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Information on EC 3.2.1.39 - glucan endo-1,3-beta-D-glucosidase and Organism(s) Solanum tuberosum and UniProt Accession Q70C53
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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 taxonomic range for the selected organisms is: Solanum tuberosum
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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
GLUB20-2
(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
-
-
-
-
(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
-
-
-
-
(13)-beta-glucan 3-glucanohydrolase
-
-
-
-
(13)-beta-glucan endohydrolase
-
-
-
-
1,3-beta-glucan 3-glucanohydrolase
-
-
-
-
Acidic beta-1,3-glucanase
-
-
-
-
Anther-specific protein A6
-
-
-
-
Basic beta-1,3-endoglucanase BGN13.1
-
-
-
-
Basic beta-1,3-glucanase
-
-
-
-
Beta-1,3-endoglucanase GI
-
-
-
-
Beta-1,3-endoglucanase GII
-
-
-
-
Beta-1,3-endoglucanase GIII
-
-
-
-
Beta-1,3-endoglucanase GIV
-
-
-
-
Beta-1,3-endoglucanase GV
-
-
-
-
Beta-1,3-endoglucanase GVI
-
-
-
-
Beta-1,3-endoglucanase, basic
-
-
-
-
beta-1,3-glucanase
-
-
-
-
callase
-
-
-
-
endo-(1,3)-beta-D-glucanase
-
-
-
-
endo-(13)-beta-D-glucanase
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-
-
-
endo-1,3-beta-D-glucanase
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-
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endo-1,3-beta-glucanase
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-
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endo-1,3-beta-glucosidase
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-
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endo-1,3-glucanase
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-
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glucan endo-1,3-beta-glucosidase
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-
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Glucanase GLA
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-
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Glucanase GLB
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-
-
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kitalase
-
-
-
-
laminaranase
-
-
-
-
laminarinase
-
-
-
-
oligo-1,3-glucosidase
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-
-
-
PpGns1
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-
-
-
PR-2B
-
-
-
-
PR-35
-
-
-
-
PR-36
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-
-
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PR-37
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-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans
substrate binding structure and catalytic mechanism, overview
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
laminarihexose + H2O
laminaritriose + laminaritetraose
active with the wild-type enzyme, but also the active site mutant E259A, that shows residual activity in the substrate complex crystal and cleaves the substrate in two different ways, generating trisaccharides and tetrasaccharides, mass spectrometry
laminaritriose shows higher binding affinity and fully occupies the -1, -2 and -3 sites of the active-site cleft, even at a low molar excess of the substrate. At elevated substrate concentration laminaritetrose also occupies the active site, spanning the opposite sites +1, +2, +3 and +4 of the cleft
-
?
additional information
?
-
plant endo-1,3-beta-glucanases hydrolyze (1,3)-beta-glucans, with very limited activity towards mixed (1,3,1,4)-beta-glucans and branched (1,3,1,6)-beta-glucans
-
-
?
additional information
?
-
-
plant endo-1,3-beta-glucanases hydrolyze (1,3)-beta-glucans, with very limited activity towards mixed (1,3,1,4)-beta-glucans and branched (1,3,1,6)-beta-glucans
-
-
?
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
?
-
plant endo-1,3-beta-glucanases hydrolyze (1,3)-beta-glucans, with very limited activity towards mixed (1,3,1,4)-beta-glucans and branched (1,3,1,6)-beta-glucans
-
-
?
additional information
?
-
-
plant endo-1,3-beta-glucanases hydrolyze (1,3)-beta-glucans, with very limited activity towards mixed (1,3,1,4)-beta-glucans and branched (1,3,1,6)-beta-glucans
-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
252
enzyme isolated from culture with aeration at 135 rev/min and stirring at 0.8 vvm, pH 5.6, 28°C
62
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
the enzyme has a 23-residue signal peptide at the N-terminus
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
plant endo-1,3-beta-glucanases are involved in important physiological processes such as defence mechanisms, cell division and flowering. Endo-1,3-beta-glucanases in plants are believed to function as part of a defence mechanism against fungi by hydrolyzing the fungal cell wall, which is built mostly of (1,3)-beta-D-glucans
additional information
evolution
the enzyme belongs to the glycosyl hydrolase family 17, GH17
evolution
the enzyme is a member of plant glycoside hydrolase family 17, GH17
additional information
the geometry of the active site cleft clearly precludes any (1,4)-beta-glucan topology at the subsites from -3 to +4 and could possibly accommodate beta-1,6-branching only at subsites +1 and +2. The glucose units at subsites -1 and -2 interact with highly conserved protein residues. In contrast, subsites -3, +3 and +4 are variable, suggesting that the mode of glucose binding at these sites may vary between different plant endo-1,3-beta-glucanases. Low substrate affinity is observed at subsites +1 and +2, as manifested by disorder of the glycosyl units there. Structure-function analysis, overview
additional information
-
the geometry of the active site cleft clearly precludes any (1,4)-beta-glucan topology at the subsites from -3 to +4 and could possibly accommodate beta-1,6-branching only at subsites +1 and +2. The glucose units at subsites -1 and -2 interact with highly conserved protein residues. In contrast, subsites -3, +3 and +4 are variable, suggesting that the mode of glucose binding at these sites may vary between different plant endo-1,3-beta-glucanases. Low substrate affinity is observed at subsites +1 and +2, as manifested by disorder of the glycosyl units there. Structure-function analysis, overview
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). Q70C53_SOLTU
338
0
37855
TrEMBL
Secretory Pathway (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged mutant E259A in complex with laminarihexose, hanging drop vapour diffusion, mixing of 0.0015 ml of 7 mg/ml protein in 20 mM Tris-HCl, pH 8.0, with 0.0015 ml of reservoir solution containing 0.1 M sodium citrate, pH 5.6, 0.2 M ammonium acetate, 24% PEG 8000, 21°C, 2-7 days, crystals in form of bunched needles, single and larger crystals by use of streak-seeding, X-ray diffraction structure determination and analysis at 1.55-1.68 A, 3G and 7G crystal structures by molecular replacement
two different crystal forms: higher density and lower density determined at 1.40 A and 1.26 A resolution, respectively. The crystal structures reveal an unusual packing mode, clearly visible in the LD structure, caused by the presence of the C-terminal His6 tag, which extends from the compact fold of the enzyme molecule and docks in the catalytic cleft of a neighbouring molecule. In this way, an infinite chain of His-tag-linked protein molecules is formed along the c direction. Purified recombinant His-tagged enzyme by hanging drop vapour diffusion method, mixing of 0.0015 ml of 8 mg/ml protein in 20 mM Tris-HCl, pH 8.0, with 0.0015 ml of reservoir solution containing 0.1 M sodium acetate, pH 4.6, 0.2 M ammonium acetate, 25-30% PEG 4000, 21°C, 2 days, X-ray diffraction structure determination and analysis, modelling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C6A
significant decrease in activity towards carboxymethyl-curdlan and laminarin, strong increase in activity towards lichenan
E259A
site-directed mutagenesis, substitution of the nucleophilic residue, the active site mutant retains residual endoglucanase activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21 cell-free extract by ammonium sulfate fractionation, anion exchange chromatography, nickel affinity chromatography, and dialysis
recombinant His-tagged mutant E259A from Escherichia coli strain BL21 to homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene gluB20-2, recombinant expression of C-terminally His-tagged mutant E259A in Escherichia coli strain BL21
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
heterologous 1,3-beta-glucanase production in Escherichia coli is favoured with moderate culture aeration (0.7-0.9 vvm) and moderate stirring (125150 rev/min)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Witek, A.I.; Witek, K.; Hennig, J.
Conserved Cys residue influences catalytic properties of potato endo-(1-->3)-beta-glucanase GLUB20-2
Acta Biochim. Pol.
55
791-797
2008
Solanum tuberosum (Q70C53), Solanum tuberosum
Wojtkowiak, A.; Witek, K.; Hennig, J.; Jaskolski, M.
Two high-resolution structures of potato endo-1,3-beta-glucanase reveal subdomain flexibility with implications for substrate binding
Acta Crystallogr. Sect. D
68
713-723
2012
Solanum tuberosum (Q70C53), Solanum tuberosum Desiree (Q70C53)
Wojtkowiak, A.; Witek, K.; Hennig, J.; Jaskolski, M.
Structures of an active-site mutant of a plant 1,3-beta-glucanase in complex with oligosaccharide products of hydrolysis
Acta Crystallogr. Sect. D
69
52-62
2013
Solanum tuberosum (Q70C53), Solanum tuberosum
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