3.2.1.3: glucan 1,4-alpha-glucosidase
This is an abbreviated version!
For detailed information about glucan 1,4-alpha-glucosidase, go to the full flat file.
Word Map on EC 3.2.1.3
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3.2.1.3
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aspergillus
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niger
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glycogen
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alpha-amylase
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maltose
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corn
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awamori
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amylolytic
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pompe
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sucrase
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myopathy
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saccharification
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rhizopus
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lactase
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brush
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sucrase-isomaltase
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acarbose
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dextrin
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glycogenosis
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maltotriose
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amylopectin
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flour
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amylases
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starch-binding
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isomaltase
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infantile
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maltodextrins
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occidentalis
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bran
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disaccharidase
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food industry
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pullulanase
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liquefaction
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beta-cyclodextrins
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debranching
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beta-amylase
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carbohydrases
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3.2.1.20
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cassava
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maltooligosaccharides
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trehalase
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saccharify
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bioethanol
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medicine
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industry
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energy production
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paper production
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glucanotransferase
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nutrition
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maltoheptaose
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analysis
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maltotetraose
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biotechnology
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cgtase
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biofuel production
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isoamylase
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liquefied
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1-deoxynojirimycin
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starchy
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synthesis
- 3.2.1.3
- aspergillus
- niger
- glycogen
- alpha-amylase
- maltose
- corn
- awamori
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amylolytic
- pompe
- sucrase
- myopathy
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saccharification
- rhizopus
- lactase
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brush
- sucrase-isomaltase
- acarbose
- dextrin
- glycogenosis
- maltotriose
- amylopectin
- flour
- amylases
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starch-binding
- isomaltase
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infantile
- maltodextrins
- occidentalis
- bran
- disaccharidase
- food industry
- pullulanase
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liquefaction
- beta-cyclodextrins
-
debranching
- beta-amylase
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carbohydrases
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3.2.1.20
- cassava
- maltooligosaccharides
- trehalase
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saccharify
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bioethanol
- medicine
- industry
- energy production
- paper production
-
glucanotransferase
- nutrition
- maltoheptaose
- analysis
- maltotetraose
- biotechnology
- cgtase
- biofuel production
- isoamylase
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liquefied
- 1-deoxynojirimycin
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starchy
- synthesis
Reaction
Synonyms
1,4-alpha-D-glucan glucohydrolase, 1,4-alpha-D-glucan-glucohydrolase, acid maltase, alpha-(1,4)-D-glucan glucohydrolase, alpha-1,4-D-glucan glucohydrolase, alpha-1,4-glucan glucohydrolase, AMG, AmyA, AmyC, AmyD, amyloglucosidase, AnGA, APGA1, AtriGA15A, exo-1,4-alpha-D-glucan glucanohydrolase, exo-1,4-alpha-D-glucanohydrolase, exo-1,4-alpha-glucosidase, exo-amylase, GA, GA A, GA1, GA2, GAI, GAII, GAM, GAM-1, GAM-2, gamma-amylase, GAMP, GHF15 glucoamylase, GLA, Gla1, GlaA, GLL1, Glu-1.1, Glu-A, Glu1, GlucaM, Glucan 1,4-alpha-glucosidase, glucoamylase, glucoamylase 1, glucoamylase 2, glucoamylase C, glucoamylase D, glucoamylase G1, glucoamylase GA15A, glucoamylase P, glucose amylase, GluR, glycoamylase, HjGA, HrGA, lysosomal alpha-glucosidase, maltase glucoamylase, maltase-glucoamylase, maltooligosaccharide-metabolizing enzyme, Meiotic expression upregulated protein 17, MGA, MGAM, More, PDE_05527, PoGA, PoGA15A, PoxGA15A, raw starch-degrading enzyme, raw starch-degrading glucoamylase, RSDE, RSDG, SBD, Sga1, SSG, Sta1, Sta1p, starch-digesting glucoamylase, TagA, tGA, TmGLA, TmGlu1, TtcGA
ECTree
3.2.1.3 glucan 1,4-alpha-glucosidaseAdvanced search results
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results (General Information
General Information on EC 3.2.1.3 - glucan 1,4-alpha-glucosidase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
malfunction
metabolism
dynamic metabolic response of Aspergillus niger to glucose perturbation, regulatory mechanism for reduced glucoamylase production. Reduction of the total adenine nucleotides and major precursor amino acids indicate the upregulated RNA synthesis is required to produce stress proteins, and partially explains the drop of glucoamylase production when Aspergillus niger experiences a fluctuated glucose concentration environment, adenine nucleotides dynamic concentration profiles, overview
physiological function
additional information
evolution
the enzyme belongs to the glycosyl hydrolase family 15, GH15
evolution
the enzyme belongs to the glycosyl hydrolase family 15, GH15
evolution
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the enzyme belongs to the superfamily of CBM 20, phylogenetic tree
evolution
the enzyme is a member of the glycoside hydrolase family 15 (GH15)
evolution
the enzyme is a member of the glycoside hydrolase family 15 (GH15)
evolution
the enzyme is a member of the glycoside hydrolase family 15 (GH15)
evolution
the glucoamylase contains a catalytic domain belonging to glycosyl hydrolase family 15, GH15
evolution
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the enzyme is a member of the glycoside hydrolase family 15 (GH15)
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evolution
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the enzyme is a member of the glycoside hydrolase family 15 (GH15)
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evolution
Aspergillus japonicus Saito
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the enzyme belongs to the superfamily of CBM 20, phylogenetic tree
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evolution
Aspergillus tritici CGMCC 3.15694.3.2
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the glucoamylase contains a catalytic domain belonging to glycosyl hydrolase family 15, GH15
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evolution
Penicillium oxalicum GXU20
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the enzyme belongs to the glycosyl hydrolase family 15, GH15
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evolution
Aspergillus tritici WZ99
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the glucoamylase contains a catalytic domain belonging to glycosyl hydrolase family 15, GH15
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evolution
Tricholoma matsutake NBRC 30605
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the enzyme belongs to the glycosyl hydrolase family 15, GH15
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malfunction
the starch-binding domain (SBD) deletion analysis reveals that SBD plays a very important role in raw starch hydrolysis by the enzyme PoGA15A
malfunction
Penicillium oxalicum GXU20
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the starch-binding domain (SBD) deletion analysis reveals that SBD plays a very important role in raw starch hydrolysis by the enzyme PoGA15A
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physiological function
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enzyme hydrolyses glycogen to meet the energy requirements during asexual development
physiological function
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glucoamylase enzymes catalyze hydrolysis of alpha(1-4) glycosidic bonds to release D-glucose residues from the non-reducing ends of starch and oligosaccharides. Glucoamylase also has limited ability to release D-glucose residues by promoting hydrolysis of alpha(1-6) linkages of amylopectin
physiological function
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glucoamylase is an exo-acting enzyme that catalyses the production of beta-glucose from the non-reducing ends of amylose, amylopectin and glycogen
physiological function
glucoamylase is an exoglucohydrolase that primarily catalyzes the hydrolysis of alpha-1,4 glycosidic linkages in raw starch and soluble oligosaccharides to generate beta-D-glucose
physiological function
reduction of the total adenine nucleotides and major precursor amino acids indicate the upregulated RNA synthesis is required to produce stress proteins, and partially explains the drop of glucoamylase production when Aspergillus niger experiences a fluctuated glucose concentration environment
physiological function
Rhizopus arrhizus 99-880
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glucoamylase enzymes catalyze hydrolysis of alpha(1-4) glycosidic bonds to release D-glucose residues from the non-reducing ends of starch and oligosaccharides. Glucoamylase also has limited ability to release D-glucose residues by promoting hydrolysis of alpha(1-6) linkages of amylopectin
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physiological function
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glucoamylase is an exo-acting enzyme that catalyses the production of beta-glucose from the non-reducing ends of amylose, amylopectin and glycogen
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additional information
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the replacement of native beta-glucosidase Bgl1 signal peptide by that of Sta1, SPS-Bgl1, increases the production of the enzyme by about threefold without affecting the ratio between the values of activity associated to cells and free in the medium
additional information
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enzyme structure modelling and comparison of the structural model of Tetracladium sp. glucoamylase with the solved structure of the Hypocrea jecorina glucoamylase
additional information
the relative orientation between the carbohydrate-binding domain (CBM) and the catalytic domain is flexible, as the domains can adopt different orientations independently of ligand binding, suggesting a role as an anchor to increase the contact time and the relative concentration of substrate near the active site. The C-terminal CBM adopts the well known beta-sandwich motif, which is a hallmark of carbohydrate-binding modules
additional information
the relative orientation between the carbohydrate-binding domain (CBM) and the catalytic domain is flexible, as the domains can adopt different orientations independently of ligand binding, suggesting a role as an anchor to increase the contact time and the relative concentration of substrate near the active site. The C-terminal CBM adopts the well known beta-sandwich motif, which is a hallmark of carbohydrate-binding modules
additional information
the relative orientation between the carbohydrate-binding domain (CBM) and the catalytic domain is flexible, as the domains can adopt different orientations independently of ligand binding, suggesting a role as an anchor to increase the contact time and the relative concentration of substrate near the active site. The model of enzyme HrGA with two molecules in the asymmetric unit includes residues 29-616 and up to seven N-glycosylation sites and has acarbose bound in the active site. The C-terminal CBM adopts the well known beta-sandwich motif, which is a hallmark of carbohydrate-binding modules
additional information
the starch-binding domain (SBD) plays a very important role in raw starch hydrolysis by the enzyme PoGA15A
additional information
the thermostable glucoamylase from Aspergillus flavus strain NSH9 contains no starch binding domain (SBD)
additional information
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the thermostable glucoamylase from Aspergillus flavus strain NSH9 contains no starch binding domain (SBD)
additional information
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the replacement of native beta-glucosidase Bgl1 signal peptide by that of Sta1, SPS-Bgl1, increases the production of the enzyme by about threefold without affecting the ratio between the values of activity associated to cells and free in the medium
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additional information
-
the relative orientation between the carbohydrate-binding domain (CBM) and the catalytic domain is flexible, as the domains can adopt different orientations independently of ligand binding, suggesting a role as an anchor to increase the contact time and the relative concentration of substrate near the active site. The C-terminal CBM adopts the well known beta-sandwich motif, which is a hallmark of carbohydrate-binding modules
-
additional information
-
the relative orientation between the carbohydrate-binding domain (CBM) and the catalytic domain is flexible, as the domains can adopt different orientations independently of ligand binding, suggesting a role as an anchor to increase the contact time and the relative concentration of substrate near the active site. The C-terminal CBM adopts the well known beta-sandwich motif, which is a hallmark of carbohydrate-binding modules
-
additional information
Aspergillus flavus NSH9
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the thermostable glucoamylase from Aspergillus flavus strain NSH9 contains no starch binding domain (SBD)
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additional information
Penicillium oxalicum GXU20
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the starch-binding domain (SBD) plays a very important role in raw starch hydrolysis by the enzyme PoGA15A
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