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Information on EC 3.2.1.3 - glucan 1,4-alpha-glucosidase and Organism(s) Saccharomycopsis fibuligera and UniProt Accession Q8TFE5
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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.
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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: Saccharomycopsis fibuligera
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
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-
-
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acid maltase
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-
-
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alpha-1,4-glucan glucohydrolase
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-
-
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amyloglucosidase
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-
-
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exo-1,4-alpha-glucosidase
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-
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GAI
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-
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GAII
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-
-
-
gamma-amylase
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-
-
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Glucan 1,4-alpha-glucosidase
glucoamylase
glucose amylase
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-
-
-
lysosomal alpha-glucosidase
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-
-
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Meiotic expression upregulated protein 17
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-
-
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Glucan 1,4-alpha-glucosidase
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-
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glucoamylase
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-
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-
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
active site structure, catalytic residue is Tyr464, catalytic domain and raw starch binding site
Hydrolysis of terminal (1->4)-linked alpha-D-glucose residues successively from non-reducing ends of the chains with release of beta-D-glucose
active site structure, catalytic residue is Tyr464, catalytic domain and raw starch binding site
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
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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
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
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-
-
-
?
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
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 7.5
-
activity range, 75% of maximal activity at pH 4.8 and 6.8, profile overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 65
-
activity range, maximal activity at 50°C, 75% of maximal activity at 60°C, profile overview
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q8TFE5_SACFI
515
0
57423
TrEMBL
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
-
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
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
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
-
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant nonglycosylated enzyme, 10 mg/ml protein in 50 mM acetate, pH 5.4, with 15% PEG 8000, X-ray diffraction structure determination and analysis at 1.1-1.6 A resolution, modelling
purified recombinant nonglycosylated enzyme, 10 mg/ml protein in 50 mM acetate, pH 5.4, with 15% PEG 8000, X-ray diffraction structure determination and analysis at 1.1-1.6 A resolution, modelling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H447A
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
H447A/D450A
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
R15A
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
T462A
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
H447A
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
H447A/D450A
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
R15A
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
T462A
site-directed mutagenesis, structure analysis compared to the wild-type, crystal structure
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Saccharomyces cerevisiae strain AH22 medium by gel filtration and ion exchange chromatography to homogeneity
recombinant wild-type and mutant enzymes from Saccharomyces cerevisiae strain AH22 medium by gel filtration and ion exchange chromatography to homogeneity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzymes in Saccharomyces cerevisiae strain AH22, secretion of recombinant enzymes
expression of wild-type and mutant enzymes in Saccharomyces cerevisiae strain AH22, secretion of recombinant enzymes
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sauer, J.; Sigurskjold, B.W.; Christensen, U.; Frandsen, T.P.; Mirgorodskaya, E.; Harrison, M.; Roepstorff, P.; Svensson, B.
Glucoamylase: structure/function relationships, and protein engineering
Biochim. Biophys. Acta
1543
275-293
2000
Aspergillus awamori, Aspergillus niger, Saccharomycopsis fibuligera
Sevcik, J.; Hostinova, E.; Solovicova, A.; Gasperik, J.; Dauter, Z.; Wilson, K.S.
Structure of the complex of a yeast glucoamylase with acarbose reveals the presence of a raw starch binding site on the catalytic domain
FEBS J.
273
2161-2171
2006
Saccharomycopsis fibuligera (P08017), Saccharomycopsis fibuligera (Q8TFE5), Saccharomycopsis fibuligera, Saccharomycopsis fibuligera HUT 7212 (P08017), Saccharomycopsis fibuligera HUT 7212, Saccharomycopsis fibuligera IFO 0111 (Q8TFE5)
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)
Natalia, D.; Vidilaseris, K.; Satrimafitrah, P.; Ismaya, W.; Purka, P.; Permentier, H.; Fibriansah, G.; Puspasari, F.; Nurachman, Z.; Dijkstra, B.; Soemitro, S.
Biochemical characterization of a glucoamylase from Saccharomycopsis fibuligera R64
Biologia
66
27-32
2011
Saccharomycopsis fibuligera, Saccharomycopsis fibuligera R64
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