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Information on EC 3.2.1.20 - alpha-glucosidase and Organism(s) Homo sapiens and UniProt Accession O43451

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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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This record set is specific for:
Homo sapiens
UNIPROT: O43451
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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 alpha-glucosidase
-
maltase-glucoamylase
-
acid alpha-glucosidase
acid GAA
-
-
acid maltase
AGL
-
-
-
-
alglucosidase alfa
alpha-1,4-glucosidase
-
-
-
-
alpha-D-glucosidase
-
-
-
-
alpha-glucopyranosidase
-
-
-
-
alpha-glucosidase
alpha-glucoside hydrolase
-
-
-
-
glucoinvertase
-
-
-
-
glucosidoinvertase
-
-
-
-
glucosidosucrase
-
-
-
-
maltase
-
-
-
-
maltase glucoamylase
-
-
maltase-glucoamylase
myozyme
-
-
neutral alpha-glucosidase
-
-
recombinant human GAA
-
-
rhGAA
-
-
additional information
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-methylumbelliferyl-alpha-D-glucopyranoside + H2O
4-methylumbelliferone + alpha-D-glucose
show the reaction diagram
assay at pH 4.0, 37°C, reaction stopped by addition of glycine or sodium carbonate
-
-
?
dextrin + H2O
alpha-D-glucose + ?
show the reaction diagram
a mixture of shorter linear and branched dextrin chains is hydrolyzed at the nonreducing ends into glucose
-
-
?
starch + H2O
alpha-D-glucose
show the reaction diagram
1,4-alpha-D-glucooligosaccharide + H2O
alpha-D-glucose
show the reaction diagram
4-methylumbelliferyl alpha-D-glucopyranoside + H2O
4-methylumbelliferone + alpha-D-glucopyranose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl alpha-D-glucoside + H2O
4-methylumbelliferone + alpha-D-glucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-alpha-D-glucopyranoside + H2O
4-methylumbelliferol + alpha-D-glucose
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-alpha-D-glucopyranoside + H2O
4-methylumbelliferone + alpha-D-glucose
show the reaction diagram
-
assay at room temperature, 10 min incubation, 7.4 nM enzyme concentration
-
-
?
4-methylumbelliferyl-alpha-glucoside + H2O
4-methylumbelliferone + alpha-D-glucose
show the reaction diagram
4-nitrophenyl 2-deoxy-alpha-D-glucopyranoside + H2O
4-nitrophenol + 2-deoxy-alpha-D-glucose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
show the reaction diagram
-
assay at pH 6.8, 37°C, reaction stopped by adding of NaOH
-
-
?
4-nitrophenyl alpha-D-glucoside + H2O
4-nitrophenol + alpha-D-glucose
show the reaction diagram
-
-
-
-
?
glycogen + H2O
alpha-D-glucose
show the reaction diagram
glycogen + H2O
D-glucose + ?
show the reaction diagram
-
-
-
?
maltopentaose + H2O
alpha-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
-
-
-
-
?
maltotriitol + H2O
?
show the reaction diagram
-
-
-
-
?
maltotriose + H2O
maltose + D-glucose
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
show the reaction diagram
-
-
-
-
?
palatinose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
-
-
-
?
resorufin alpha-D-glucopyranoside + H2O
?
show the reaction diagram
-
assay at room temperature, 10 min incubation, 7.4 nM enzyme concentration
-
-
?
starch + H2O
alpha-D-glucose
show the reaction diagram
starch + H2O
D-glucose + ?
show the reaction diagram
-
gelatinized maize starch
-
-
?
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
starch + H2O
alpha-D-glucose
show the reaction diagram
one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion
-
-
?
1,4-alpha-D-glucooligosaccharide + H2O
alpha-D-glucose
show the reaction diagram
-
short glucose oligomers, substrate derived from starch by alpha-amylase activity, the enzyme is important in mucosal alpha-glucogenesis, MGAM primes and mucosal sucrase-isomaltase activity sustains and constrains prandial alpha-glucogenesis from starch oligomers, regulation mechanism, overview
-
-
?
glycogen + H2O
D-glucose + ?
show the reaction diagram
-
-
-
?
maltose + H2O
2 D-glucose
show the reaction diagram
-
-
-
-
?
additional information
?
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acarbose
bound to the active site primarily through side-chain interactions with its acarvosine unit, almost no interactions with its glycone rings, binding structure, overview
myricetin
potent inhibitor with high binding affinity for both N- and C-terminals of the enzyme. Molecular dynamics reveal that myricetin interacts in its stretched conformation through water-mediated interactions with the C-terminus and by normal hydrogen bonding with the N-terminus. Residue W1369 of the extended 21 amino acid residue helical loop of C-terminal plays a major role in myricetin binding
(2R,3S,4S)-1-[(2S,3S)-2,4-dihydroxy-3-(tridecyloxy)butyl]-3,4-dihydroxy-2-(hydroxymethyl)tetrahydrothiophenium
-
-
(2R,3S,4S)-1-[(2S,3S)-2,4-dihydroxy-3-methoxybutyl]-3,4-dihydroxy-2-(hydroxymethyl)tetrahydrothiophenium
-
-
(2R,3S,4S)-1-[(2S,3S)-3-(benzyloxy)-2,4-dihydroxybutyl]-3,4-dihydroxy-2-(hydroxymethyl)tetrahydrothiophenium
-
-
(2R,3S,4S)-1-[(2S,3S)-3-ethoxy-2,4-dihydroxybutyl]-3,4-dihydroxy-2-(hydroxymethyl)tetrahydrothiophenium
-
-
1-deoxynojirimycin
competitive inhibition, binds strongly to the enzyme
16-hydroxy-cleroda-3,13-dine-16,15-olide
-
25% inhibition at 0.1 mM
3'-(3-methylbut-2-enyl)-3',4',7-trihydroxyflavane
-
-
3'-O-methylponkoranol
-
inhibits the different subunits to different extents, with extraordinary selectivity for C-terminal subunit of the enzyme
3,4-dihydroxyisolonchocarpin
-
noncompetitive inhibition
4'-(4-toluenesulfonamide)-3,4-dihydroxychalcone
-
-
4'-amino-4-hydroxychalcone
-
-
4-hydroxyisolonchocarpin
-
noncompetitive inhibition
8-(1,1-dimethylallyl)-5'-(3-methylbut-2-enyl)-3',4',5,7-tetrahydroxyflanvonol
-
-
acarbose
-
-
actinodaphnine
-
26% inhibition at 0.1 mM
antroquinonol
-
7% inhibition at 0.1 mM
Berberine
-
16% inhibition at 0.1 mM
blintol
Brossoflurenone A
-
-
Brossoflurenone B
-
-
Broussochalcone A
-
noncompetitive inhibition
Broussochalcone B
-
noncompetitive inhibition
catechin
-
10% inhibition at 0.1 mM
conduritol B epoxide
-
active-site directed inhibitor
curcumin
-
60% inhibition at 0.1 mM
D-glucono-delta-lactone
-
-
de-O-sulfonated kotalanol
de-O-sulfonated ponkoranol
-
no inhibition of N-terminal subunit N2
de-O-sulfonated salacinol
-
-
docosanol
-
3% inhibition at 0.1 mM
eupafolin
-
-
fisetin
-
-
glycogen
-
competitive inhibition of hydrolysis of 4-methylumbelliferyl-alpha-D-glucopyranoside, non-competitive inhibition of hydrolysis of maltose
Kazinol A
-
-
kazinol B
-
-
Kazinol E
-
-
kotalanol
luteolin
-
-
maltose
maltotriose
methyl-alpha-D-glucopyranoside
-
no inhibition of maltose hydrolysis, competitive inhibition of glycogen hydrolysis
miglitol
-
-
Mn2+
-
-
myricetin
-
-
N-butyl-deoxynojirimycin
competitive inhibition
N-butyldeoxynojirimycin
-
-
N-ethyl-deoxynojirimycin
competitive inhibition
N-methyl-deoxynojirimycin
competitive inhibition
NEM
-
2 mM, 70% inhibition
Nojirimycin
-
-
papyriflavonol A
-
-
PCMB
-
-
quercetin
-
18% inhibition at 0.1 mM
salacinol
sucrose
-
no inhibition of maltose hydrolysis, competitive inhibition of glycogen hydrolysis
tetracosanol
-
1% inhibition at 0.1 mM
trehalose
-
no inhibition of maltose hydrolysis, competitive inhibition of glycogen hydrolysis
Tris
-
-
turanose
-
-
Zn2+
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-deoxynojirimycin
increases enzyme activity and protein levels in mutants
albumin
-
activates
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.4
4-methylumbelliferyl alpha-D-glucopyranoside
-
0.076
4-Methylumbelliferyl-alpha-D-glucopyranoside
-
-
2.1
4-methylumbelliferyl-alpha-glucoside
-
recombinant enzyme
30
glycogen
-
-
2.35
maltopentaose
-
-
1.59 - 10
maltose
3.1
maltotetraose
-
-
0.15
maltotriitol
-
-
2
maltotriose
-
-
11.11
p-nitrophenyl-alpha-D-glucopyranoside
-
-
0.166
resorufin alpha-D-glucopyranoside
-
-
15.4
starch
-
-
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00055
1-deoxynojirimycin
the Ki value is calculated
0.0462
3'-(3-methylbut-2-enyl)-3',4',7-trihydroxyflavane
-
-
0.000000055 - 0.0000005
3'-O-methylponkoranol
0.0081
3,4-dihydroxyisolonchocarpin
-
-
0.0097
4-hydroxyisolonchocarpin
-
-
0.0042
8-(1,1-dimethylallyl)-5'-(3-methylbut-2-enyl)-3',4',5,7-tetrahydroxyflanvonol
-
-
0.000009 - 0.062
acarbose
0.000013 - 0.00049
blintol
0.0121
Brossoflurenone A
-
-
0.0136
Brossoflurenone B
-
-
0.0072
Broussochalcone A
-
-
0.0162
Broussochalcone B
-
-
0.000026 - 0.000078
de-O-sulfonated kotalanol
0.000000043 - 0.000000096
de-O-sulfonated ponkoranol
0.0136
Kazinol A
-
-
0.0203
kazinol B
-
-
0.0049
Kazinol E
-
-
0.000064 - 0.00019
kotalanol
0.000211 - 0.001
miglitol
0.00474
N-butyl-deoxynojirimycin
the Ki value is calculated
0.0062
N-ethyl-deoxynojirimycin
the Ki value is calculated
0.00236
N-methyl-deoxynojirimycin
the Ki value is calculated
0.0023
papyriflavonol A
-
-
0.000058 - 0.000213
salacinol
additional information
additional information
-
9.8 mM for short glucose oligomers
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001
(2R,3S,4S)-1-[(2S,3S)-2,4-dihydroxy-3-(tridecyloxy)butyl]-3,4-dihydroxy-2-(hydroxymethyl)tetrahydrothiophenium
Homo sapiens
-
pH and temperature not specified in the publication
0.0053
(2R,3S,4S)-1-[(2S,3S)-2,4-dihydroxy-3-methoxybutyl]-3,4-dihydroxy-2-(hydroxymethyl)tetrahydrothiophenium
Homo sapiens
-
pH and temperature not specified in the publication
0.00044
(2R,3S,4S)-1-[(2S,3S)-3-(benzyloxy)-2,4-dihydroxybutyl]-3,4-dihydroxy-2-(hydroxymethyl)tetrahydrothiophenium
Homo sapiens
-
pH and temperature not specified in the publication
0.0017
(2R,3S,4S)-1-[(2S,3S)-3-ethoxy-2,4-dihydroxybutyl]-3,4-dihydroxy-2-(hydroxymethyl)tetrahydrothiophenium
Homo sapiens
-
pH and temperature not specified in the publication
0.0757
3'-(3-methylbut-2-enyl)-3',4',7-trihydroxyflavane
Homo sapiens
-
-
0.0191
3,4-dihydroxyisolonchocarpin
Homo sapiens
-
-
0.2689
4'-(4-toluenesulfonamide)-3,4-dihydroxychalcone
Homo sapiens
-
at pH 6.8 and 37°C
0.1937
4'-amino-4-hydroxychalcone
Homo sapiens
-
at pH 6.8 and 37°C
0.0123
4-hydroxyisolonchocarpin
Homo sapiens
-
-
0.0036
8-(1,1-dimethylallyl)-5'-(3-methylbut-2-enyl)-3',4',5,7-tetrahydroxyflanvonol
Homo sapiens
-
-
0.0000996
acarbose
Homo sapiens
-
at pH 6.8 and 37°C
0.0276
Brossoflurenone A
Homo sapiens
-
-
0.0333
Brossoflurenone B
Homo sapiens
-
-
0.0053
Broussochalcone A
Homo sapiens
-
-
0.0111
Broussochalcone B
Homo sapiens
-
-
0.008
de-O-sulfonated salacinol
Homo sapiens
-
pH and temperature not specified in the publication
0.048
eupafolin
Homo sapiens
-
at pH 6.8 and 37°C
0.0196
fisetin
Homo sapiens
-
at pH 6.8 and 37°C
0.012
Kazinol A
Homo sapiens
-
-
0.0263
kazinol B
Homo sapiens
-
-
0.0106
Kazinol E
Homo sapiens
-
-
0.0184
luteolin
Homo sapiens
-
at pH 6.8 and 37°C
0.0302
myricetin
Homo sapiens
-
at pH 6.8 and 37°C
0.0068 - 0.0092
N-butyldeoxynojirimycin
0.0021
papyriflavonol A
Homo sapiens
-
-
0.0214
quercetin
Homo sapiens
-
at pH 6.8 and 37°C
0.0052
salacinol
Homo sapiens
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23.5
-
-
4.72
4-methylumbelliferyl alpha-D-glucopyranoside as a substrate
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.8
-
acid alpha-glucosidase assay at
4
-
hydrolysis of glycogen or maltose, recombinant enzyme
4 - 4.5
-
hydrolysis of glycogen
4 - 5.5
-
4-methylumbelliferyl-alpha-glucoside
4.5
-
hydrolysis of maltose
4.5 - 5
-
hydrolysis of 4-methylumbelliferyl alpha-glucoside
5.6
-
hydrolysis of maltotriitol and potato starch
6.5 - 7.5
-
-
6.8
-
assay at
7
-
neutral alpha-glucosidase assay at
7.5
-
4-methylumbelliferyl-alpha-glucoside
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 7
-
pH 4.0: about 60% of maximal activity with potato starch as substrate, about 45% of maximal activity with maltotriitol as substrate, pH 7.0: about 70% of maximal activity with potato starch as substrate, about 65% of maximal activity with maltotriitol as substrate
5.5 - 8.5
-
pH 5.5: about 25% of maximal activity, alpha-glucosidase AB. About 30% of maximal activity, alpha-glucosidase C. pH 8.5: about 45% of maximal activity, alpha-glucosidase AB. About 70% of maximal activity, alpha-glucosidase C
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
additional information
-
assay at room temperature
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 4.6
-
for CHO cell-derived rhGAA
4.2 - 4.6
-
for CHO cell-derived tgGAA
4.6 - 4.9
-
for CHO cell-derived HP-GAA
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
Uniprot
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
small-intestinal brush-border epithelial cells
Manually annotated by BRENDA team
-
dried blood spot specimen from patients with infantile Pompe disease
Manually annotated by BRENDA team
-
fibroblasts
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is anchored to brush border epithelial cells
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
mutations in the gene of the enzyme result in reduced activity, effect is a lysosomal storage disorder, Pompe disease
malfunction
-
enzyme mutations cause accumulation of glycogen in lysosomes, resulting in Pompe disease
metabolism
-
the enzyme is responsible for the final step of starch hydrolysis
physiological function
-
the C-terminal subunit of maltase-glucoamylase assists alpha-amylase in digesting starch molecules and potentially may compensate for developmental or pathological amylase deficiencies
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
MGA_HUMAN
2753
1
312022
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
110000
150000
30000
-
gel filtration
33000
-
1 * 33000, SDS-PAGE
76000
-
mature recombinant enzyme, gel filtration
92000
-
alpha-glucosidase C, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 110000, recombinant enzyme, SDS-PAGE
dimer
-
-
monomer
-
1 * 33000, SDS-PAGE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
recombinant N-terminal catalytic subunit secreted from transformed S2 cells
glycoprotein
proteolytic modification
-
the 110000 Da precursor is an intrinsic membrane protein, which is transported into lysosomes after solubilization by proteolysis
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apoenzyme and enzyme complexed with acarbose, X-ray diffraction structure determination and anaylsis at 2.0 A and 1.9 A resolution, respectively
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A445P
increased activity, enzyme mutants responsive to 1-deoxynojirimycin
A610V
increased activity, enzyme mutants responsive to 1-deoxynojirimycin
E579K
increased activity, enzyme mutants responsive to 1-deoxynojirimycin
G377R
increased activity, enzyme mutants responsive to 1-deoxynojirimycin
G549R
increased activity, enzyme mutants responsive to 1-deoxynojirimycin
H612Q
increased activity, enzyme mutants responsive to 1-deoxynojirimycin
L552P
increased activity, enzyme mutants responsive to 1-deoxynojirimycin
M519V
increased activity, enzyme mutants responsive to 1-deoxynojirimycin
N470del
increased activity, enzyme mutants responsive to 1-deoxynojirimycin
P266S
increased activity, enzyme mutants responsive to 1-deoxynojirimycin
P285R
increased activity, enzyme mutants responsive to 1-deoxynojirimycin
P545L
increased activity, enzyme mutants responsive to 1-deoxynojirimycin
S529V
increased activity, enzyme mutants responsive to 1-deoxynojirimycin
V466G
increased activity, enzyme mutants responsive to 1-deoxynojirimycin
Y455F
increased activity, enzyme mutants responsive to 1-deoxynojirimycin
Y575S
increased activity, enzyme mutants responsive to 1-deoxynojirimycin
N513E
-
the mutation interferes with posttranslational modification and the intracellular transport of the alpha-glucosidase precursor
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 9
-
4°C, 24 h, stable
393316
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
15 min, stable up to
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
neutral alpha-glucosidase is less stable than acid alpha-glucosidase
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged C-terminal subunits ctMGAMN2 and ctMGAMN20 from Spodoptera frugiperda Sf9 cells by nickel affinity chromatography, recombinant His6-tagged N-terminal subunit ntMGAM from Drosophila S2 by cobalt affinity chromatography and ion exchange chromatography
-
recombinant N-terminally His-tagged N-terminal domain from Drosophila melanogaster S2 cells by copper affinity chromatography and ion exchange chromatography
-
rhGAA purified from the milk of transgenic Oryctolagus cuniculus
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in COS-7 cells
overexpression of the N-terminal catalytic subunit in Drosophila melanogaster S2 cells and secretion of the recombinant protein from the cells
expressed in Mus musculus
expression in Chinese hamster ovary K1 cells
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expression in mammary gland of transgenic mice
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N- and C-terminal catalytic subunits, expression of His6-tagged N-terminal subunit ntMGAM in Drosophila S2 cells, expression of His6-tagged C-terminal subunits ctMGAMN2 and ctMGAMN20 in Spodoptera frugiperda Sf9 cells
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produced in CHO cells (CHO-GAA). rhGAA purified from the milk of transgenic Oryctolagus cuniculus
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recombinant expression of N-terminally His-tagged N-terminal domain in Drosophila melanogaster S2 cells
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
potential treatment for Pompe disease
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tsuji, A.; Suzuki, Y.
Solubilization of membrane-bound acid alpha-glucosidase by proteolysis
Biochem. Biophys. Res. Commun.
151
1358-1363
1988
Homo sapiens
Manually annotated by BRENDA team
Minamiura, N.; Matoba, K.; Nishinaka, H.; Yamamoto, T.
Identity of alpha-glucosidase of human kidney with urine F-1 alpha-glucosidase
J. Biochem.
91
809-816
1982
Homo sapiens
Manually annotated by BRENDA team
Martiniuk, F.; Hirschhorn, R.
Characterization of neutral isozymes of human alpha-glucosidase: differences in substrate specificity, molecular weight and electrophoretic mobility
Biochim. Biophys. Acta
658
248-261
1981
Homo sapiens
Manually annotated by BRENDA team
Koster, J.F.; Slee, R.G.
Some properties of human liver acid alpha-glucosidase
Biochim. Biophys. Acta
482
89-97
1977
Homo sapiens
Manually annotated by BRENDA team
Chadalavada, D.M.; Sivakami, S.
Purification and biochemical characterisation of human placental acid alpha-glucosidase
Biochem. Mol. Biol. Int.
42
1051-1061
1997
Homo sapiens
Manually annotated by BRENDA team
Fuller, M.; van der Ploeg, A.; Reuser, A.J.J.; Anson, D.S.; Hopwood, J.J.
Isolation and characterisation of a recombinant, precursor form of lysosomal acid alpha-glucosidase
Eur. J. Biochem.
234
903-909
1995
Homo sapiens
Manually annotated by BRENDA team
Hermans, M.M.P.; Kroos, M.A.; van Beeumen, J.; Oostra, B.A.; Reuser, A.J.J.
Human lysosomal alpha-glucosidase. Characterization of the catalytic site
J. Biol. Chem.
266
13507-13512
1991
Homo sapiens
Manually annotated by BRENDA team
Hermans, M.M.P.; Wisselaar, H.A.; Kroos, M.A.; Oostra, B.A.; Reuser, A.J.J.
Human lysosomal alpha-glucosidase: functional characterization of the glycosylation sites
Biochem. J.
289
681-686
1993
Homo sapiens
-
Manually annotated by BRENDA team
Bijvoet, A.G.A.; Kroos, M.A.; Pieper, F.R.; van der Vliet, M.; de Boer, H.; van der Ploeg, A.T.; Verbeet, M.P.; Reuser, A.J.J.
Recombinant human acid alpha-glucosidase: high level production in mouse milk, biochemical characteristics, correction of enzyme deficiency in GSDII KO mice
Hum. Mol. Genet.
7
1815-1824
1998
Homo sapiens
Manually annotated by BRENDA team
Zhang, H.; Kallwass, H.; Young, S.P.; Carr, C.; Dai, J.; Kishnani, P.S.; Millington, D.S.; Keutzer, J.; Chen, Y.T.; Bali, D.
Comparison of maltose and acarbose as inhibitors of maltase-glucoamylase activity in assaying acid alpha-glucosidase activity in dried blood spots for the diagnosis of infantile Pompe disease
Genet. Med.
8
302-306
2006
Homo sapiens
Manually annotated by BRENDA team
Sim, L.; Quezada-Calvillo, R.; Sterchi, E.E.; Nichols, B.L.; Rose, D.R.
Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity
J. Mol. Biol.
375
782-792
2008
Homo sapiens (O43451)
Manually annotated by BRENDA team
Quezada-Calvillo, R.; Robayo-Torres, C.C.; Ao, Z.; Hamaker, B.R.; Quaroni, A.; Brayer, G.D.; Sterchi, E.E.; Baker, S.S.; Nichols, B.L.
Luminal substrate 'brake' on mucosal maltase-glucoamylase activity regulates total rate of starch digestion to glucose
J. Pediatr. Gastroenterol. Nutr.
45
32-43
2007
Homo sapiens
Manually annotated by BRENDA team
Yoshimizu, M.; Tajima, Y.; Matsuzawa, F.; Aikawa, S.; Iwamoto, K.; Kobayashi, T.; Edmunds, T.; Fujishima, K.; Tsuji, D.; Itoh, K.; Ikekita, M.; Kawashima, I.; Sugawara, K.; Ohyanagi, N.; Suzuki, T.; Togawa, T.; Ohno, K.; Sakuraba, H.
Binding parameters and thermodynamics of the interaction of imino sugars with a recombinant human acid alpha-glucosidase (alglucosidase alfa): insight into the complex formation mechanism
Clin. Chim. Acta
391
68-73
2008
Homo sapiens (P10253), Homo sapiens
Manually annotated by BRENDA team
Wan, L.; Lee, C.C.; Hsu, C.M.; Hwu, W.L.; Yang, C.C.; Tsai, C.H.; Tsai, F.J.
Identification of eight novel mutations of the acid alpha-glucosidase gene causing the infantile or juvenile form of glycogen storage disease type II
J. Neurol.
255
831-838
2008
Homo sapiens
Manually annotated by BRENDA team
McVie-Wylie, A.J.; Lee, K.L.; Qiu, H.; Jin, X.; Do, H.; Gotschall, R.; Thurberg, B.L.; Rogers, C.; Raben, N.; OCallaghan, M.; Canfield, W.; Andrews, L.; McPherson, J.M.; Mattaliano, R.J.
Biochemical and pharmacological characterization of different recombinant acid alpha-glucosidase preparations evaluated for the treatment of Pompe disease
Mol. Genet. Metab.
94
448-455
2008
Homo sapiens
Manually annotated by BRENDA team
Motabar, O.; Shi, Z.D.; Goldin, E.; Liu, K.; Southall, N.; Sidransky, E.; Austin, C.P.; Griffiths, G.L.; Zheng, W.
A new resorufin-based alpha-glucosidase assay for high-throughput screening
Anal. Biochem.
390
79-84
2009
Homo sapiens
Manually annotated by BRENDA team
Flanagan, J.J.; Rossi, B.; Tang, K.; Wu, X.; Mascioli, K.; Donaudy, F.; Tuzzi, M.R.; Fontana, F.; Cubellis, M.V.; Porto, C.; Benjamin, E.; Lockhart, D.J.; Valenzano, K.J.; Andria, G.; Parenti, G.; Do, H.V.
The pharmacological chaperone 1-deoxynojirimycin increases the activity and lysosomal trafficking of multiple mutant forms of acid alpha-glucosidase
Hum. Mutat.
30
1683-1692
2009
Homo sapiens (O43451)
Manually annotated by BRENDA team
Ryu, H.W.; Lee, B.W.; Curtis-Long, M.J.; Jung, S.; Ryu, Y.B.; Lee, W.S.; Park, K.H.
Polyphenols from Broussonetia papyrifera displaying potent alpha-glucosidase inhibition
J. Agric. Food Chem.
58
202-208
2010
Homo sapiens
Manually annotated by BRENDA team
Jones, K.; Sim, L.; Mohan, S.; Kumarasamy, J.; Liu, H.; Avery, S.; Naim, H.Y.; Quezada-Calvillo, R.; Nichols, B.L.; Pinto, B.M.; Rose, D.R.
Mapping the intestinal alpha-glucogenic enzyme specificities of starch digesting maltase-glucoamylase and sucrase-isomaltase
Bioorg. Med. Chem.
19
3929-3934
2011
Homo sapiens
Manually annotated by BRENDA team
Eskandari, R.; Jones, K.; Rose, D.R.; Pinto, B.M.
Selectivity of 3-O-methylponkoranol for inhibition of N- and C-terminal maltase glucoamylase and sucrase isomaltase, potential therapeutics for digestive disorders or their sequelae
Bioorg. Med. Chem. Lett.
21
6491-6494
2011
Homo sapiens
Manually annotated by BRENDA team
Roy, D.; Kumar, V.; Acharya, K.K.; Thirumurugan, K.
Probing the binding of Syzygium-derived alpha-glucosidase inhibitors with N- and C-terminal human maltase glucoamylase by docking and molecular dynamics simulation
Appl. Biochem. Biotechnol.
172
102-114
2014
Homo sapiens (O43451)
Manually annotated by BRENDA team
Lin, A.H.; Nichols, B.L.; Quezada-Calvillo, R.; Avery, S.E.; Sim, L.; Rose, D.R.; Naim, H.Y.; Hamaker, B.R.
Unexpected high digestion rate of cooked starch by the Ct-maltase-glucoamylase small intestine mucosal alpha-glucosidase subunit
PLoS ONE
7
e35473
2012
Homo sapiens
Manually annotated by BRENDA team
Li, J.P.; Zhang, X.Z.; Wu, J.G.; Liang, Z.Y.; Tian, Y.H.; Chen, C.; Tang, Y.G.; Zhang, F.B.
Seminal plasma neutral alpha-glucosidase activity as an early predictor of patency and natural pregnancy after microsurgical vasoepididymostomy
Andrologia
2019
e13235
2019
Homo sapiens
Manually annotated by BRENDA team
Jhong, C.; Riyaphan, J.; Lin, S.; Chia, Y.; Weng, C.
Screening alpha-glucosidase and alpha-amylase inhibitors from natural compounds by molecular docking in silico
Biofactors
41
242-251
2015
Homo sapiens
Manually annotated by BRENDA team
Schneider, J.L.; Balu-Iyer, S.V.
Phosphatidylserine converts immunogenic recombinant human acid alpha-glucosidase to a tolerogenic form in a mouse model of Pompe disease
J. Pharm. Sci.
105
3097-3104
2016
Homo sapiens (P10253)
Manually annotated by BRENDA team