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Information on EC 3.2.1.20 - alpha-glucosidase and Organism(s) Saccharolobus solfataricus and UniProt Accession P0CD66

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IUBMB Comments
This single entry covers a group of enzymes whose specificity is directed mainly towards the exohydrolysis of (1->4)-alpha-glucosidic linkages, and that hydrolyse oligosaccharides rapidly, relative to polysaccharide, which are hydrolysed relatively slowly, or not at all. The intestinal enzyme also hydrolyses polysaccharides, catalysing the reactions of EC 3.2.1.3 glucan 1,4-alpha-glucosidase and, more slowly, hydrolyses (1->6)-alpha-D-glucose links.
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Saccharolobus solfataricus
UNIPROT: P0CD66
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Word Map
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The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
maltotetraose
+
3
H2O
=
4
alpha-D-glucose
+
3
=
4
Synonyms
alpha-glucosidase, maltase, neutral alpha-glucosidase, alpha-d-glucosidase, alglucosidase alfa, intestinal maltase, intestinal alpha-glucosidase, alpha-1,4-glucosidase, recombinant human gaa, alpha-glucosidase ii, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
acid maltase
-
-
-
-
AGL
-
-
-
-
alpha-1,4-glucosidase
-
-
-
-
alpha-D-glucosidase
-
-
-
-
alpha-glucopyranosidase
-
-
-
-
alpha-glucosidase
-
-
-
-
alpha-glucoside hydrolase
-
-
-
-
glucoinvertase
-
-
-
-
glucosidoinvertase
-
-
-
-
glucosidosucrase
-
-
-
-
maltase
-
-
-
-
maltase-glucoamylase
-
-
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-glucose residues with release of D-glucose
show the reaction diagram
substrate recognition and catalytic mechanism, active site structure, residues R400, D87, W284, M321, F327 are involved in formation of the +1 subsite in the GH31 alpha-glucosidase substrate binding
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
alpha-D-glucoside glucohydrolase
This single entry covers a group of enzymes whose specificity is directed mainly towards the exohydrolysis of (1->4)-alpha-glucosidic linkages, and that hydrolyse oligosaccharides rapidly, relative to polysaccharide, which are hydrolysed relatively slowly, or not at all. The intestinal enzyme also hydrolyses polysaccharides, catalysing the reactions of EC 3.2.1.3 glucan 1,4-alpha-glucosidase and, more slowly, hydrolyses (1->6)-alpha-D-glucose links.
CAS REGISTRY NUMBER
COMMENTARY hide
9001-42-7
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
show the reaction diagram
-
-
-
?
glycogen + H2O
alpha-D-glucose
show the reaction diagram
recombinant enzyme
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
show the reaction diagram
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
show the reaction diagram
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
show the reaction diagram
-
-
-
-
?
dextrin + H2O
?
show the reaction diagram
-
-
-
-
?
isomaltose + H2O
2 alpha-D-glucose
show the reaction diagram
-
-
-
-
?
maltodextrin + H2O
alpha-D-glucose
show the reaction diagram
-
-
-
-
?
maltoheptaose + H2O
maltohexaose + D-glucose
show the reaction diagram
-
-
-
-
?
maltohexaose + H2O
maltopentaose + D-glucose
show the reaction diagram
-
-
-
-
?
maltose + H2O
2 D-glucose
show the reaction diagram
maltose + H2O
alpha-D-glucose + D-glucose
show the reaction diagram
-
-
-
-
?
maltotetraose + H2O
alpha-D-glucose
show the reaction diagram
-
-
-
-
?
maltotriose + H2O
maltose + D-glucose
show the reaction diagram
-
-
-
-
?
methyl-alpha-glucoside + H2O
methanol + alpha-D-glucose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
show the reaction diagram
-
-
-
-
?
starch + H2O
alpha-D-glucose
show the reaction diagram
-
no activity
-
-
?
additional information
?
-
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
maltose + H2O
alpha-D-glucose + D-glucose
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
n-Propanol
-
maximal stimulation at 7.5%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
4-nitrophenyl alpha-D-glucopyranoside
pH 4.5, 85°C, recombinant enzyme
64.9
glycogen
pH 5.5, 85°C, recombinant enzyme
3.2
p-nitrophenyl-alpha-D-glucoside
-
-
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
33
4-nitrophenyl alpha-D-glucopyranoside
pH 4.5, 85°C, recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18.8
-
purified recombinant enzyme, substrate 4-nitrophenyl alpha-D-glucopyranoside
35.6
-
purified recombinant enzyme, substrate maltose
6.66
-
purified recombinant enzyme, substrate maltohexaose
6.95
-
purified recombinant enzyme, substrate maltotriose
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5
recombinant enzyme, substrate glycogen
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 6.5
-
about 50% of maximal activity at pH 3.5 and at pH 6.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65 - 115
-
65°C: about 30% of maximal activity, 115°C: about 25% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme is involved in starch degradation
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
470000
recombinant enzyme, native PAGE
480000
recombinant enzyme, gel filtration
80500
x * 80500, about, sequence calculation
400000
-
gel filtration
80000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 80500, about, sequence calculation
hexamer
domain structure analysis, quarternary organization, comparison to alpha-xylosidase Yic1
pentamer
-
5 * or 4 * 80000, PAGE after treatment with 6 M guanidine hydrochloride
tetramer
-
4 * or 5 * 80000, PAGE after treatment with 6 M guanidine hydrochloride
tetramer or pentamer
-
x * 80000
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant wild-type and selenomethionine-labeled enzyme, hanging drop vapour diffusion method, hexameric crystal form, X-ray diffraction structure determination and analysis of the different crystal forms at 2.5 A resolution, structure modelling of domains, full-length enzyme, and active site
purified recombinant wild-type and selenomethionine-labeled enzyme, hanging drop vapour diffusion method, 2-5 mg/ml protein in 20 mM Tris-HCl, pH 7.5, and 20 mM NaCl, 0.002 ml protein solution is mixed with 0.003 ml reservoir solution and equilibrated against 1 ml reservoir solution, different compositions of the reservoir solution result in different crystal forms, overview, X-ray diffraction structure determination and analysis of the different crystal forms at 2.5-4.2 A resolution
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
protein production method optimization and evaluation of a microfiltration membrane bioreactor to improve the control of the concentration of key components in the growth of recombinant Escherichia coli strain BL21(DE3) cells expressing the enzyme, influence of medium composition and inducers, overview
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 8.5
-
completely stable
656561
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
105
-
half-life: 11 h
75
-
50% remaining activity after 40-70 h, half-life: 156 h
90
-
loss of 21.2% activity within 2 h
95
-
half-life: 3 h
98
-
half-life 160-180 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
proteolytic treatment of chemically denatured enzyme generated by guanidine hydrochloride pretreatment results in complete maltase degradation
-
treatment with trypsin or chymotrypsin at 30°C or proteinase K at 30°C or at 55°C for 20 min in 40 mM N-2-hydroxyethylpiperazine-N'-2-ethanesulfonic acid, pH 7.6, 8 mM magnesium acetate, 0.3 mM EDTA, 2 mM dithiothreitol, 10 mM sodium chloride and 20 mM potassium chloride has no effect
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ethanol
-
20 min in both 50% n-propanol and 25% ethanol increases maltase activity by over 50%
n-propanol
-
20 min in both 50% n-propanol and 25% ethanol increases maltase activity by over 50%
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and selenomethionine-labeled enzyme from Escherichia coli strain NF1830 by ammonium sulfate fractionation, ion exchange chromatography, and gel filtration
recombinant enzyme from Escherichia coli by selective and progressive thermal precipitation, 14.5fold to homogeneity
-
recombinant wild-type and selenomethionine-labeled enzyme from Escherichia coli by ammonium sulfate fractionation, ion exchange chromatography, and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene malA, DNA and amino acid sequence analysis, phylogenetic tree, overexpression of wild-type and selenomethionine-labeled enzyme in Escherichia coli strain NF1830
gene malA, library preparation, DNA and amino acid sequence determination and analysis, genetic structure and organization, sequences 3' to position -33, including a consensus archaeal TATA box, play an essential role in malA expression, detection of malA homologues, overview, phylogenetic analysis, expression of MalA in Escherichia coli revealing differences from the native enzyme in thermostability and electrophoretic behavior, overview
enzyme expression in Lactococcus lactis strain NZ9000, method optimization, overview
-
expression in Escherichia coli
expression of the thermostable, cytosolic enzyme in Escherichia coli strain BL21(DE3) using a microfiltration membrane bioreactor to improve the control of the concentration of key components in the growth of the cells, overview
-
gene malA, overexpression of wild-type and selenomethionine-labeled enzyme in Escherichia coli
-
gene SsGA, DNA sequence determination and analysis, expression in Escherichia coli BL21(DE3), cytosolic recombinant enzyme
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
glycosyl hydrolase production in Sulfolobuis solfataricus requires a trans-acting factor for wild-type levels of expression
induction when cells which were maintained in sucrose minimal medium with yeast extract are down shifted to sucrose minimal medium without yeast extract addtion
-
levels of malA mRNA are reduced 4fold as a consequence of yeast extract medium supplementation to sucrose minimal medium
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
target for therapy of type 2 diabetes, antitumor activites, antiviral activites
nutrition
-
usage in industrial processes to hydrolyze starch, saccharification step
synthesis
-
glucose production from maltodextrins employing a thermophilic immobilized cell biocatalyst in a packed-bed reactor, biotransformation of a commercial dextrin mixture at industrial concentrations (30–40%, w/v) into glucose at 75°C, achieving up to 98% conversion
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rolfsmeier, M.; Blum, P.
Purification and characterization of a maltase from the extremely thermophilic crenarchaeote Sulfolobus solfataricus
J. Bacteriol.
177
482-485
1995
Saccharolobus solfataricus
Manually annotated by BRENDA team
Martino, A.; Schiraldi, C.; Fusco, S.; Di Lernia, I.; Costabile, T.; Pellicano, T.; Marotta, M.; Generoso, M.; van der Oost, J.; Sensen, C.W.; Charlebois, R.L.; Moracci, M.; Rossi, M.; De Rosa, M.
Properties of the recombinant alpha-glucosidase from Sulfolobus solfataricus in relation to starch processing
J. Mol. Catal. B
11
787-794
2001
Saccharolobus solfataricus, Saccharolobus solfataricus MT-4 / DSM 5833
-
Manually annotated by BRENDA team
Chang, S.T.; Parker, K.N.; Bauer, M.W.; Kelly, R.M.
alpha-Glucosidase from Pyrococcus furiosus
Methods Enzymol.
330
260-269
2001
Pyrococcus furiosus, Pyrococcus woesei, Saccharolobus solfataricus, Thermococcus sp., Thermococcus sp. AN1, Saccharolobus solfataricus 98/2
Manually annotated by BRENDA team
Ernst, H.A.; Willemoes, M.; Lo Leggio, L.; Leonard, G.; Blum, P.; Larsen, S.
Characterization of different crystal forms of the alpha-glucosidase MalA from Sulfolobus solfataricus
Acta Crystallogr. Sect. F
61
1039-1042
2005
Saccharolobus solfataricus
Manually annotated by BRENDA team
Ernst, H.A.; Lo Leggio, L.; Willemoes, M.; Leonard, G.; Blum, P.; Larsen, S.
Structure of the Sulfolobus solfataricus alpha-glucosidase: implications for domain conservation and substrate recognition in GH31
J. Mol. Biol.
358
1106-1124
2006
Saccharolobus solfataricus (P0CD66), Saccharolobus solfataricus
Manually annotated by BRENDA team
Giuliano, M.; Schiraldi, C.; Marotta, M.R.; Hugenholtz, J.; De Rosa, M.
Expression of Sulfolobus solfataricus alpha-glucosidase in Lactococcus lactis
Appl. Microbiol. Biotechnol.
64
829-832
2004
Saccharolobus solfataricus
Manually annotated by BRENDA team
Schiraldi, C.; Martino, A.; Acone, M.; Di Lernia, I.; Di Lazzaro, A.; Marulli, F.; Generoso, M.; Carteni, M.; De Rosa, M.
Effective production of a thermostable alpha-glucosidase from Sulfolobus solfataricus in Escherichia coli exploiting a microfiltration bioreactor
Biotechnol. Bioeng.
70
670-676
2000
Saccharolobus solfataricus, Saccharolobus solfataricus MT-4 / DSM 5833
Manually annotated by BRENDA team
Rolfsmeier, M.; Haseltine, C.; Bini, E.; Clark, A.; Blum, P.
Molecular characterization of the alpha-glucosidase gene (malA) from the hyperthermophilic archaeon Sulfolobus solfataricus
J. Bacteriol.
180
1287-1295
1998
Saccharolobus solfataricus (P0CD66), Saccharolobus solfataricus
Manually annotated by BRENDA team
Hakamata, W.; Kurihara, M.; Okuda, H.; Nishio, T.; Oku, T.
Design and screening strategies for alpha-glucosidase inhibitors based on enzymological information
Curr. Top. Med. Chem.
9
3-12
2009
Apis mellifera, Aspergillus niger, Geobacillus stearothermophilus, Beta vulgaris, Saccharomyces cerevisiae, Oryza sativa, Zea mays, Saccharolobus solfataricus (P0CD66)
Manually annotated by BRENDA team
Haseltine, C.; Montalvo-Rodriguez, R.; Carl, A.; Bini, E.; Blum, P.
Extragenic pleiotropic mutations that repress glycosyl hydrolase expression in the hyperthermophilic archaeon Sulfolobus solfataricus
Genetics
152
1353-1361
1999
Saccharolobus solfataricus (D0KQM8), Saccharolobus solfataricus, Saccharolobus solfataricus 98/2 (D0KQM8)
Manually annotated by BRENDA team
Schiraldi, C.; Martino, A.; Costabile, T.; Generoso, M.; Marotta, M.; De Rosa, M.
Glucose production from maltodextrins employing a thermophilic immobilized cell biocatalyst in a packed-bed reactor
Enzyme Microb. Technol.
34
415-421
2004
Saccharolobus solfataricus, Saccharolobus solfataricus MT4
-
Manually annotated by BRENDA team
Haseltine, C.; Montalvo-Rodriguez, R.; Bini, E.; Carl, A.; Blum, P.
Coordinate transcriptional control in the hyperthermophilic archaeon Sulfolobus solfataricus
J. Bacteriol.
181
3920-3927
1999
Saccharolobus solfataricus
Manually annotated by BRENDA team