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Information on EC 3.2.1.39 - glucan endo-1,3-beta-D-glucosidase

for references in articles please use BRENDA:EC3.2.1.39
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EC Tree
IUBMB Comments
Different from EC 3.2.1.6 endo-1,3(4)-beta-glucanase. Very limited action on mixed-link (1->3,1->4)-beta-D-glucans. Hydrolyses laminarin, paramylon and pachyman.
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This record set is specific for:
UNIPROT: Q9L816
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
beta-1,3-glucanase, beta-glucanase, glud2, laminarinase, 1,3-beta-glucanase, endo-beta-1,3-glucanase, exo-beta-1,3-glucanase, beta-1,3 glucanase, callase, beta-1,3-endoglucanase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
(1->3)-beta-glucan endohydrolase
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(1->3)-beta-glucan endohydrolase BGN13.1
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(1->3)-beta-glucan endohydrolase GI
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(1->3)-beta-glucan endohydrolase GII
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(1->3)-beta-glucan endohydrolase GIII
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(1->3)-beta-glucan endohydrolase GIV
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(1->3)-beta-glucan endohydrolase GV
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(1->3)-beta-glucan endohydrolase GVI
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(1->3)-beta-glucanase
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(1->3)-beta-glucanase A1
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(1->3)-beta-glucanase BGN13.1
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(1->3)-beta-glucanase isoenzyme GI
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(1->3)-beta-glucanase isoenzyme GII
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(1->3)-beta-glucanase isoenzyme GIII
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(1->3)-beta-glucanase isoenzyme GIV
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(1->3)-beta-glucanase isoenzyme GV
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(1->3)-beta-glucanase isoenzyme GVI
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(13)-beta-glucan 3-glucanohydrolase
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(13)-beta-glucan endohydrolase
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1,3-beta-glucan 3-glucanohydrolase
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Acidic beta-1,3-glucanase
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Anther-specific protein A6
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Basic beta-1,3-endoglucanase BGN13.1
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Basic beta-1,3-glucanase
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Beta-1,3-endoglucanase GI
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Beta-1,3-endoglucanase GII
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Beta-1,3-endoglucanase GIII
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Beta-1,3-endoglucanase GIV
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Beta-1,3-endoglucanase GV
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Beta-1,3-endoglucanase GVI
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Beta-1,3-endoglucanase, basic
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beta-1,3-glucanase
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callase
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endo-(1,3)-beta-D-glucanase
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endo-(13)-beta-D-glucanase
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endo-1,3-beta-D-glucanase
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endo-1,3-beta-glucanase
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endo-1,3-beta-glucosidase
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endo-1,3-glucanase
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glucan endo-1,3-beta-glucosidase
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Glucanase GLA
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Glucanase GLB
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kitalase
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laminaranase
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laminarinase
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oligo-1,3-glucosidase
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PpGns1
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PR-2B
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PR-35
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PR-36
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PR-37
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
3-beta-D-glucan glucanohydrolase
Different from EC 3.2.1.6 endo-1,3(4)-beta-glucanase. Very limited action on mixed-link (1->3,1->4)-beta-D-glucans. Hydrolyses laminarin, paramylon and pachyman.
CAS REGISTRY NUMBER
COMMENTARY hide
9025-37-0
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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
curdlan + H2O
?
show the reaction diagram
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?
laminarin + H2O
?
show the reaction diagram
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?
lichenan + H2O
?
show the reaction diagram
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?
pachyman + H2O
?
show the reaction diagram
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?
zymosan A + H2O
?
show the reaction diagram
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?
additional information
?
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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
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
Q9L816_9ACTN
478
0
49432
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49000
x * 49000, deduced from gene sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 49000, deduced from gene sequence
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
catalytic domain, to 1.5 A resolution. The overall structure contains two antiparallel six- and seven-stranded beta-sheets stacked in a beta-sandwich jelly-roll motif. The active-site cleft of the enzyme shows the closure of one end primarily caused by two protruding loop insertions and two key residues, Y38 and Y134
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70
70 min, 50% residual activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hong, T.Y.; Cheng, C.W.; Huang, J.W.; Meng, M.
Isolation and biochemical characterization of an endo-1,3-beta-glucanase from Streptomyces sioyaensis containing a C-terminal family 6 carbohydrate-binding module that binds to 1,3-beta-glucan
Microbiology
148
1151-1159
2002
Streptomyces sioyaensis (Q9L816), Streptomyces sioyaensis
Manually annotated by BRENDA team
Hong, T.Y.; Hsiao, Y.Y.; Meng, M.; Li, T.T.
The 1.5 A structure of endo-1,3-beta-glucanase from Streptomyces sioyaensis: evolution of the active-site structure for 1,3-beta-glucan-binding specificity and hydrolysis
Acta Crystallogr. Sect. D
64
964-970
2008
Streptomyces sioyaensis (Q9L816), Streptomyces sioyaensis
Manually annotated by BRENDA team