Information on EC 3.2.1.59 - glucan endo-1,3-alpha-glucosidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.2.1.59
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RECOMMENDED NAME
GeneOntology No.
glucan endo-1,3-alpha-glucosidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Endohydrolysis of (1->3)-alpha-D-glucosidic linkages in isolichenin, pseudonigeran and nigeran
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
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SYSTEMATIC NAME
IUBMB Comments
3-alpha-D-glucan 3-glucanohydrolase
Products from pseudonigeran (1,3-alpha-D-glucan) are nigerose and alpha-D-glucose.
CAS REGISTRY NUMBER
COMMENTARY hide
9075-84-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain 1
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Manually annotated by BRENDA team
HU-M1
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
no activity in Bacillus subtilis
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Manually annotated by BRENDA team
putative; growth on fermented soybean
UniProt
Manually annotated by BRENDA team
gene agn1
UniProt
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
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-
-
Manually annotated by BRENDA team
ki-8
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Manually annotated by BRENDA team
effective production by strain M-7, low production by strain strain F-560
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-1,3-glucan + H2O
?
show the reaction diagram
alpha-1,3-glucan + H2O
beta-D-glucose + ?
show the reaction diagram
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MutAp displays endo-hydrolytic activity. A tetrasaccharide is the minimal substrate for MutAp. The polysaccharide-binding domain in MutAp may be involved in processivity, either by partially disrupting the crystalline structure of (1-3)-alpha-glucan and thereby making it more accessible to hydrolysis, or by assisting in retention of (1-3)-alpha-glucan after each round of hydrolysis. The enzyme breaks an intrachain glycosidic linkage of (1-3)-alpha-glucan, and then continues its hydrolysis towards the non-reducing end by releasing beta-glucose residues in a processive manner. Acts by inversion of the anomeric configuration
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?
alpha-1,3-glucan pentasaccharide + H2O
alpha-1,3-glucan tetrasaccharide + D-glucose
show the reaction diagram
minimum size of substrate accepted
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?
borohydride-treated alpha-1,3-glucan hexasaccharide + H2O
alpha-1,3-glucan tetrasaccharide + alpha-1,3-glucan disaccharide alditol
show the reaction diagram
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-
?
carboxymethyl alpha-1,3-glucan + H2O
?
show the reaction diagram
fungal cell walls + H2O
?
show the reaction diagram
glucan + H2O
?
show the reaction diagram
glucan + H2O
isomaltose + nigerose + nigerotriose + oligosaccharides
show the reaction diagram
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insoluble, sticky glucan of Streptococcus mutans
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?
glucan + H2O
nigerose + glucose
show the reaction diagram
isolichenin + H2O
?
show the reaction diagram
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-
-
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lentinus alpha-1,3-glucan + H2O
?
show the reaction diagram
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-
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?
limit glucan + H2O
?
show the reaction diagram
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?
mutan + H2O
?
show the reaction diagram
nigeran + H2O
?
show the reaction diagram
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-
-
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?
nigeropentaose + H2O
D-glucose + nigerose
show the reaction diagram
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-
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?
nigerotetraose + H2O
D-glucose + nigerose
show the reaction diagram
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?
nigerotriose + H2O
D-glucose + nigerose
show the reaction diagram
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?
pseudonigeran + H2O
?
show the reaction diagram
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pseudonigeran + H2O
nigerose + alpha-D-glucose
show the reaction diagram
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-1,3-glucan + H2O
?
show the reaction diagram
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-
-
-
?
glucan + H2O
?
show the reaction diagram
isolichenin + H2O
?
show the reaction diagram
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-
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nigeran + H2O
?
show the reaction diagram
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-
-
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pseudonigeran + H2O
?
show the reaction diagram
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-
-
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-
additional information
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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no requirement of divalent metal
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glucoamylase
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strongly decreases activity
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glucocerebrosidase
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strongly decreases activity
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iodoacetamide
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p-chloromercuribenzoic acid
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additional information
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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CCAGCC motif in the agn1 promoter acts as an upstream activating sequence that is dependent on Ace2p. The motif is essential for agn1 promoter activity in vivo
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
80
limit glucan
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0.46
pseudonigeran
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additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
91.3 - 158.7
alpha-1,3-glucan
additional information
additional information
Bacillus circulans
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the amount of reducing sugar in the supernatant of the enzyme assay is determined
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8.5
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additional information
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Agn1p shows a pronounced pH optimum at pH 3, whereas Agn2p shows highest activity to (1,3)-alpha-glucan at pH 6
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 7
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pH 3: 30% of optimum activity, pH 7: 20% of optimum activity
4.5 - 8.5
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pH 4.5: 40% of optimal activity, pH 8.5: 70% of optimal activity
4.5 - 8
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sharp decrease below pH 4.5, gradual decrease up to pH 8.0
4.5 - 7
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4.5: about 35% of maximal activity, pH 7.0: about 60% of maximal activity
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 80
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30°C: 18% of optimum activity, 80°C: 25% of optimum activity
30 - 50
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30°C: about 75% of maximal activity, 50°C: about 30% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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high expression level
Manually annotated by BRENDA team
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high expression level
Manually annotated by BRENDA team
additional information
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no activity in conidiophores, cleistothecial primordia or ascospores
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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cell separation is achieved by the concerted action of the Eng1 endo-beta-1,3-glucanase and Ang1 endo-alpha-1,3-glucanase, which are transported to the septum and localize to a ringlike structure that surrounds the septum. Mislocation of Eng1 and Agn1 might be the reason underlying the failure to separate efficiently
Manually annotated by BRENDA team
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Agn2 lacks a signal peptide for entry into the secretory pathway and therefore localizes intracellularly to the cytosol of the diploid cell
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65000
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SDS-PAGE
67000
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4 * 67000, SDS-PAGE
68000
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SDS-PAGE
75000
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SDS-PAGE and MALDI-MS
78000
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SDS-PAGE
134000
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SDS-PAGE
160000
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SDS-PAGE
180000
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HPLC
274000
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gel filtration
279000
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aggregated form, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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50000, Agn2p, SDS-PAGE
monomer
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1 * 47000, SDS-PAGE
oligomer
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possibly oligomeric or aggregated form, molecular weight larger than 300000, x * 68000, SDS-PAGE, Streptomyces chartreusis
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
no glycoprotein
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.8
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50% loss of activity after 10 min
136691
4.2
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50% loss of activity after 30 min
136691
5.25 - 10.5
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30°C, stable for at least 1.5 h
136691
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
21
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diluted enzyme, 1:19, 0.2 M acetate bufferm pH 5.5, at room temperature is stable for 24-48 h
35
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1 h, stable up to
37
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pH 5.5, 3 days, 3% loss of activity
40
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5% loss of activity after 90 min
65
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pH 6.0, 10 min, complete inactivation
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing, -15°C, appreciable loss in activity
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the enzyme in crude state is highly stable after two treatments of freezing and thawing
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 18 months, 17% loss of activity
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4°C, 2 years, pH 6, stable
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4°C, crude enzyme is stable for about 2 weeks
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Agn2p purified by immobilized metal ion affinity chromatography followed by anion exchange chromatography
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NRRL-B-12324
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recombinant secreted wild-type and deletion mutant enzymes from Escherichia coli strain Rosetta-gami B (DE3) culture supernatant by dialysis, anion exchange chromatography, ammonium sulfate fractionation and hydrophobic interaction chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Agn1p signal peptide (amino acids 1-20) cloned between the XhoI and NheI sites of pND092, producing pND054
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expression in Aspergillus oryzae
gene agn1, sequence comparisons and phylogenetic analysis, heterologous expression in Schizosaccharomyces pombe agn1 null mutant strain 1252. Complementation of a Schizosaccharomyces pombe agn1DELTA strain with the Paracoccidioides brasiliensis AGN1 gene restores the wild-type phenotype, indicating functionality of the gene
gene Pc12g07500, heterologous expression in Saccharomyces cerevisiae strain IME208 confirms that Pc12g07500 encodes an active alpha-1,3 endoglucanase, secretion of the recombinant enzyme to culture medium; gene Pc12g13330, heterologous expression in Saccharomyces cerevisiae strain IME208 confirmes that Pc12g13330 encodes an inactive alpha-1,3 endoglucanase, secretion of the recombinant enzyme to culture medium
recombinant expression of wild-type and deletion mutant enzymes in Escherichia coli strain Rosetta-gami B (DE3), secretion of enzyme to the culture medium, recombinant expression as GFP-tagged proteins, overview
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tagged Agn2p at its carboxyl terminus with six histidines, expression in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
co-cultivation with Bacillus subtilis induces mutanase production from gene Pc12g07500 by 15fold; co-cultivation with Bacillus subtilis induces mutanase production from gene Pc12g13330 by 8fold
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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the enzyme has a potential as a caries preventive agent, due to the ability to remove the biofilms created by oral bacteria in vitro and to reduce plaque formation in vivo
pharmacology
additional information
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Agn2p participates in the endolysis of the ascus wall by hydrolysing its (1,3)-alpha-glucan, thereby assisting in the release of ascospores