Any feedback?
Information on EC 3.2.1.3 - glucan 1,4-alpha-glucosidase and Organism(s) Aspergillus oryzae and UniProt Accession P36914
for references in articles please use BRENDA:EC3.2.1.3Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.2.1.3 glucan 1,4-alpha-glucosidaseIUBMB Comments
Most forms of the enzyme can rapidly hydrolyse 1,6-alpha-D-glucosidic bonds when the next bond in the sequence is 1,4, and some preparations of this enzyme hydrolyse 1,6- and 1,3-alpha-D-glucosidic bonds in other polysaccharides. This entry covers all such enzymes acting on polysaccharides more rapidly than on oligosaccharides. EC 3.2.1.20 alpha-glucosidase, from mammalian intestine, can catalyse similar reactions.
Specify your search results
Word Map
- 3.2.1.3
- aspergillus
- niger
- glycogen
- alpha-amylase
- maltose
- corn
- awamori
-
amylolytic
- pompe
- sucrase
- myopathy
-
saccharification
- rhizopus
- lactase
-
brush
- sucrase-isomaltase
- acarbose
- dextrin
- glycogenosis
- maltotriose
- amylopectin
- flour
- amylases
-
starch-binding
- isomaltase
-
infantile
- maltodextrins
- occidentalis
- bran
- disaccharidase
- food industry
- pullulanase
-
liquefaction
- beta-cyclodextrins
-
debranching
- beta-amylase
-
carbohydrases
-
3.2.1.20
- cassava
- maltooligosaccharides
- trehalase
-
saccharify
-
bioethanol
- medicine
- industry
- energy production
- paper production
-
glucanotransferase
- nutrition
- maltoheptaose
- analysis
- maltotetraose
- biotechnology
- cgtase
- biofuel production
- isoamylase
-
liquefied
- 1-deoxynojirimycin
-
starchy
- synthesis
The taxonomic range for the selected organisms is: Aspergillus oryzae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
glucoamylase, amyloglucosidase, acid maltase, maltase-glucoamylase, lysosomal alpha-glucosidase, maltase glucoamylase, gamma-amylase, glucose amylase, gam-1, glucoamylase p, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1,4-alpha-D-glucan glucohydrolase
-
-
-
-
acid maltase
-
-
-
-
alpha-1,4-glucan glucohydrolase
-
-
-
-
amyloglucosidase
exo-1,4-alpha-glucosidase
-
-
-
-
GAI
-
-
-
-
GAII
-
-
-
-
gamma-amylase
Glucan 1,4-alpha-glucosidase
-
-
-
-
glucoamylase
glucose amylase
-
-
-
-
lysosomal alpha-glucosidase
-
-
-
-
Meiotic expression upregulated protein 17
-
-
-
-
amyloglucosidase
-
-
-
-
gamma-amylase
-
-
-
-
glucoamylase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
cleavage of alpha-1,4-linkages is preferred to cleavage of alpha-1,6-linkages
-
SYSTEMATIC NAME
IUBMB Comments
4-alpha-D-glucan glucohydrolase
Most forms of the enzyme can rapidly hydrolyse 1,6-alpha-D-glucosidic bonds when the next bond in the sequence is 1,4, and some preparations of this enzyme hydrolyse 1,6- and 1,3-alpha-D-glucosidic bonds in other polysaccharides. This entry covers all such enzymes acting on polysaccharides more rapidly than on oligosaccharides. EC 3.2.1.20 alpha-glucosidase, from mammalian intestine, can catalyse similar reactions.
CAS REGISTRY NUMBER
COMMENTARY
9032-08-0
-
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
methyl-alpha-D-glucoside + H2O
methanol + alpha-D-glucose
-
no activity
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
-
-
-
-
?
additional information
?
-
-
different regulation mechanisms, the regulation is influenced by carbohydrate degradation and consumption under different culture conditions, overview
-
-
?
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
beta-D-glucose + ?
-
the enzyme hydrolyzes alpha-1,4 glycosidic linkages in raw, sparsely soluble or soluble starches and related oligosaccharides with the inversion of the anomeric configuration to produce beta-glucose
-
-
?
starch + H2O
glucose + ?
-
soluble
beta-glucose and maltooligosaccharides
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme contains 7 subsites for substrate binding, subsite affinities
-
-
?
NATURAL SUBSTRATE
NATURAL 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
starch + H2O
beta-D-glucose + ?
-
the starch binding domain of glucoamylase plays an active role in hydrolyzing raw starch and supports the enzyme adsorption to the cell wall where local increase of enzyme concentration may result in enhanced glucose flow to the cell
-
-
?
starch + H2O
starch + beta-D-glucose
-
the enzyme is required for degradation of raw starch
-
-
?
additional information
?
-
-
different regulation mechanisms, the regulation is influenced by carbohydrate degradation and consumption under different culture conditions, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
0.48 mg/ml for starch with glucoamylase II and III. 0.5 mg/ml for starch with glucoamylase I
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 6
-
pH 3.0: about 60% of maximal activity, pH 6.0: about 55% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35 - 60
-
35°C: about 50% of maximal activity, 60°C: about 90% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
high enzyme expression in solid-state fermentation on surface of wheat-based solid medium or wheat kernels, evaluation of culture conditions, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
54000
68400
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
additional information
-
the enzyme consists of a catalytic domain and a starch binding domain connected by an O-glycosylated peptide linker located at the N-terminus, the enzyme contains 7 subsites for substrate binding
additional information
-
fungal glucoamylases contain up to 7 subsites for substrate binding with highly varying affinity, the enzymes have two domains, namely a catalytic domain and a starch binding domain, the two domains are connected by an O-glycosylated polypeptide linker located at the N-terminus
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
alpha-D-mannopyranose is the dominant sugar present - about 91 residues. Hexosamine is also present as a minor component, 2.6% of the total carbohydrate. 41 alpha-D-mannopyranose residues are O-2 and O-3 glycosylated and 17 alpha-D-mannopyranose residues are involved in O-4 glycosylation
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biofuel production
the sake yeast strains constructed in this study are expected to produce bioethanol from starchy materials such as corn. Furthermore, to improve the efficiency of hydrolysis, a combination of sake yeast and various enzymes that cleave alpha-glucoside bonds shall be used
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ono, K.; Shigeta, S.; Oka, S.
Effective purification of glucoamylase in Koji, a solid culture of Aspergillus oryzae on steamed rice, by affinity chromatography using an immobilized acarbose (BAY g-5421)
Agric. Biol. Chem.
52
1707-1714
1988
Aspergillus oryzae
-
Kleinman, M.J.; Wilkinson, A.E.; Wright, I.P.; Evans, I.H.; Bevan, E.A.
Purification and properties of an extracellular glucoamylase from a diastatic strain of Saccharomyces cerevisiae
Biochem. J.
249
163-170
1988
Aspergillus oryzae, Saccharomyces cerevisiae, Rhizopus sp., Saccharomyces cerevisiae 1ab
Carter, R.D.; Hu, S.; Dill, K.
13C n.m.r. studies of the carbohydrate portion of glucoamylase from Aspergillus oryzae
Int. J. Biol. Macromol.
9
269-272
1987
Aspergillus oryzae
-
Manjunath, P.; Shenoy, B.C.; Raghavendra Roa, M.R.
Fungal glucoamylases
J. Appl. Biochem.
5
235-260
1983
Aspergillus awamori, Aspergillus candidus, Aspergillus foetidus, Aspergillus niger, Aspergillus oryzae, Aspergillus phoenicis, Acremonium charticola, Amorphotheca resinae, Coniophora cerebella, Endomyces sp., Thermomyces lanuginosus, Pyricularia grisea, Mucor rouxianus, Rhizopus arrhizus
Mitsue, T.; Saha, B.C.; Ueda, S.
Glucoamylase of Aspergillus oryzae cultured on steamed rice
J. Appl. Biochem.
1
410-422
1979
Aspergillus oryzae
-
Razzaque, A.; Ueda, S.
Glucoamylase of Aspergillus oryzae
J. Ferment. Technol.
56
296-302
1978
Aspergillus oryzae
-
te Biesebeke, R.; van Biezen, N.; de Vos, W.M.; van den Hondel, C.A.; Punt, P.J.
Different control mechanisms regulate glucoamylase and protease gene transcription in Aspergillus oryzae in solid-state and submerged fermentation
Appl. Microbiol. Biotechnol.
67
75-82
2005
Aspergillus oryzae
Norouzian, D.; Akbarzadeh, A.; Scharer, J.M.; Moo Young, M.
Fungal glucoamylases
Biotechnol. Adv.
24
80-85
2005
Aspergillus awamori, Aspergillus foetidus, Aspergillus niger, Aspergillus oryzae, Aspergillus phoenicis, Aspergillus terreus, Mucor javanicus, Neurospora crassa, Rhizopus arrhizus, Rhizopus niveus, Rhizopus microsporus var. oligosporus, Mycothermus thermophilus, Trichoderma reesei, Mucor rouxians, Arthrobotrys amerospora, Monascus kaoliang, Monascus kaoliang F-1, Aspergillus awamori X-100, Aspergillus terreus NA-170, Aspergillus niger NRRL 330, Aspergillus terreus NA-770
Kotaka, A.; Sahara, H.; Hata, Y.; Abe, Y.; Kondo, A.; Kato-Murai, M.; Kuroda, K.; Ueda, M.
Efficient and direct fermentation of starch to ethanol by sake yeast strains displaying fungal glucoamylases
Biosci. Biotechnol. Biochem.
72
1376-1379
2008
Rhizopus arrhizus (P07683), Aspergillus oryzae (P36914), Aspergillus oryzae
Kumar, P.; Satyanarayana, T.
Microbial glucoamylases: characteristics and applications
Crit. Rev. Biotechnol.
29
225-255
2009
Aspergillus fumigatus, Aspergillus nidulans, Aspergillus niger, Aspergillus oryzae, Aspergillus phoenicis, Aspergillus sp., Aspergillus terreus, Aureobasidium pullulans, Saccharomyces cerevisiae, Moesziomyces antarcticus, Cephalosporium eichhorniae, Thermochaetoides thermophila, Thermoanaerobacter thermohydrosulfuricus, Thermoanaerobacterium thermosaccharolyticum, Curvularia lunata, Saccharomycopsis fibuligera, Endomycopsis fibuligera, Fusarium solani, Thermomyces lanuginosus, Humicola sp., Monascus sp. (in: Fungi), Mucor circinelloides, Mucor javanicus, Neurospora crassa, Paecilomyces variotii, Rhizopus arrhizus, Rhizopus sp., Saccharomyces cerevisiae 'var. diastaticus', Schwanniomyces castellii, Mycothermus thermophilus, Saccharolobus solfataricus, Thermoplasma acidophilum, Trichoderma reesei, Lactobacillus amylovorus, Thielaviopsis paradoxa, Thermomucor indicae-seudaticae, Picrophilus torridus, Arthrobotrys amerospora, Lentinula edodes L-54, Aspergillus awamori (Q12537)
EXTERNAL LINKS (specific for EC-Number 3.2.1.3)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
