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Information on EC 3.2.1.39 - glucan endo-1,3-beta-D-glucosidase and Organism(s) Rhizomucor miehei and UniProt Accession A0A023I7E1
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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: Rhizomucor miehei
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
(1->3)-beta-glucan endohydrolase
-
-
-
-
(1->3)-beta-glucan endohydrolase BGN13.1
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-
-
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(1->3)-beta-glucan endohydrolase GI
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-
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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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-
-
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(1->3)-beta-glucan endohydrolase GV
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-
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(1->3)-beta-glucan endohydrolase GVI
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-
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(1->3)-beta-glucanase
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-
-
-
(1->3)-beta-glucanase A1
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-
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(1->3)-beta-glucanase BGN13.1
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-
-
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(1->3)-beta-glucanase isoenzyme GI
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-
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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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-
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(1->3)-beta-glucanase isoenzyme GV
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-
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(1->3)-beta-glucanase isoenzyme GVI
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-
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-
(13)-beta-glucan 3-glucanohydrolase
-
-
-
-
(13)-beta-glucan endohydrolase
-
-
-
-
1,3-beta-glucan 3-glucanohydrolase
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-
-
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Acidic beta-1,3-glucanase
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-
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Anther-specific protein A6
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-
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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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-
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-
Beta-1,3-endoglucanase GII
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-
-
-
Beta-1,3-endoglucanase GIII
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-
-
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Beta-1,3-endoglucanase GIV
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-
-
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Beta-1,3-endoglucanase GV
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-
-
-
Beta-1,3-endoglucanase GVI
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-
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Beta-1,3-endoglucanase, basic
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-
-
-
beta-1,3-glucanase
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-
-
-
callase
-
-
-
-
endo-(1,3)-beta-D-glucanase
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-
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-
endo-(13)-beta-D-glucanase
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-
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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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-
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Glucanase GLA
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Glucanase GLB
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kitalase
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-
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laminaranase
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-
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laminarinase
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-
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oligo-1,3-glucosidase
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-
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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
LITERATURE
hydrolysis of O-glycosyl bond
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-
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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
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
2 laminaripentaose + H2O
octasaccharide + ?
transglycosylation activity, product is a linear beta-1,3-octasaccharide containing an intrachain beta-1,6 linkage
-
-
?
laminaripentaose + H2O
laminaritetraose + ?
efficient hydrolytic activity
-
-
?
laminaritetraose + H2O
laminaritriose + ?
efficient hydrolytic activity
-
-
?
reduced laminarin + H2O
laminaritriose + laminaritetraose + laminari-oligosaccharides
high hydrolytic activity
-
-
?
yeast beta-D-glucan + H2O
laminaritriose + laminari-oligosaccharides
-
-
-
?
additional information
?
-
-
the enzyme hardly cleaves the beta-1,3 linkage in laminaribiose
-
-
?
additional information
?
-
the enzyme hardly cleaves the beta-1,3 linkage in laminaribiose
-
-
?
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 60
the enzyme retains over 50 % of its activity between 40 and 60°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the glycosyl hydrolase family 81, GH81, but has a unique structure
additional information
additional information
the enzyme monomer consists of an N-terminal beta-sandwich domain, a C-terminal (alpha/alpha)6 domain and an additional domain between them. Glu553 and Glu557 are proposed to serve as the proton donor and basic catalyst, respectively, in a single-displacement mechanism. In addition, Tyr386, Tyr482 and Ser554 possibly contribute to both the position or the ionization state of the basic catalyst Glu557, catalytic cleft and the active site structure, overview
additional information
the enzyme monomer consists of an N-terminal beta-sandwich domain, a C-terminal (alpha/alpha)6 domain and an additional domain between them. Glu553 and Glu557 are proposed to serve as the proton donor and basic catalyst, respectively, in a single-displacement mechanism. In addition, Tyr386, Tyr482 and Ser554 possibly contribute to both the position or the ionization state of the basic catalyst Glu557, catalytic cleft and the active site structure, 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). A0A023I7E1_RHIMI
796
0
89495
TrEMBL
Secretory Pathway (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme monomer consists of an N-terminal beta-sandwich domain, a C-terminal (alpha/alpha)6 domain and an additional domain between them, three-dimensional structure of enzyme RmLam81A domain A, domain B and domain C, overview
additional information
the enzyme monomer consists of an N-terminal beta-sandwich domain, a C-terminal (alpha/alpha)6 domain and an additional domain between them, three-dimensional structure of enzyme RmLam81A domain A, domain B and domain C, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant detagged wild-type and selenomethionine-labeled enzymes, sitting drop vapour diffusion method, mixing of 0.001 ml of 20 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 100 mM NaCl, with 0.001 ml of precipitant solution containing 200 mM Li2SO4, 30% w/v PEG 4000, 100 mM Tris-HCl, pH 8.5, or 160 mM Li2SO4, 24% w/v PEG 4000, 80 mM Tris-HCl, pH 8.5, 6% v/v 2-methyl-2,4-pentanediol, 2-4 weeks, X-ray diffraction structure determination and analysis at 2.0-2.3 A resolution
the overall structure of the Lam81A monomer consists of an N-terminal beta-sandwich domain, a C-terminal (alpha/alpha)6 domain and an additional domain between them. Residues Glu553 and Glu557 are proposed to serve as the proton donor and basic catalyst, respectively, in a single-displacement mechanism. In addition, Tyr386, Tyr482 and Ser554 possibly contribute to both the position or the ionization state of the basic catalyst Glu557
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E158A
mutation switches the activity from mainly transglycosylation to beta-1,3-glucanase. Hydrolytic activity toward reduced laminarin is 348.5fold higher than the wild type
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 8
the enzyme exhibits good pH stability within the range of pH 4.0-8.0, retaining over 80 % of its activity after 30 min
744118
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
the enzyme is stable up to 50 °C, with more than 90 % of its activity remaining after 30 min
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and selenomethionine-labeled enzymes from Escherichia coli by nickel affinity chromatography, ultrafiltration, tag cleavage by Bacillus subtilis proteases, and gel filtration
Ni-IDA column chromatography, and Sephacryl S-100 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged wild-type and selenomethionine-labeled enzyme in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zhou, P.; Chen, Z.; Yan, Q.; Yang, S.; Hilgenfeld, R.; Jiang, Z.
The structure of a glycoside hydrolase family 81 endo-?-1,3-glucanase.
Acta Crystallogr. Sect. D
69
2027-2038
2013
Rhizomucor miehei (A0A023I7E1), Rhizomucor miehei (U5HK45), Rhizomucor miehei CAU432 (A0A023I7E1)
Qin, Z.; Yan, Q.; Yang, S.; Jiang, Z.
Modulating the function of a beta-1,3-glucanosyltransferase to that of an endo-beta-1,3-glucanase by structure-based protein engineering
Appl. Microbiol. Biotechnol.
100
1765-1776
2016
Rhizomucor miehei, Rhizomucor miehei (A0A0K0M737), Rhizomucor miehei CAU432, Rhizomucor miehei CAU432 (A0A0K0M737)
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