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Information on EC 3.2.1.3 - glucan 1,4-alpha-glucosidase and Organism(s) Thermoanaerobacterium thermosaccharolyticum and UniProt Accession O85672

for references in articles please use BRENDA:EC3.2.1.3
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EC Tree
IUBMB 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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This record set is specific for:
Thermoanaerobacterium thermosaccharolyticum
UNIPROT: O85672
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Word Map
The taxonomic range for the selected organisms is: Thermoanaerobacterium thermosaccharolyticum
The enzyme appears in selected viruses and cellular organisms
Synonyms
glucoamylase, amyloglucosidase, acid maltase, maltase-glucoamylase, lysosomal alpha-glucosidase, maltase glucoamylase, gamma-amylase, glucose amylase, gam-1, glucoamylase p, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
1,4-alpha-D-glucan glucohydrolase
-
-
-
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acid maltase
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-
-
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alpha-1,4-glucan glucohydrolase
-
-
-
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amyloglucosidase
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-
-
-
exo-1,4-alpha-glucosidase
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-
-
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GAI
-
-
-
-
GAII
-
-
-
-
gamma-amylase
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-
-
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Glucan 1,4-alpha-glucosidase
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-
-
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glucoamylase
glucose amylase
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-
-
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lysosomal alpha-glucosidase
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-
-
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Meiotic expression upregulated protein 17
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-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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 hide
9032-08-0
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
starch + H2O
beta-D-glucose + ?
show the reaction diagram
-
-
-
?
amylopectin + H2O
D-glucose + ?
show the reaction diagram
-
-
beta-glucose
?
glycogen + H2O
glucose + ?
show the reaction diagram
-
-
beta-glucose
?
maltodextrin + H2O
beta-glucose + ?
show the reaction diagram
-
-
-
?
maltose + H2O
2 D-glucose
show the reaction diagram
-
-
-
-
?
maltose + H2O
2 glucose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
show the reaction diagram
-
-
-
-
?
starch + H2O
D-glucose + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
enzyme can attack alpha-1,4-glycosidic linkages and alpha-1,6-glycosidic linkages. The velocity of oligosaccharide hydrolysis decreases with a decrease in size of substrate
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
starch + H2O
beta-D-glucose + ?
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu2+
-
inhibitor and activator
Mn2+
-
inhibitor and activator
Zn2+
-
inhibitor and activator
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2,7-trihydroxyindolizidine
-
-
1,7-dihydroxyindolizidine
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-
2-Amino-2-ethyl-1,3-propanediol
-
-
beta-cyclodextrins
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above 5 mM, slight inhibition
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.01 - 20
maltose
additional information
starch
-
value is about 18 mg/ml
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 75
-
50°C: about 40% of maximal activity, 75°C: about 25% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
75000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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1 * 75000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
tGA crystals are grown at 24°C by the hanging-drop vapor diffusion method, 0.002 ml of a 14 mg/ml tGA solution in 20 mM Tris-HCl, pH 7.5, are mixed with the same volume of reservoier solution containing 14-16% polyethylene glycol 3350, 100 mm Tris-HCl, pH 8.0 and 200 mM Li2SO4, crystals of native tGA and tGA complexed with acarbose diffract to 2.2 A and 2.1 A resolution, respectively
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ultracentrifugation, anion exchange, gel permeation
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
food industry
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ethanol production, production of sugars
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Specka, U.; Mayer, F.; Antranikian, G.
Purification and properties of a thermoactive glucoamylase from Clostridium thermosacharolyticum
Appl. Environ. Microbiol.
57
2317-2323
1991
Thermoanaerobacterium thermosaccharolyticum
Manually annotated by BRENDA team
Aleshin, A.E.; Feng, P.H.; Honzatko, R.B.; Reilly, P.J.
Crystal structure and evolution of a prokaryotic glucoamylase
J. Mol. Biol.
327
61-73
2003
Thermoanaerobacterium thermosaccharolyticum (O85672), Thermoanaerobacterium thermosaccharolyticum
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team