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
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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
results (
results (KM Value
KM Value on EC 3.2.1.3 - glucan 1,4-alpha-glucosidase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.14
maltoheptaose
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wild-type enzyme or mutant enzymes Gly183Lys or S184H
0.2
maltotriose
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15°C, pH 4.2, glucoamylase immobilized on macroporous silica
0.25
maltotriose
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recombinant enzyme expressed in Saccharomyces cerevisiae
0.89
maltotriose
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30°C, pH 4.2, glucoamylase immobilized on macroporous silica
0.017
starch
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30°C, pH 4.2, glucoamylase immobilized on macroporous silica
additional information
maltose
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Km value 0.029 mg/ml, pH 5.5, temperature not specified in the publication
additional information
additional information
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0.56 g/l for amylopectin from potato
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additional information
additional information
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6.8 mg/ml for maltose, 1.9 mg/ml for soluble starch
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additional information
additional information
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0.76 g/l for glycogen from oyster
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additional information
additional information
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0.97 g/l for soluble starch of Zulkowsky type
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additional information
additional information
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0.92% for soluble starch, glucoamylase M2
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additional information
additional information
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101 g/l for dextran
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additional information
additional information
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Km-values for the wild type enzyme and the mutant enzymes V181T/N182Y/G183A, P307A/T310V/Y312M/N313G and V181T/N182Y/G183A/P307A/T310V/Y312M/N313G
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additional information
additional information
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0.48 mg/ml for starch with glucoamylase II and III. 0.5 mg/ml for starch with glucoamylase I
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additional information
additional information
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0.741 mg/ml, hydrolysis of amylopectin with glucoamylase I. 0.667 mg/ml, hydrolysis of amylopectin with glucoamylase II. 0.455 mg/ml. Hydrolysis of amylose with glucoamylase I. 0.286 mg/ml, hydrolysis of amylose with glucoamylase II. 1.11 mg/ml, hydrolysis of glycogen with glucoamylase I. 1.54 mg/ml, hydrolysis of glycogen with glucoamylase II
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additional information
additional information
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4 g/l for maltose
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additional information
additional information
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3.8 g/l for pullulan
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additional information
additional information
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6.57 mg/ml for glucoamylase I with starch as substrate, 4.52 mg/ml for glucoamylase II with starch as substrate. 0.15 mg/ml for glucoamylase II with alpha-cyclodextrin as substrate, 2.0 mg/ml for glucoamylase II with beta-cyclodextrin as substrate
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additional information
additional information
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0.37 g/l for glycogen from rat liver
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additional information
additional information
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1.2 g/l for soluble starch
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additional information
additional information
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0.333 mg/ml for maltose
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additional information
additional information
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Km-values for C320A/E400C and the cysteinesulfinic acid derivative of C320A/E400C
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additional information
additional information
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kinetics, recombinant enzyme
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additional information
additional information
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kinetics and thermodynamics of wild-type and mutant enzymes
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additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
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kinetics and thermodynamics, substrate specificity for fermentation
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additional information
additional information
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ligand binding kinetics, wild-type enzyme and mutants
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additional information
additional information
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modelling of potato starch saccharification by commercial Aspergillus niger enzyme, kinetics
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additional information
additional information
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biphasic kinetics for maltodextrin degradation
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additional information
additional information
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kinetic analysis of glucoamylase-catalyzed hydrolysis of starch granules from various botanical sources, overview, Ko increases as the starch granule crystaline structure becomes dense
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additional information
additional information
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kinetics and thermodynamics of native and EDTA-coupled enzyme, overview
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additional information
additional information
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kinetics and thermodynamics of polyacrylamide gel-immobilized purified enzyme
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additional information
additional information
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kinetics of native enzyme, and aniline-coupled glucoamylase-1/ACG-1, aniline-coupled glucoamylase-7/ACG-7, and 13 min aniline-coupled glucoamylase-13/ACG-13, overview
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additional information
additional information
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kinetics of starch hydrolysis by AMG modeled for two different systems, free enzyme in aqueous solution and entrapped enzyme within vesicles in aqueous suspension, overview, Michaelis-Menten kinetic model with product inhibition for intrinsic kinetics
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additional information
additional information
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Km-value: 4.34 g/l with corn maltodextrin as a substrate for the N-terminal subunit of MGAM, Vmax: 7.51 U/mg with corn maltodextrin as a substrate for the N-terminal subunit of MGAM. Km-value: 7.01 g/l with alpha-limit dextrin as a substrate for the N-terminal subunit of MGAM, Vmax: 11.0 U/mg with alpha-limit dextrin as a substrate for the N-terminal subunit of MGAM. Km-value: 0.06 g/l with corn maltodextrin as a substrate for the immunoprecipitated maltase-glucoamylase. Km-value: 0.49 g/l with alpha-limit dextrin as a substrate for immunoprecipitated maltase-glucoamylase, Vmax: 11.0 U/mg with alpha-limit dextrin as a substrate for the immunoprecipitated maltase-glucoamylase
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additional information
additional information
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steady-state and pre-steady-state kinetic measurements using maltooligosacchrides as substrates, analysis and modelling, overview
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additional information
additional information
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thermodynamics and kinetics of starch hydrolysis, overview
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additional information
additional information
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Michaelis-Menten and Lineweaver-Burk kinetics
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additional information
additional information
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4.5 g/l with soluble starch
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additional information
additional information
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kinetic values Km and Vmax with soluble starch are 2.84 mg/ml and 239.2 U/ml, respectively, Lineweaver-Burk kinetics
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additional information
additional information
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KM values for amylopectin, glycogen and starch are 0.056, 0.062 and 0.065 mg/ml, respectively
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additional information
additional information
Michaelis-Menten kinetics, Km and Vmax of the glucoamylase are calculated as 15.02 g/l and 81.13 U/mg, pH 5.0, 45°C
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additional information
additional information
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Michaelis-Menten kinetics, Km and Vmax of the glucoamylase are calculated as 15.02 g/l and 81.13 U/mg, pH 5.0, 45°C
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additional information
additional information
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using raw cassava starch as substrate, the enzyme has a Km value of 0.72 mg/mL with Vmax of 0.01248 mmol/min/mg
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additional information
starch
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value is about 18 mg/ml
additional information
starch
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value is between 0.21 and 0.28 mg/ml
additional information
starch
Km value of wild-type is 34.5 mg/ml, pH 4.6, 70°C, of mutant T47A 61.1 mg/ml, mutant W48A 52.9 mg/ml
additional information
starch
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Km value of wild-type is 34.5 mg/ml, pH 4.6, 70°C, of mutant T47A 61.1 mg/ml, mutant W48A 52.9 mg/ml
additional information
starch
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Km value 0.094 mg/ml, pH 5.5, temperature not specified in the publication
