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Information on EC 3.2.1.4 - cellulase and Organism(s) Bacillus subtilis and UniProt Accession A8D0T0
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3.2.1.4 cellulaseIUBMB Comments
Will also hydrolyse 1,4-linkages in beta-D-glucans also containing 1,3-linkages.
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Word Map
- 3.2.1.4
- cellulose
- trichoderma
- biomass
- reesei
- xylanase
-
cellulolytic
-
saccharification
-
lignocellulosic
- cellobiose
- straw
- lignin
- polysaccharide
- aspergillus
- glycoside
- beta-glucosidase
- corn
-
biofuels
- pectinase
- xylan
- hemicellulose
- bagasse
- penicillium
- endoglucanases
-
bioethanol
- xylose
- amylase
- polygalacturonase
- sugarcane
-
carbohydrate-binding
-
feedstock
- viride
- glucans
- thermocellum
- bran
- carboxymethylcellulose
-
microcrystalline
- exoglucanase
-
cellulose-binding
- laccase
-
biorefinery
- rumen
- biotechnology
- analysis
-
novozyme
-
silage
- endoxylanase
-
compost
- industry
- textile industry
- food industry
- biofuel production
- agriculture
-
deconstruct
- xylobiose
- diagnostics
- harzianum
- degradation
- chrysosporium
- synthesis
- detergent
- environmental protection
- xyloglucans
The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
cellulase, cel7a, cellobiohydrolase i, cel5a, cel6a, avicelase, endocellulase, celluclast, cel7b, cbhii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
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
-
-
-
-
Cel5A
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
-
-
-
-
endo-beta-1,4-glucanase
endocellulase E1
-
-
-
-
endoglucanase
-
-
-
-
endoglucanase D
-
-
-
-
FI-CMCASE
-
-
-
-
pancellase SS
-
-
-
-
Thermoactive cellulase
-
-
-
-
Cellulase
-
-
-
-
CMCase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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
9012-54-8
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
filter paper + H2O
?
-
8.4% of the activity with carboxymethyl cellulose
-
-
?
carboxymethylcellulose + H2O
additional information
-
-
-
glucose + cellobiose
?
additional information
?
-
-
wild-type and mutant can not hydrolyze Avicel, laminarin and chitosan
-
-
?
additional information
?
-
-
the enzyme shows multisubstrate specificity, showing significantly higher activity with lichenan and beta-glucan and lower activity with laminarin, hydroxyethylcellulose, and steam exploded bagasse
-
-
?
additional information
?
-
-
no substrates: 4-nitrophenyl beta-D-glucopyranoside, cellulose
-
-
?
additional information
?
-
-
no substrates: alpha-glucan, cellobiose and xylan
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the enzyme shows multisubstrate specificity, showing significantly higher activity with lichenan and beta-glucan and lower activity with laminarin, hydroxyethylcellulose, and steam exploded bagasse
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
chimeric construct C10 has a Ca2+ ion bound to the backbone oxygen of G130 and to the side chains of D168, D170 and N171 with an average distance of 2.3 A
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
carboxymethylcellulose
-
binding of the cellulose-binding domain to avicel is inhibited by carboxymethylcellulose, but not by barley beta-glucan and glucose at concentration of 0.1% and 0.5%
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
carboxymethyl cellulose
-
Km value is 0.13 mg/ml, pH not specified in the publication, temperature not specified in the publication
-
additional information
carboxymethyl cellulose
-
Km-value 0.00176 mM, pH 9.0, 40°C
-
additional information
carboxymethylcellulose
-
Km of Egl330 and Egl499 are 1.73 x 10 mg/ml and 1.14 x 10 mg/ml, respectively. Vmax of Egl330 is 1.78fold higher than that of Egl499, increases from 284 U/mg to 786 U/mg. The catalytic efficiency (kcat/Km) of Egl330 is slightly higher than that of Egl499
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
437
carboxymethylcellulose
-
the turnover rate (kcat) of Egl330 increased by 78% compared to wild-type
-
additional information
additional information
-
kinetic analysis shows both the turnover rate (kcat) and the catalytic efficiency (kcat/Km) of Egl330 increased for the substrate carboxymethylcellulose compared to Egl499
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
2.82 U/ml for the native extracellular enzyme, 6.78-8.54 U/ml for the recombinant extracellular enzyme expressed in Escherichia coli strain BL21(DE3)
additional information
-
2.82 U/ml for the native extracellular enzyme, 6.78-8.54 U/ml for the recombinant extracellular enzyme expressed in Escherichia coli strain BL21(DE3)
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
60
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
enzyme activity is enhanced by carboxymethylcellulose, peptone, and yeast extract addition, medium with lichenan or beta-glucan shows 2.5 or 2.8fold higher activity, respectively, at same concentration as of carboxymethylcellulose, optimization of culture medium conditions for production of cellulase activity by Plackett-Burman design, detailed overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
cellulolytic enzymes, including endo-beta-1,4-glucanases, EC 3.2.1.4, exo-beta-1,4-glucanases, EC 3.2.1.91, and beta-glucosidases, EC 3.2.1.21, collectively known as cellulases, act in a synergistic manner to facilitate complete cleavage of the cellulose beta-1,4-glycosidic bonds to form glucose
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). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of chimera C10 in complex with crown ether. The structure of C10 adopts the same classical TIM barrel fold as the parental structures of CelA core and Cel5A. A Ca2+ ion is bound to the backbone oxygen of G130 and to the side chains of D168, D170 and N171 with an average distance of 2.3 A
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
I62T/L79I/A93T/S308P/I370V/L374P/M416V/F472I/I484V/W494R
-
S40 mutant, DNA shuffling. Higher hydrolytic activities than the wild-type enzyme
K120E/D272H/S283G/S308P/L374P
-
M1-23 mutant, random mutation. Higher hydrolytic activities than the wild-type enzyme
K120E/S283G/S308P/L374P
-
M1 mutant, random mutation. Higher hydrolytic activities than the wild-type enzyme, shows 1.25fold increase in activity
N39D/K120E/N175H/V255A/S308P/L386S/K398R
-
S75 mutant, DNA shuffling. Higher hydrolytic activities than the wild-type enzyme
T32I/N39D/K120E/S248G/S283G/S308P/R314G/I370N/L374P/N403D/N451D/S467N
-
S78 mutant, DNA shuffling. Higher hydrolytic activities than the wild-type enzyme
V74A/K120E/D272G/K337E/S355P/D459G/K479E/K482E/K491N
-
M44 mutant, random mutation. Higher hydrolytic activities than the wild-type enzyme, shows 1.56fold increase in activity
V74A/K120E/D272G/K337E/S355P/T449I/D459G/K479E/K482E/D488N/K491N
-
M44-11 mutant, random mutation. Higher hydrolytic activities than the wild-type enzyme
additional information
additional information
-
construction of chimeric enzymes between the Bacillus subtilis cellulase and an alkalophilic Bacillus cellulase
additional information
-
C-terminus truncation mutant Egl330, truncation of the cellulose binding domain, a great improvement in thermal stability is observed in Egl330
additional information
-
variants (M44-11, S75 and S78) show 2.03fold to 2.68fold increased activities toward sodium carboxymethyl cellulose
additional information
generation of a set of chimeric proteins derived from the recombination of Geobacillus sp. CelA and Bacillus subtilis 168 Cel5A. The designed chimeras are assembled from 16 gene fragments of the two parents. Chimeric cellulase C10 shows significantly higher activity (22%-43%) and higher thermostability compared to the parental enzymes. A 310 helix is responsible for the improved thermostability. In the presence of ionic calcium and crown ether, the chimeric C10 retains 40% residual activity even after heat treatment at 90°C
additional information
cellulolytic activity of Paenibacillus sp. strain CAA11 is significantly enhanced by expressing a heterologous endoglucanase 168Cel5 from Bacillus subtilis under both aerobic and anaerobic conditions. The strain harboring the 168cel5 gene reveals 2fold bigger halo zone on Congo-red plate and 1.75fold more aerobic cellulose utilization in liquid medium compared with the negative control. Under anaerobic conditions, the recombinant strain expressing 168Cel5 consumes 1.83fold more cellulose (5.10 g/l) and produces 5fold more ethanol (0.65 g/l) along with 5fold more total acids (1.6 g/l) compared with the control, resulting in 2.73fold higher yields
additional information
-
cellulolytic activity of Paenibacillus sp. strain CAA11 is significantly enhanced by expressing a heterologous endoglucanase 168Cel5 from Bacillus subtilis under both aerobic and anaerobic conditions. The strain harboring the 168cel5 gene reveals 2fold bigger halo zone on Congo-red plate and 1.75fold more aerobic cellulose utilization in liquid medium compared with the negative control. Under anaerobic conditions, the recombinant strain expressing 168Cel5 consumes 1.83fold more cellulose (5.10 g/l) and produces 5fold more ethanol (0.65 g/l) along with 5fold more total acids (1.6 g/l) compared with the control, resulting in 2.73fold higher yields
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
75
CelDR retains 70% of its maximum activity at 75°C after incubation for 30 min
65
80
80
-
M44-11 mutant shows higher stability than others and retains more than 50% of its activity after incubation at 80°C for 1 h
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
chimeric enzymes between the Bacillus subtilis cellulase and an alkalophilic Bacillus cellulase, expression in Escherichia coli
-
gene 168cel5 or eglS, recombinant expression of the enzyme, in an expression construct comprising DNA sequences encoding P43 promoter, signal peptide of Bacillus subtilis nprB, and mature Bacillus subtilis strain 168 Cel5 residues 30-499, in Paenibacillus sp. strain CAA11
gene celI15, DNA and amino acid sequence determination and analysis, functional expression in Escherichia coli strain BL21(DE3) as extracellular enzyme, subcloning in Escherichia coli strain JM109
gene CelL15, DNA and amino acid sequence determination and analysis, sequence comparisosns, expression in Escherichia coli strain BL21 (DE3)
gene CelL73, DNA and amino acid sequence determination and analysis, sequence comparisosns, expression in Escherichia coli strain BL21 (DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
construction of a pipeline based on Leishmania tarentolae cell-free system to characterize 30 putative thermostable endo-1,4-beta-glucanases and xylanases identified in public genomic databases. The system uses high-throughput assays for glucanase and xylanase activities that rely on solubilisation of labelled particulate substrates performed in multiwell plates
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Robson, L.M.; Chambliss, G.H.
Cellulases of bacterial origin
Enzyme Microb. Technol.
11
626-644
1989
Acetivibrio cellulolyticus, Bacillus subtilis, Bacillus sp. (in: Bacteria), Cellulomonas fimi, Acetivibrio thermocellus, Dickeya chrysanthemi, Ruminococcus albus, Thermobifida fusca, Thermomonospora curvata, Bacillus sp. (in: Bacteria) No. 1139, Bacillus sp. (in: Bacteria) N-4, Ruminococcus albus F40
-
Aa, K.; Flengsrud, R.; Lindahl, V.; Tronsmo, A.
Characterization of production and enzyme properties of an endo-beta-1,4-glucanase from Bacillus subtilis CK-2 isolated from compost soil
Antonie van Leeuwenhoek
66
319-326
1994
Bacillus subtilis, Bacillus subtilis CK-2
Au, K.S.; Chan, K.Y.
Purification and properties of the endo-1,4-beta-glucanase from Bacillus subtilis
J. Gen. Microbiol.
133
2155-2162
1987
Bacillus subtilis
-
Nakamura, A.; Fukumori, F.; Horinouchi, S.; Masaki, H.; Kudo,T.; Uozumi, T.; Horikoshi, K.; Beppu, T.
Construction and characterization of the chimeric enzymes between the Bacillus subtilis cellulase and an alkalophilic Bacillus cellulase
J. Biol. Chem.
266
1579-1583
1991
Bacillus subtilis, Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) N-4 (NK1)
Lin, L.; Meng, X.; Liu, P.; Hong, Y.; Wu, G.; Huang, X.; Li, C.; Dong, J.; Xiao, L.; Liu, Z.
Improved catalytic efficiency of endo-beta-1,4-glucanase from Bacillus subtilis BME-15 by directed evolution
Appl. Microbiol. Biotechnol.
82
671-679
2009
Bacillus subtilis, Bacillus subtilis BME-15
Wang, Y.; Yuan, H.; Wang, J.; Yu, Z.
Truncation of the cellulose binding domain improved thermal stability of endo-beta-1,4-glucanase from Bacillus subtilis JA18
Biores. Technol.
100
345-349
2009
Bacillus subtilis, Bacillus subtilis JA18
Li, W.; Zhang, W.W.; Yang, M.M.; Chen, Y.L.
Cloning of the thermostable cellulase gene from newly isolated Bacillus subtilis and its expression in Escherichia coli
Mol. Biotechnol.
40
195-201
2008
Bacillus subtilis (A8D0T0), Bacillus subtilis, Bacillus subtilis DR (A8D0T0)
Li, W.; Huan, X.; Zhou, Y.; Ma, Q.; Chen, Y.
Simultaneous cloning and expression of two cellulase genes from Bacillus subtilis newly isolated from Golden Takin (Budorcas taxicolor Bedfordi)
Biochem. Biophys. Res. Commun.
383
397-400
2009
Bacillus subtilis (C5I945), Bacillus subtilis (C5I946), Bacillus subtilis, Bacillus subtilis LN (C5I945), Bacillus subtilis LN (C5I946), Bacillus subtilis LN
Yang, D.; Weng, H.; Wang, M.; Xu, W.; Li, Y.; Yang, H.
Cloning and expression of a novel thermostable cellulase from newly isolated Bacillus subtilis strain I15
Mol. Biol. Rep.
37
1923-1929
2010
Bacillus subtilis (B7UAM4), Bacillus subtilis, Bacillus subtilis I15 (B7UAM4)
Deka, D.; Bhargavi, P.; Sharma, A.; Goyal, D.; Jawed, M.; Goyal, A.
Enhancement of cellulase activity from a new strain of Bacillus subtilis by medium optimization and analysis with various cellulosic substrates
Enzyme Res.
2011
151656
2011
Bacillus subtilis, Bacillus subtilis AS3
Rawat, R.; Tewari, L.
Purification and characterization of an acidothermophilic cellulase enzyme produced by Bacillus subtilis strain LFS3
Extremophiles
16
637-644
2012
Bacillus subtilis, Bacillus subtilis LFS3
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
Kowsalya, R.; Gurusamy, R.
Optimization, purification and characterization of thermostable cellulase from Bacillus subtilis KG10 isolated from virgin forest of Kovai Kutralam, Coimbatore, India
Int. J. Pharm. Bio. Sci.
5
B432-B448
2014
Bacillus subtilis, Bacillus subtilis KG10
-
Zafar, M.; Ahmed, S.; Khan, M.I.; Jamil, A.
Recombinant expression and characterization of a novel endoglucanase from Bacillus subtilis in Escherichia coli
Mol. Biol. Rep.
41
3295-3302
2014
Bacillus subtilis, Bacillus subtilis JS2004
Chang, C.J.; Lee, C.C.; Chan, Y.T.; Trudeau, D.L.; Wu, M.H.; Tsai, C.H.; Yu, S.M.; Ho, T.H.; Wang, A.H.; Hsiao, C.D.; Arnold, F.H.; Chao, Y.C.
Exploring the mechanism responsible for cellulase thermostability by structure-guided recombination
PLoS ONE
11
e0147485
2016
Geobacillus sp. (C5H6X3), Bacillus subtilis (P10475), Bacillus subtilis 168 (P10475), Geobacillus sp. 70PC53 (C5H6X3)
Gagoski, D.; Shi, Z.; Nielsen, L.K.; Vickers, C.E.; Mahler, S.; Speight, R.; Johnston, W.A.; Alexandrov, K.
Cell-free pipeline for discovery of thermotolerant xylanases and endo-1,4-beta-glucanases
J. Biotechnol.
259
191-198
2017
Castellaniella defragrans, Bacillus subtilis, Halosimplex carlsbadense
Kim, E.S.; Kim, B.S.; Kim, K.Y.; Woo, H.M.; Lee, S.M.; Um, Y.
Aerobic and anaerobic cellulose utilization by Paenibacillus sp. CAA11 and enhancement of its cellulolytic ability by expressing a heterologous endoglucanase
J. Biotechnol.
268
21-27
2018
Paenibacillus sp. CAA11 (A0A2S0UGE4), Bacillus subtilis (P10475), Bacillus subtilis, Bacillus subtilis 168 (P10475)
EXTERNAL LINKS (specific for EC-Number 3.2.1.4)
Transporter Classification Database (TCDB): 4.D.3.1.6
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