3.2.1.59: glucan endo-1,3-alpha-glucosidase
This is an abbreviated version!
For detailed information about glucan endo-1,3-alpha-glucosidase, go to the full flat file.
Word Map on EC 3.2.1.59
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3.2.1.59
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mutans
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glucans
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dental
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trichoderma
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dextranase
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harzianum
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paenibacillus
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circulans
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caries
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streptococcal
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medicine
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water-insoluble
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protoplast-forming
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cariogenic
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schizophyllum
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saccharification
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glucanohydrolases
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endolysis
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laetiporus
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sobrinus
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endo-beta-1,3-glucanase
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curdlanolyticus
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sulphureus
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rosetta-gami
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pharmacology
- 3.2.1.59
- mutans
- glucans
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dental
- trichoderma
- dextranase
- harzianum
- paenibacillus
- circulans
- caries
- streptococcal
- medicine
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water-insoluble
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protoplast-forming
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cariogenic
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schizophyllum
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saccharification
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glucanohydrolases
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endolysis
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laetiporus
- sobrinus
- endo-beta-1,3-glucanase
- curdlanolyticus
- sulphureus
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rosetta-gami
- pharmacology
Reaction
Synonyms
Agl-FH1, Agl-FH2, Agl-KA, AglST2, Agn1p, Agn2, Agn2p, alpha-1,3 endoglucanase, alpha-1,3-glucanase, alpha-1,3-glucanase HF65, alpha-1,3-glucanase HF90, cariogenanase, cariogenase, endo alpha-1,3-glucanase, endo-(1,3)-alpha-glucanase, endo-(1-->3)-alpha-glucanase, endo-(1-3)-alpha-glucanase, endo-1,3-alpha-D-glucanase, endo-1,3-alpha-glucanase, endo-alpha-1,3-glucanase, FH11, glucanase, endo-1,3-alpha-mutanase, MuB, MuC1, MuC2, mutanase, MutAp
ECTree
3.2.1.59 glucan endo-1,3-alpha-glucosidaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.2.1.59 - glucan endo-1,3-alpha-glucosidase
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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
alpha-1,3-glucan + H2O
beta-D-glucose + ?
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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
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
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-
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?
glucan + H2O
isomaltose + nigerose + nigerotriose + oligosaccharides
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insoluble, sticky glucan of Streptococcus mutans
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?
alpha-1,3-glucan + H2O
?
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prepared from sucrose using Streptococcus mutans ATCC700610 glucosyltransferase I
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?
alpha-1,3-glucan + H2O
?
Niallia circulans KA-304
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prepared from sucrose using Streptococcus mutans ATCC700610 glucosyltransferase I
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-
?
alpha-1,3-glucan + H2O
?
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Agn2p-his shows high specificity for (1,3)-alpha-glucosidic linkages
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-
?
alpha-1,3-glucan + H2O
?
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the enzyme exhibits high specificity against alpha-1,3-glucan
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?
alpha-1,3-glucan + H2O
?
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the enzyme exhibits high specificity against alpha-1,3-glucan
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?
carboxymethyl alpha-1,3-glucan + H2O
?
the enzyme displays an endolytic cut pattern and high specificity for the soluble substrate, chemically modified from Paracoccidioides brasiliensis alpha-1,3-glucan
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-
?
carboxymethyl alpha-1,3-glucan + H2O
?
the enzyme displays an endolytic cut pattern and high specificity for the soluble substrate, chemically modified from Paracoccidioides brasiliensis alpha-1,3-glucan
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-
?
glucan + H2O
?
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transcription factors Sep1p and Ace2p regulate both eng1 and ang1 expression in a cell cycle-dependent manner. Agn1p acts in concert with Eng1p to achieve efficient cell separation, thereby exposing the secondary septa as the new ends of the daughter cells
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?
glucan + H2O
?
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hydrolyzes (1,3)-alpha-glucan predominantly into pentasaccharides
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?
glucan + H2O
nigerose + glucose
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glucan produced from sucrose by Streptococcus mutans
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?
nigeran + H2O
?
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10% activity compared to alpha-1,3-glucan
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?
nigeran + H2O
?
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10% activity compared to alpha-1,3-glucan
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-
?
additional information
?
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the enzyme is expressed during sexual development and mobilizes mutan. The enzyme is dispensable for sexual development
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?
additional information
?
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enzyme cleaves insoluble glucans from cariogenic streptococci such as Streptococcus mutans, Streptococcus sobrinus
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?
additional information
?
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no activity with starch, carboxymethyl-chitin, carboxymethyl-laminarin, carboxy-methylcellulose, and dextran T500
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?
additional information
?
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no activity with starch, carboxymethyl-chitin, carboxymethyl-laminarin, carboxy-methylcellulose, and dextran T500
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?
additional information
?
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no activity with starch, carboxymethyl-chitin, carboxymethyl-laminarin, carboxy-methylcellulose, and dextran T500
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?
additional information
?
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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
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?
additional information
?
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no activity of Agn2p with (1,3)-alpha-mannan, (1,3)-beta-glucan, (1,4)-alpha-glucan or (1,6)-alpha-glucan
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-
?
additional information
?
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no activity with cellulose, xylan, dextran, amylopectin, laminarin, and amylose
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?
additional information
?
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no activity with dextran, cellulose, amylose, amylopectin, and laminarin
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-
?
additional information
?
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no activity with dextran, cellulose, amylose, amylopectin, and laminarin
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?
additional information
?
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no activity with cellulose, xylan, dextran, amylopectin, laminarin, and amylose
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?
additional information
?
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the enzyme exhibits hydrolyzing activity against alpha-1,3-glucan in fungal cell walls
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?
additional information
?
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the enzyme recognizes tetra-saccharide as a minimal substrate and hydrolyzes it to trisaccharide and glucose which is released from the reducing end. For long-chain substrates, the enzyme cleaves random internal linkages after binding to the substrate. Subsequently, the enzyme hydrolyzes and releases glucose from the reducing end, and slides into the non-reducing end. The hydrolysis continues until trisaccharide remains
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?
