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Information on EC 3.2.1.73 - licheninase and Organism(s) Rhodothermus marinus and UniProt Accession P45798

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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
                3.2.1.73 licheninase
IUBMB 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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This record set is specific for:
Rhodothermus marinus
UNIPROT: P45798
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The taxonomic range for the selected organisms is: Rhodothermus marinus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-1,3-1,4-glucanase
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(1->3,1->4)-beta-glucanase isoenzyme EII
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-
-
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1,3-1,4-beta-D-glucan 4-glucanohydrolase
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-
-
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1,3-1,4-beta-D-glucan glucanohydrolase
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-
-
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1,3;1,4-beta-glucan 4-glucanohydrolase
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-
-
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1,3;1,4-beta-glucan endohydrolase
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-
-
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beta-(1--> 3), (1--> 4)-D-glucan 4-glucanohydrolase
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-
-
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endo-beta-1,3-1,4 glucanase
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-
-
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laminarinase
-
-
-
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Lichenase
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-
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Mixed linkage beta-glucanase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
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-
-
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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 hide
37288-51-0
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
beta-glucan + H2O
?
show the reaction diagram
-
-
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-(1,3)-beta-D-glucooligosaccharides + H2O
4-methylumbelliferol + beta-D-oligosaccharides
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
beta-glucan + H2O
?
show the reaction diagram
-
-
-
?
laminarin + H2O
?
show the reaction diagram
-
-
-
?
lichenan + H2O
?
show the reaction diagram
-
-
-
?
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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-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
i.e. Rhodothermus obamensis
UniProt
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GUB_RHOMR
286
0
33145
Swiss-Prot
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
16 h, completely stable
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene bglA, recombinant expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
Borriss, R.; Krah, M.; Brumer, H.3rd.; Kerzhner, M.A.; Ivanen, D.R.; Eneyskaya, E.V.; Elyakova, L.A.; Shishlyannikov, S.M.; Shabalin, K.A.; Neustroev, K.N.
Enzymatic synthesis of 4-methylumbelliferyl (1-->3)-beta-D-glucooligosaccharides-new substrates for beta-1,3-1,4-D-glucanase
Carbohydr. Res.
338
1455-1467
2003
Rhodothermus marinus
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team