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Information on EC 3.2.1.203 - carboxymethylcellulase
for references in articles please use BRENDA:EC3.2.1.203
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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
3.2.1.203 carboxymethylcellulase
IUBMB Comments
The enzyme from the acidophilic bacterium Alicyclobacillus acidocaldarius is an endo-cleaving hydrolase that cleaves β(1→4)-linked residues. However, it is specific for (carboxymethyl)cellulose and does not act on cellulosic substrates such as avicel.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 3.2.1.203
- cmcase
- xylanase
- rumen
-
cellulolytic
- carboxymethylcellulose
- straw
- cellulases
- avicel
- avicelase
- endoglucanase
-
fibrolytic
- ruminococcus
- flavefaciens
- succinogenes
- fibrobacter
- cellobiase
- cellotriose
- cellotetraose
-
cellulosome
-
3.2.1.4
- neocallimastix
Reaction Schemes
showEndohydrolysis of (1->4)-beta-D-glucosidic linkages in (carboxymethyl)cellulose.
Synonyms
carboxymethylcellulase, thermoacidophilic cellulase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CelG
CMCase
EG1
thermoacidophilic cellulase
CMCase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Endohydrolysis of (1->4)-beta-D-glucosidic linkages in (carboxymethyl)cellulose.
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
4-beta-D-(carboxymethyl)glucan 4-(carboxymethyl)glucanohydrolase
The enzyme from the acidophilic bacterium Alicyclobacillus acidocaldarius is an endo-cleaving hydrolase that cleaves beta(1->4)-linked residues. However, it is specific for (carboxymethyl)cellulose and does not act on cellulosic substrates such as avicel.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(carboxymethyl)cellulose + H2O
(carboxymethyl)cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
4-methylumbelliferyl cellopentaoside + H2O
cellotetraose + 4-methylumbelliferyl beta-D-glucopyranoside
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl cellotetraoside + H2O
cellotriose + 4-methylumbelliferyl beta-D-glucopyranoside
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl cellotrioside + H2O
cellobiose + 4-methylumbelliferyl beta-D-glucopyranoside
-
Substrates: -
Products: -
Products: -
?
carboxymethyl cellulose + H2O
carboxymethyl cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
pullulan + H2O
?
-
Substrates: 7.2% of the activity with (carboxymethyl)cellulose
Products: -
Products: -
?
xylan + H2O
?
-
Substrates: 6.8% of the activity with (carboxymethyl)cellulose
Products: -
Products: -
?
(carboxymethyl)cellulose + H2O
(carboxymethyl)cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
-
Substrates: -
Products: -
Products: -
?
(carboxymethyl)cellulose + H2O
(carboxymethyl)cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
-
Substrates: specific substrate
Products: -
Products: -
?
(carboxymethyl)cellulose + H2O
(carboxymethyl)cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
-
Substrates: specific substrate
Products: -
Products: -
?
(carboxymethyl)cellulose + H2O
(carboxymethyl)cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
-
Substrates: specific substrate
Products: -
Products: -
?
(carboxymethyl)cellulose + H2O
(carboxymethyl)cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
-
Substrates: -
Products: -
Products: -
?
(carboxymethyl)cellulose + H2O
?
-
Substrates: -
Products: -
Products: -
?
avicel + H2O
?
-
Substrates: 29.8% of the activity with (carboxymethyl)cellulose
Products: -
Products: -
?
carboxymethyl cellulose + H2O
?
Substrates: -
Products: -
Products: -
?
carboxymethyl cellulose + H2O
carboxymethyl cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
Substrates: -
Products: -
Products: -
?
carboxymethyl cellulose + H2O
carboxymethyl cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
Substrates: -
Products: -
Products: -
?
carboxymethylcellulose + H2O
?
-
Substrates: enzyme is specific for carboxymethylcellulose
Products: -
Products: -
?
carboxymethylcellulose + H2O
?
-
Substrates: enzyme is specific for carboxymethylcellulose
Products: -
Products: -
?
carboxymethylcellulose + H2O
?
-
Substrates: enzyme is specific for carboxymethylcellulose
Products: -
Products: -
?
filter paper + H2O
?
-
Substrates: 19.5% of the activity with (carboxymethyl)cellulose
Products: -
Products: -
?
remazol brilliant blue R-carboxymethylcellulose + H2O
?
-
Substrates: -
Products: -
Products: -
?
remazol brilliant blue R-carboxymethylcellulose + H2O
?
-
Substrates: -
Products: -
Products: -
?
remazol brilliant blue R-carboxymethylcellulose + H2O
?
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is specific for internal glycosidic bonds
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with cellotriose and 4-methylumbelliferyl beta-D-glucopyranoside
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme shows negligible activity with crystalline substrate such as Avicel and filter paper
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 2-nitrophenyl beta -D-galactopyranoside
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity with 2-nitrophenyl beta -D-galactopyranoside
Products: -
Products: -
?
additional information
?
-
-
Substrates: no substrates: cellobiose, 4-nitrophenyl-beta-D-glucopyranoside
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(carboxymethyl)cellulose + H2O
(carboxymethyl)cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
(carboxymethyl)cellulose + H2O
(carboxymethyl)cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
-
Substrates: -
Products: -
Products: -
?
(carboxymethyl)cellulose + H2O
(carboxymethyl)cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
-
Substrates: specific substrate
Products: -
Products: -
?
(carboxymethyl)cellulose + H2O
(carboxymethyl)cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
-
Substrates: specific substrate
Products: -
Products: -
?
(carboxymethyl)cellulose + H2O
(carboxymethyl)cellulose with endohydrolysed (1->4)-beta-D-glucosidic linkages
-
Substrates: specific substrate
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Ca2+
sequence contains a calcium-binding site (Ser465 to Val470) near the catalytic cleft. Ca2+ induces hydrophobic interactions between the calcium site and its nearby region by driving a conformational change. Calcium-binding site mutants D468A and D468V show increased activity compared with the wild type with 0 mM or 10 mM Ca2+ added
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Infections
Action of selenium against Sclerotinia sclerotiorum: Damaging membrane system and interfering with metabolism.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
(carboxymethyl)cellulose
-
Km value 9.3 g/l, pH 5.0, 50°C
additional information
carboxymethyl cellulose
Km value of wild-type, 29.95 mg/ml, mutant D468A, 46.8 mg/ml, mutant D469V 204.9 mg/ml, pH 5.5, 60°C
-
additional information
carboxymethyl cellulose
Km value is 0.14 mg/ml, 0.17 mg/ml, 0.13 mg/ml, and 0.17 mg/ml for wild-type, mutant F16S, mutant Y95F and mutant F16S/Y95F, respectively
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
3.38
carboxymethyl cellulose
mutant D469V, pH 5.5, 60°C, calculated as amounts of reducing equivalents
-
5.01
carboxymethyl cellulose
mutant D469E, pH 5.5, 60°C, calculated as amounts of reducing equivalents
-
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
234
mutant D468V, presence of 10 mM Ca2+, pH 5.5, 60°C
282
mutant D468A, presence of 10 mM Ca2+, pH 5.5, 60°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 9
-
pH 5.0: about 50% of maximal activity, pH 9.0: about 60% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
70
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 40
-
25°C: about 60% of maximal activity, 40°C: about 60% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
optimization of cellulase production by Aspergillus fumigatus on Stipa tenacissima biomass
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q9AJS0_ALIAC
537
0
58963
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
88000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure reveals that mutation D468A triggers a conformational change similar to that induced by Ca2+ in the wild type and develops a hydrophobic interaction network between the calcium site and the neighboring hydrophobic region (Ala113 to Ala117)
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
-
Y95F
-
4.0fold increase in kcat and 2.5fold improvement in hydrolytic activity on cellulosic substrates, while maintaining thermostability
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
-
after incubation at 4°C and pH 10 for 3 h the enzyme retains 82% of the original activity, while this is 74% for incubation at 50°C and pH 10 for 1 h
6 - 12
-
the enzyme is stable in the pH range 6-10 and retains 70% activity at pH 12.0
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 60
-
the enzyme is stable in temperature range of 20°C to 45°C and retains more than 50% activity at 60°C for 30 min
50
55 - 65
-
more than 90% of the original enzyme activity is maintained at temperatures ranging from 55 to 65°C after 45 min. Above 65°C, the enzyme activity is moderately lost with 65% remaining
70
wild-type and mutants F16S and Y95F, 2 h, more than 80% residual activity
50
wild-type and mutants F16S and Y95F, active for more than 12 h
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, HiTrap phenyl column chromatography, and HiTrap HP column chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli KACC 91335P. Production of CMCase by Escherichia coli KACC 91335P in a pilot-scale bioreactor is enhanced by shifting the optimal conditions of the aeration rate and agitation speed from the cell growth to its production of CMCase
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is markedly induced by growth on amorphous polysaccharides such as alkali-treated bagasse and xylan
expression is markedly induced by growth on amorphous polysaccharides such as alkali-treated bagasse and xylan
-
expression is markedly induced by growth on amorphous polysaccharides such as alkali-treated bagasse and xylan
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biofuel production
biofuel production
-
bioethanol production with carboxymethylcellulase of Pseudomonas poae using castor bean (Ricinus communis L.) cake
biofuel production
Pseudomonas poae AB3
-
bioethanol production with carboxymethylcellulase of Pseudomonas poae using castor bean (Ricinus communis L.) cake
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
de Oliveira Junior, S.D.; Dos Santos Gouvea, P.R.; de Aguiar, L.V.B.; Pessoa, V.A.; Dos Santos Cruz Costa, C.L.; Chevreuil, L.R.; Dedo BritoNascimento, L.B.; Dos Santos, E.S.; Sales-Campos, C.
Production of lignocellulolytic enzymes and phenolic compounds by Lentinus strigosus from the amazon using solid-state fermentation (SSF) of guarana (Paullinia cupana) residue
Appl. Biochem. Biotechnol.
194
2882-2900
2022
Panus neostrigosus
brenda
Park, C.; Lee, J.; Li, J.; Lee, J.
Enhanced production of carboxymethylcellulase by recombinant Escherichia coli strain from rice bran with shifts in optimal conditions of aeration rate and agitation speed on a pilot-scale
Appl. Sci. (Basel)
9
4083
2019
Bacillus velezensis, Bacillus velezensis A-68
-
brenda
Gares, M.; Benaissa, A.; Hiligsmann, S.; Cherfia, R.; Flahaut, S.; Alloun, W.; Djelid, H.; Chaoua, S.; Kacem Chaouche, N.
Box-Behnken design optimization of xylanase and cellulase production by Aspergillus fumigatus on Stipa tenacissima biomass
Mycologia
115
437-455
2023
Aspergillus fumigatus
brenda
Santos, A.D.S.; Pereira, G.M.; Mazotto de Almeida, A.M.; Santos, R.R.D.; Terzi, S.D.C.; Pacheco, T.F.; Beatriz Vermelho, A.; Correa Cabral, L.M.; Couri, S.; Damaso, M.C.T.
Production, concentration and partial characterization of an enzymatic extract produced by an Aspergillus niger mutant in solid state fermentation
Prep. Biochem. Biotechnol.
52
1109-1118
2022
Aspergillus niger, Aspergillus niger 3T5B8
brenda
EXTERNAL LINKS (specific for EC-Number 3.2.1.203)
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