3.2.1.6: endo-1,3(4)-beta-glucanase
This is an abbreviated version!
For detailed information about endo-1,3(4)-beta-glucanase, go to the full flat file.
Word Map on EC 3.2.1.6
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3.2.1.6
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cellulase
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xylanase
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cellulolytic
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carboxymethyl
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straw
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trichoderma
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carboxymethylcellulase
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beta-glucosidase
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fpase
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beta-glucans
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thermocellum
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lignocellulosic
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xylan
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saccharification
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avicel
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lichenan
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reesei
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hemicellulose
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avicelase
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endoglucanases
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bagasse
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cellulosic
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bran
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cellobiohydrolase
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cellulose-binding
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cellulomonas
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cellulose-degrading
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exoglucanase
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fibrobacter
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lignocellulolytic
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cellobiase
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cellulosome
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succinogenes
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cellooligosaccharides
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cellotriose
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mixed-linkage
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xylanolytic
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microcrystalline
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cellotetraose
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agriculture
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fibrolytic
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acid-swollen
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cellopentaose
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synthesis
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food industry
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drug development
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degradation
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nutrition
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analysis
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lignocellulose-degrading
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macerans
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laminaribiose
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neocallimastix
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dockerin
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biotechnology
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sawdust
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endo-1,4-beta-xylanase
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endo-1,4-beta-d-glucanase
- 3.2.1.6
- cellulase
- xylanase
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cellulolytic
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carboxymethyl
- straw
- trichoderma
- carboxymethylcellulase
- beta-glucosidase
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fpase
- beta-glucans
- thermocellum
-
lignocellulosic
- xylan
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saccharification
- avicel
- lichenan
- reesei
- hemicellulose
- avicelase
- endoglucanases
- bagasse
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cellulosic
- bran
- cellobiohydrolase
-
cellulose-binding
- cellulomonas
-
cellulose-degrading
- exoglucanase
- fibrobacter
-
lignocellulolytic
- cellobiase
- cellulosome
- succinogenes
- cellooligosaccharides
- cellotriose
-
mixed-linkage
-
xylanolytic
-
microcrystalline
- cellotetraose
- agriculture
-
fibrolytic
-
acid-swollen
- cellopentaose
- synthesis
- food industry
- drug development
- degradation
- nutrition
- analysis
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lignocellulose-degrading
- macerans
- laminaribiose
- neocallimastix
-
dockerin
- biotechnology
- sawdust
- endo-1,4-beta-xylanase
- endo-1,4-beta-d-glucanase
Reaction
Synonyms
1,3-(4)-beta-glucanase (endoglucanase), 1,3-1,4-beta-glucanase EII (barley), 1,3-beta-D-glucanase, AFUA_1G05290, AFUA_2G14360, AFUA_4G13360, AFUA_5G02280, Agl9A, AkLam36, barley-beta-D-glucanase, beta-1,3-1,4 glucanase, beta-1,3-1,4-glucanase, beta-1,3-glucanase, beta-1,3:1,4 glucanase, beta-D-(1-3)-glucanase, beta-glucanase, bglBC1, CBM-CD, CC1G_01665, Cel8A, CelL, chitosanase, CMCase, CtLic26A, enda-beta-(1-3),(1-4)-glucanase, endo beta-1,3-glucanase IV, endo-1,3(4)-beta-D-glucanase, endo-1,3(4)-beta-glucanase, endo-1,3-1,4-beta-D-glucanase, endo-1,3-beta-D-glucanase, endo-1,3-beta-glucanase, endo-1,4-beta-glucanase, endo-beta-(1-3)-D-glucanase, endo-beta-1,3(4)-glucanase, endo-beta-1,3-1,4-D-glucanase, endo-beta-1,3-1,4-glucanase, endo-beta-1,3-glucanase, endo-beta-1,4-glucanase, eng1, ENG16A, Eng2, Eng3, Eng4, Eng5, Engl1, Fsbeta-glucanase, GluA, H(A16-M), HdLam33, LAM, Lam16A, LamA, lamarinase, laminaranase, laminarinase, laminarinase 16A, laminarinase II, laminarinase Lam16A, LamR, LIC 1, Lic16A, Lic8H, Lichenase, More, nonlytic endo-beta-1,3-glucanase I, SsGlc, TcGlu2, TeEgl5A, Xyn10B
ECTree
3.2.1.6 endo-1,3(4)-beta-glucanaseAdvanced search results
results (
results (Organism
Organism on EC 3.2.1.6 - endo-1,3(4)-beta-glucanase
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ORGANISM 
COMMENTARY 
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional CMCase and chitosanase, reactions of EC 3.2.1.4 and EC 3.2.16, respectively
UniProt
bifunctional CMCase and chitosanase, reactions of EC 3.2.1.4 and EC 3.2.16, respectively
UniProt
H(A16-M), a 1,3-1,4-beta-glucanase from Bacillus macerans in which the 16 N-terminal residues have been replaced by the respective residues of the enzyme from Bacillus amyloliquefaciens
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