalytic module to interact with the substrate
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
-
-
-
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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
-
-
-
-
FI-CMCASE
-
-
-
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pancellase SS
-
-
-
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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
avicel + H2O
?
show the reaction diagram
bacterial microcrystalline cellulose + H2O
?
show the reaction diagram
weak activity
-
-
?
bacterial microcrystalline cellulose + H2O
cellotetraose
show the reaction diagram
-
weak activity
83% cellotetraose + 11% cellotriose + 4% cellobiose
-
?
carboxymethylcellulose + H2O
?
show the reaction diagram
cellopentaose + H2O
cellotetraose + glucose
show the reaction diagram
-
-
-
-
?
lichenan + H2O
?
show the reaction diagram
weak activity
-
-
?
p-nitrophenyl-cellobiose + H2O
?
show the reaction diagram
-
-
-
?
phosphoric acid-swollen cellulose + H2O
?
show the reaction diagram
xylan + H2O
?
show the reaction diagram
weak activity
-
-
?
additional information
?
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
activity with phosphoric acid-swollen cellulose
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
activity with phosphoric acid-swollen cellulose
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54618
-
x * 54618, the enzyme contains a catalytic domain belonging to family 9 and a dockering domain, it is a component of the cellulosome, calculation from nucleotide sequence
93800
x * 93800, calculation from nucleotide sequence
94000
x * 94000, recombinant enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
vapor diffusion and microseeding techniques, crystallization of complexes between hemithio-cello-deca and dodecaoses and the inactive mutants E44Q and E55Q of cellulase Cel48F
catalytic domain of CelF cellulase in the presence of a newly synthesized cellulase inhibitor
-
catalytic domain of endoglucanase A
-
crystal strcuture of free native enzyme and its complex with cellobiose solved to 1.8 A and 2.0 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E44Q
inactive mutant enzyme
E55Q
inactive mutant enzyme
E410Q
-
mutation totally inactivates carboxymethyl cellulase activity of the protein
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
entire and truncated enzyme form
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli
-
expression of truncated enzyme in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
recombination of the catalytic domains of three glycoside hydrolase family 48 bacterial cellulases (Cel48), i.e. Clostridium cellulolyticum CelF, Clostridium stercorarium CelY, and Clostridium thermocellum CelS, to create a diverse library of Cel48 enzymes with an average of 106 mutations from the closest native enzyme. The library is based on the Clostridium thermocellum CelS architecture, which consists of a 70-kDa catalytic domain connected to the organism's respective dockerin domain. Large variations in properties such as the functional temperature range, stability, and specific activity on crystalline cellulose are found. Functional status and stability are predictable from simple linear models of the sequence-property data. Recombined protein fragments contribute additively to these properties in a given chimera
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ducros, V.; Czjzek, M.; Belaich, A.; Gaudin, C.; Fierobe, H.P.; Belaich, J.P.; Davies, G.J.
Crystal structure of the catalytic domain of a bacterial cellulase belonging to family 5
Structure
15
939-949
1995
Ruminiclostridium cellulolyticum
Manually annotated by BRENDA team
Reverbel-Leroy, C.; Parsiegla, G.; Moreau, V.; Juy, M.; Tardif, C.; Driguez, H.; Belaich, J.P.; Haser, R.
Crystallization of the catalytic domain of Clostridium cellulolyticum CelF cellulase in the presence of a newly synthesized cellulase inhibitor
Acta Crystallogr. Sect. D
54
114-118
1998
Ruminiclostridium cellulolyticum
Manually annotated by BRENDA team
Parsiegla, G.; Belaich, A.; Belaich, J.P.; Haser, R.
Crystal structure of the cellulase Cel9M enlightens structure/function relationships of the variable catalytic modules in glycoside hydrolases
Biochemistry
41
11134-11142
2002
Ruminiclostridium cellulolyticum
Manually annotated by BRENDA team
Gaudin, C.; Belaich, A.; Champ, S.; Belaich, J.P.
CelE, a multidomain cellulase from Clostridium cellulolyticum: a key enzyme in the cellulosome?
J. Bacteriol.
182
1910-1915
2000
Ruminiclostridium cellulolyticum (Q46002), Ruminiclostridium cellulolyticum
Manually annotated by BRENDA team
Belaich, A.; Parsiegla, G.; Gal, L.; Villard, C.; Haser, R.; Belaich, J.P.
Cel9M, a new family 9 cellulase of the Clostridium cellulolyticum cellulosome
J. Bacteriol.
184
1378-1384
2002
Ruminiclostridium cellulolyticum
Manually annotated by BRENDA team
Parsiegla, G.; Reverbel, C.; Tardif, C.; Driguez, H.; Haser, R.
Structures of mutants of cellulase Cel48F of Clostridium cellulolyticum in complex with long hemithiocellooligosaccharides give rise to a new view of the substrate pathway during processive action
J. Mol. Biol.
375
499-510
2008
Ruminiclostridium cellulolyticum (P37698), Ruminiclostridium cellulolyticum
Manually annotated by BRENDA team
Smith, M.A.; Rentmeister, A.; Snow, C.D.; Wu, T.; Farrow, M.F.; Mingardon, F.; Arnold, F.H.
A diverse set of family 48 bacterial glycoside hydrolase cellulases created by structure-guided recombination
FEBS J.
279
4453-4465
2012
Ruminiclostridium cellulolyticum (P37698), Ruminiclostridium cellulolyticum DSM 5812 (P37698)
Manually annotated by BRENDA team