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Information on EC 3.2.1.3 - glucan 1,4-alpha-glucosidase and Organism(s) Saccharolobus solfataricus and UniProt Accession Q97ZD0

for references in articles please use BRENDA:EC3.2.1.3
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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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Saccharolobus solfataricus
UNIPROT: Q97ZD0
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The taxonomic range for the selected organisms is: Saccharolobus solfataricus
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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-
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amyloglucosidase
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-
-
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exo-1,4-alpha-glucosidase
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GAI
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-
-
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GAII
-
-
-
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gamma-amylase
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Glucan 1,4-alpha-glucosidase
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glucoamylase
glucose amylase
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lysosomal alpha-glucosidase
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Meiotic expression upregulated protein 17
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-
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-
REACTION
REACTION DIAGRAM
COMMENTARY hide
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
show the reaction diagram
reaction mechanism depends on the substrate, i.e. hydrolysis or transglycosylation, overview
PATHWAY SOURCE
PATHWAYS
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-
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
maltooligomers + H2O
? + beta-D-glucose
show the reaction diagram
substrate specificity
-
-
r
maltotriose + H2O
maltose + beta-D-glucose
show the reaction diagram
exoglycosidic hydrolysis of terminal glucose in forward reaction, preferred substrate, synthesis of isomaltose from beta-D-glucose in the reverse reaction with low activity
anomeric product configuration analysis at 80°C
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r
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + D-glucose
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
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stimulates activity
Ca2+
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stimulates activity
Co2+
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stimulates activity
Cu2+
-
inhibitor and activator
Fe2+
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stimulates activity
Mg2+
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stimulates activity
Mn2+
-
inhibitor and activator
Na+
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stimulates activity
Sn2+
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stimulates activity
Zn2+
-
inhibitor and activator
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,2,7-trihydroxyindolizidine
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1,7-dihydroxyindolizidine
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1-deoxynojirimycin
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2-Amino-2-ethyl-1,3-propanediol
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2-epilentiginosine
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4-chloromercuribenzoate
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alpha-cyclodextrin
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amino alcohols
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beta-cyclodextrin
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castanospermine
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gamma-cyclodextrin
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N-bromosuccinimide
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
56.3
purified recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 100
90% of maximal activity at 80°C, low activity at 100°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene ssg
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65000
-
SDS-PAGE, assumed
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme 80.9fold from Escherichia coli by heat treatment at 70°C, hydrophobic interaction chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ssg, phylogenetic analysis, expression in Escherichia coli
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
the enzyme is potentially useful in improvement of industrial starch processing by eliminating the need to adjust both pH and temperature
food industry
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ethanol production, production of sugars
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kim, M.S.; Park, J.T.; Kim, Y.W.; Lee, H.S.; Nyawira, R.; Shin, H.S.; Park, C.S.; Yoo, S.H.; Kim, Y.R.; Moon, T.W.; Park, K.H.
Properties of a novel thermostable glucoamylase from the hyperthermophilic archaeon Sulfolobus solfataricus in relation to starch processing
Appl. Environ. Microbiol.
70
3933-3940
2004
Saccharolobus solfataricus (Q97ZD0), Saccharolobus solfataricus
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