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Information on EC 3.2.1.39 - glucan endo-1,3-beta-D-glucosidase
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EC Tree
3.2.1.39 glucan endo-1,3-beta-D-glucosidaseIUBMB 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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Word Map
- 3.2.1.39
- chitinase
- glucans
- barley
- beta-glucans
-
pathogenesis-related
- polysaccharide
- cellulase
- beta-1,3-glucans
- xylanase
- trichoderma
- elicitors
- chitin
- phytophthora
-
biocontrol
- callose
- lichenan
- solani
-
mannoproteins
- rhizoctonia
-
transglycosylation
-
defense-related
-
thaumatin-like
-
zymolyase
-
digesta
-
mycoparasitism
- harzianum
- laminaribiose
-
mixed-linkage
- circulans
- capsici
-
hemicellulase
-
fibrobacter
- gentiobiose
- curdlan
- digitata
-
carbohydrases
-
laminaria
- pectinase
-
neurexins
- pharmacology
- medicine
- synthesis
- food industry
- biotechnology
- agriculture
- analysis
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(1->3)-beta-glucan endohydrolase
-
-
-
-
(1->3)-beta-glucan endohydrolase BGN13.1
-
-
-
-
(1->3)-beta-glucan endohydrolase GI
-
-
-
-
(1->3)-beta-glucan endohydrolase GII
-
-
-
-
(1->3)-beta-glucan endohydrolase GIII
-
-
-
-
(1->3)-beta-glucan endohydrolase GIV
-
-
-
-
(1->3)-beta-glucan endohydrolase GV
-
-
-
-
(1->3)-beta-glucan endohydrolase GVI
-
-
-
-
(1->3)-beta-glucanase
-
-
-
-
(1->3)-beta-glucanase A1
-
-
-
-
(1->3)-beta-glucanase BGN13.1
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-
-
-
(1->3)-beta-glucanase isoenzyme GI
-
-
-
-
(1->3)-beta-glucanase isoenzyme GII
-
-
-
-
(1->3)-beta-glucanase isoenzyme GIII
-
-
-
-
(1->3)-beta-glucanase isoenzyme GIV
-
-
-
-
(1->3)-beta-glucanase isoenzyme GV
-
-
-
-
(1->3)-beta-glucanase isoenzyme GVI
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-
-
-
(13)-beta-glucan 3-glucanohydrolase
-
-
-
-
(13)-beta-glucan endohydrolase
-
-
-
-
1,3-beta-glucan 3-glucanohydrolase
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-
-
-
Acidic beta-1,3-glucanase
-
-
-
-
Anther-specific protein A6
-
-
-
-
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
-
-
-
-
Beta-1,3-endoglucanase GIV
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-
-
-
Beta-1,3-endoglucanase GV
-
-
-
-
Beta-1,3-endoglucanase GVI
-
-
-
-
Beta-1,3-endoglucanase, basic
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-
-
-
beta-1,3-glucanase
-
-
-
-
callase
-
-
-
-
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
-
-
-
-
endo-1,3-beta-glucosidase
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-
-
-
endo-1,3-glucanase
-
-
-
-
glucan endo-1,3-beta-glucosidase
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-
-
-
Glucanase GLA
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-
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Glucanase GLB
-
-
-
-
kitalase
-
-
-
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laminaranase
-
-
-
-
laminarinase
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-
-
-
oligo-1,3-glucosidase
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-
-
-
PpGns1
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-
-
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PR-2B
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-
-
-
PR-35
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-
-
-
PR-36
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-
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-
PR-37
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-
-
-
additional information
LamA contains a catalytic module of the glycoside hydrolase family 16, GH16
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
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
9025-37-0
-
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
laminarin + H2O
laminaritriose
preferred substrate
main product
-
?
additional information
?
-
the catalytic module has an inhibitory effect on the growth of Candida albicans and Rhizoctonia solani. The presence of the carbohydrate-binding module and the analogue of coagulation factor Fa5/8C enhance the inhibitory effect
-
-
?
additional information
?
-
the catalytic module specifically hydrolyzes beta-1,3- and beta-1,3-1,4-glucan. The catalytic module has an inhibitory effect on the growth of Candida albicans and Rhizoctonia solani. The presence of the carbohydrate-binding module and the analogue of coagulation factor Fa5/8C enhance the inhibitory effect
-
-
?
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 catalytic module has an inhibitory effect on the growth of Candida albicans and Rhizoctonia solani. The presence of the carbohydrate-binding module and the analogue of coagulation factor Fa5/8C enhance the inhibitory effect
-
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
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). SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
putative functional units of the single protein strain include, from N to C terminus, a leader peptide, three repeats of the S-layer homologous module, a catalytic module of glycoside hydrolase family 16, four repeats of the carbohydrate-binding module of family CBM_4_9, and an analogue of coagulation factor Fa5/8C
additional information
the beta-1,3-glucanase LamA is highly modular, containing a signal sequence, three repeats of the S-layer homologous module, a segment with unknown function, a catalytic module of glycoside hydrolase family 16, GH16, four repeats of CBM4 family, and a F5/8C module representing a discoidin domain, DS domain, from N- to C-terminus. The recombinant isolated purified His-tagged DS domain forms dimers
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
W1679A
site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
W1688A
site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
W1729A
site-directed mutagenesis, mutation in the F5/8C module or DS domain, the mutant domain forms inclusion bodies upon expression in Escherichia coli
Y1714A
site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
Y1768A
site-directed mutagenesis, the mutation in the F5/8C module or DS domain decreases the protein affinity to laminarin
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
melting temperatures of wild-type and mutant DS domains between 52.3°C and 58.3°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant LamA discoidin domains from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of the isolated wild-type and mutant LamA discoidin domains as soluble His-tagged proteins in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cheng, Y.M.; Hong, T.Y.; Liu, C.C.; Meng, M.
Cloning and functional characterization of a complex endo-beta-1,3-glucanase from Paenibacillus sp.
Appl. Microbiol. Biotechnol.
81
1051-1061
2009
Paenibacillus sp. CCRC 17245 (Q000P7)
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Release 2023.1 (January 2023)
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