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Information on EC 3.2.1.73 - licheninase and Organism(s) Brevibacillus brevis and UniProt Accession P37073
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3.2.1.73 licheninaseIUBMB Comments
Acts on lichenin and cereal beta-D-glucans, but not on beta-D-glucans containing only 1,3- or 1,4-bonds.
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Word Map
- 3.2.1.73
- cellulases
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cellulolytic
- trichoderma
- knee
- reesei
- cellobiohydrolase
- exoglucanase
- thermocellum
- avicel
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carboxymethyl
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lignocellulosic
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cellulosic
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arthroscopic
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saccharification
- beta-glucosidase
- carboxymethylcellulose
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cellulose-binding
- straw
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microcrystalline
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glutenins
- cellulosome
- bagasse
- cellotriose
- lichenan
- xyloglucans
- cellulomonas
- cellotetraose
- xylanases
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3.2.1.4
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hemicellulases
- cmcase
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patellar
- endo-beta-1,4-glucanase
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patellofemoral
- succinogenes
- endoxylanase
-
dockerins
- humicola
-
fpase
- fibrobacter
-
cellulose-degrading
-
lysholm
-
lignocellulolytic
- mannanase
- cellodextrins
- meniscal
- cellobiase
- thermobifida
-
xylanolytic
- brewing
- synthesis
- endocellulase
- agriculture
- biofuel production
- degradation
- food industry
- analysis
- industry
- nutrition
The taxonomic range for the selected organisms is: Brevibacillus brevis
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
endoglucanase, plica, glu-1, glu-3, endo-beta-glucanase, 1,3-1,4-beta-glucanase, 1,3-1,4-beta-d-glucanase, bglc8h, af-egl7, xyniii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(1->3,1->4)-beta-glucanase isoenzyme EII
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1,3-1,4-beta-D-glucan 4-glucanohydrolase
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1,3-1,4-beta-D-glucan glucanohydrolase
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1,3;1,4-beta-glucan 4-glucanohydrolase
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1,3;1,4-beta-glucan endohydrolase
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beta-(1--> 3), (1--> 4)-D-glucan 4-glucanohydrolase
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endo-beta-1,3-1,4 glucanase
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laminarinase
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Lichenase
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Mixed linkage beta-glucanase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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SYSTEMATIC NAME
IUBMB Comments
(1->3)-(1->4)-beta-D-glucan 4-glucanohydrolase
Acts on lichenin and cereal beta-D-glucans, but not on beta-D-glucans containing only 1,3- or 1,4-bonds.
CAS REGISTRY NUMBER
COMMENTARY
37288-51-0
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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
additional information
?
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lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
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?
additional information
?
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beta-1,3-1,4-glucanases or lichenases are enzymes that in a strictly specific manner hydrolyze beta-glucans of many cereal species and lichens containing beta-1,3 and beta-1,4 bonds
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?
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
?
-
lichenases stringently catalyze endohydrolysis of the beta-1,4-glycoside bond adjacent to 3-O-substituted glucose residue in cereal beta-glucans and lichenan
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?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
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no inhibition up to a concentration of 10% SDS-PAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 11
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pH 6.0: about 55% of maximal activity, pH 11.0: about 45% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 80
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40°C: about 40% of maximal activity, 80°C: about 30% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene bglBB, recombinant expression in Escherichia coli, the enzyme is secreted
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
application of lichenases is attractive and promising for biocatalytic conversion of biomass, in particular, in the areas of their biotechnological application, such as brewing industry, animal feed manufacture, and biofuel production
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Louw, M.E.; Reid, S.J.
Characterization, cloning and sequencing of a thermostable endo-(1,3-1,4)beta-glucanase-encoding gene from an alkalophilic Bacillus brevis
Appl. Microbiol. Biotechnol.
38
507-513
1993
Brevibacillus brevis
Goldenkova-Pavlova, I.V.; Tyurin, A.A.; Mustafaev, O.N.
The features that distinguish lichenases from other polysaccharide-hydrolyzing enzymes and the relevance of lichenases for biotechnological applications
Appl. Microbiol. Biotechnol.
102
3951-3965
2018
Bacillus amyloliquefaciens, Bacillus amyloliquefaciens (P07980), Bacillus altitudinis, Paenibacillus barcinonensis (A0A097QQT4), Bacillus pumilus (A0A0F6QU36), Paenibacillus barengoltzii (A0A0K1P4J7), Bacillus velezensis (A0A0M4NIK2), Acetivibrio thermocellus (A3DBX3), Acetivibrio thermocellus (Q84C00), Bacillus subtilis (A8CGP1), Bacillus subtilis (G0YW23), Bacillus subtilis (P04957), Bacillus subtilis (Q45691), Paenibacillus polymyxa (A9Z0X6), Ruminococcus albus (E9SCT3), Bacillus sp. SJ-10 (I1W007), Bacillus tequilensis (K0A689), Fibrobacter succinogenes (P17989), Niallia circulans (P19254), Bacillus licheniformis (P27051), Brevibacillus brevis (P37073), Rhodothermus marinus (P45798), Bacillus sp. N137 (Q45648), Bacillus sp. A3 (Q6YAT3), Paenibacillus macerans (Q846Q0), Bacillus subtilis MA139 (A8CGP1), Bacillus tequilensis CGX5-1 (K0A689), Acetivibrio thermocellus DSM 1237 (A3DBX3), Bacillus subtilis 168 (P04957), Ruminococcus albus 8 (E9SCT3), Acetivibrio thermocellus NBRC 103400 (A3DBX3), Brevibacillus brevis ALK36 (P37073), Bacillus velezensis S2 (A0A0M4NIK2), Bacillus altitudinis YC-9, Bacillus subtilis NCIB 8565 (Q45691), Paenibacillus polymyxa CP7 (A9Z0X6), Niallia circulans ATCC 21367 (P19254), Rhodothermus marinus ITI378 (P45798), Bacillus amyloliquefaciens ATCC 23350, Bacillus amyloliquefaciens ATCC 15841 (P07980), Acetivibrio thermocellus ATCC 27405 (A3DBX3), Fibrobacter succinogenes S85 (P17989), Acetivibrio thermocellus VPI 7372 (A3DBX3), Bacillus pumilus US570 (A0A0F6QU36), Bacillus subtilis SU40 (G0YW23), Paenibacillus barcinonensis BP-23 (A0A097QQT4), Acetivibrio thermocellus F7 (Q84C00), Acetivibrio thermocellus NCIMB 10682 (A3DBX3), Acetivibrio thermocellus NRRL B-4536 (A3DBX3)
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