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Information on EC 3.2.1.3 - glucan 1,4-alpha-glucosidase and Organism(s) Homo sapiens and UniProt Accession O43451

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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Homo sapiens
UNIPROT: O43451
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The taxonomic range for the selected organisms is: Homo sapiens
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
maltase-glucoamylase
-
1,4-alpha-D-glucan glucohydrolase
-
-
-
-
acid maltase
-
-
-
-
alpha-1,4-glucan glucohydrolase
-
-
-
-
amyloglucosidase
-
-
-
-
exo-1,4-alpha-glucosidase
-
-
-
-
GAI
-
-
-
-
GAII
-
-
-
-
gamma-amylase
-
-
-
-
Glucan 1,4-alpha-glucosidase
-
-
-
-
glucoamylase
glucose amylase
-
-
-
-
lysosomal alpha-glucosidase
-
-
-
-
maltase glucoamylase
-
-
maltase-glucoamylase
-
-
Meiotic expression upregulated protein 17
-
-
-
-
MGAM
-
-
additional information
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
dextrin + 6 H2O
7 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
D-glucose + ?
show the reaction diagram
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl D-glucose
4-nitrophenol + D-glucose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
show the reaction diagram
-
-
-
-
?
alpha-limit dextrin + H2O
?
show the reaction diagram
-
-
-
-
?
maltodextrin + H2O
?
show the reaction diagram
-
corn maltodextrin
-
-
?
maltopentaose + H2O
?
show the reaction diagram
-
-
-
-
?
maltose + H2O
2 D-glucose
show the reaction diagram
-
-
-
-
?
maltose + H2O
?
show the reaction diagram
-
-
-
-
?
maltotetraose + H2O
?
show the reaction diagram
-
-
-
-
?
maltotriose + H2O
?
show the reaction diagram
-
-
-
-
?
starch + H2O
?
show the reaction diagram
starch + H2O
beta-D-glucose + ?
show the reaction diagram
starch + H2O
D-glucose + ?
show the reaction diagram
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
D-glucose + ?
show the reaction diagram
one of the two enzymes responsible for catalyzing the last glucose-releasing step in starch digestion
-
-
?
starch + H2O
beta-D-glucose + ?
show the reaction diagram
-
one of the key intestinal enzymes involved in the breakdown of glucose oligosaccharides in the small intestine
-
-
?
starch + H2O
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
(2S,3S,4R,5R)-1-((1S,2R,3S,4S)-3,4-dihydroxy-2-(hydroxymethyl)tetrahydro-1H-selenophenium-1-yl)-2,4,5,7-tetrahydroxyheptan-3-yl sulfate
-
a structure analogue of salacinol, synthesis, overview
(2S,3S,4R,5R)-1-((1S,2R,3S,4S)-3,4-dihydroxy-2-(hydroxymethyl)tetrahydro-1H-thiophenium-1-yl)-2,4,5,7-tetrahydroxyheptan-3-yl sulfate
-
a structure analogue of salacinol, synthesis, overview
(2S,3S,4S)-1-[(2S,3S,4S)-4-carboxy-2,3,4-trihydroxybutyl]-3,4-dihydroxy-2-methoxytetrahydrothiophenium
-
a salacinol derivative, salacinol is a sulfonium ion with an internal sulfate counterion, synthesis of a compound with the D-arabinitol configuration in the heterocyclic ring displayed by salacinol, overview
1,4-dideoxy-1,4-[(1-butyl)-(R)-episulfoniumylidene]-D-arabinitol chloride
-
-
1,4-dideoxy-1,4-[(1-hexyl)-(R)-episulfoniumylidene]-D-arabinitol chloride
-
-
1,4-dideoxy-1,4-[(1-octadecyl)-(R)-episulfoniumylidene]-D-arabinitol chloride
-
-
1,4-dideoxy-1,4-[(1-octyl)-(R)-episulfoniumylidene]-D-arabinitol chloride
-
-
1,4-dideoxy-1,4-[(1-tetradecyl)-(R)-episulfoniumylidene]-D-arabinitol chloride
-
-
1,4-dideoxy-1,4-[(1-tetradecyl)-(R)-episulfoniumylidene]-D-arabinitol triflate
-
-
1,4-dideoxy-1,4-[[(2S,3R,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]episelenoniumylidene]-D-arabinitol
-
a structure analogue of salacinol, synthesis, overview
1,4-dideoxy-1,4-[[(2S,3R,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]episulfoniumylidene]-D-arabinitol
-
a structure analogue of salacinol, synthesis, overview
1,4-dideoxy-1,4-[[(2S,3R,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]iminonium]-D-arabinitol
-
a structure analogue of salacinol, synthesis, overview
1,4-dideoxy-1,4-[[(2S,3S,4R,5R)-2,4,5,6-tetrahydroxy-3-(sulfooxy)hexyl]-(R)-epi-seleniumylidene]-D-arabinitol inner salt
-
-
1,4-dideoxy-1,4-[[(2S,3S,4R,5R)-2,4,5,6-tetrahydroxy-3-(sulfooxy)hexyl]-(R)-epi-sulfoniumylidene]-D-arabinitol inner salt
-
-
1,4-dideoxy-1,4-[[(2S,3S,4R,5R)-2,4,5,6-tetrahydroxy-3-(sulfooxy)hexyl]-(S)-epi-seleniumylidene]-D-arabinitol inner salt
-
-
1,4-dideoxy-1,4-[[(2S,3S,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]episelenoniumylidene]-D-arabinitol
-
a structure analogue of salacinol, synthesis, overview
1,4-dideoxy-1,4-[[(2S,3S,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]episulfoniumylidene]-D-arabinitol
-
a structure analogue of salacinol, synthesis, overview
1,4-dideoxy-1,4-[[(2S,3S,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]iminonium]-D-arabinitol
-
a structure analogue of salacinol, synthesis, overview
1,4-dideoxy-1,4-[[1-(3-methyl)-butyl]-(R)-episulfoniumylidene]-D-arabinitol chloride
-
-
1,4-dideoxy-1,4-[[1-(6-ethoxy)-hexyl]-(R)-episulfoniumylidene]-D-arabinitol chloride
-
-
1,4-dideoxy-1,4-[[1-(9-methoxy)-nonyl]-(R)-episulfoniumylidene]-D-arabinitol chloride
-
-
1-deoxynojirimycin
-
-
2-deoxy-1-ene-salacinol
-
synthesis, overview
2-deoxy-2-fluorosalacinol
-
synthesis, overview
5-(1,4-dideoxy-1,4-episulfoniumylidene-D-arabinitol)-5-deoxy-D-ribonate inner salt
-
-
5-(1,4-dideoxy-1,4-episulfoniumylidene-L-arabinitol)-5-deoxy-D-ribonate inner salt
-
-
acarbose
acarviostatin 103
-
component isolated from Streptomyces sp. strain PW638, also inhibitory to alpha-amylase, EC 3.2.1.1
blintol
ghavamiol
-
-
kotalanol
maltose
-
-
maltotetraose
-
-
maltotriose
-
-
miglitol
-
a salacinol derivative, inhibition of the isolated recombinant N-terminal catalytic domain
N-(7-oxadecyl)-1-deoxynojirimycin
-
-
N-butyl-deoxynojirimycin
-
-
N-decyl-deoxynojirimycin
-
-
N-methyl-deoxynojirimycin
-
-
salacinol
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05 - 6.66
maltopentaose
0.58 - 7.71
maltose
0.05 - 3
maltotetraose
0.22 - 4.6
maltotriose
additional information
additional information
-
Km-value: 4.34 g/l with corn maltodextrin as a substrate for the N-terminal subunit of MGAM, Vmax: 7.51 U/mg with corn maltodextrin as a substrate for the N-terminal subunit of MGAM. Km-value: 7.01 g/l with alpha-limit dextrin as a substrate for the N-terminal subunit of MGAM, Vmax: 11.0 U/mg with alpha-limit dextrin as a substrate for the N-terminal subunit of MGAM. Km-value: 0.06 g/l with corn maltodextrin as a substrate for the immunoprecipitated maltase-glucoamylase. Km-value: 0.49 g/l with alpha-limit dextrin as a substrate for immunoprecipitated maltase-glucoamylase, Vmax: 11.0 U/mg with alpha-limit dextrin as a substrate for the immunoprecipitated maltase-glucoamylase
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00014
(2S,3S,4R,5R)-1-((1S,2R,3S,4S)-3,4-dihydroxy-2-(hydroxymethyl)tetrahydro-1H-selenophenium-1-yl)-2,4,5,7-tetrahydroxyheptan-3-yl sulfate
-
pH 6.5, 37°C
0.00065
(2S,3S,4R,5R)-1-((1S,2R,3S,4S)-3,4-dihydroxy-2-(hydroxymethyl)tetrahydro-1H-thiophenium-1-yl)-2,4,5,7-tetrahydroxyheptan-3-yl sulfate
-
pH 6.5, 37°C
0.01
(2S,3S,4S)-1-[(2S,3S,4S)-4-carboxy-2,3,4-trihydroxybutyl]-3,4-dihydroxy-2-methoxytetrahydrothiophenium
-
pH 6.5, 37°C, derived from D-arabinitol, recombinant enzyme
0.032
1,4-dideoxy-1,4-[(1-butyl)-(R)-episulfoniumylidene]-D-arabinitol chloride
-
pH 6.5, 37°C
0.075
1,4-dideoxy-1,4-[(1-hexyl)-(R)-episulfoniumylidene]-D-arabinitol chloride
-
pH 6.5, 37°C
0.051
1,4-dideoxy-1,4-[(1-octadecyl)-(R)-episulfoniumylidene]-D-arabinitol chloride
-
pH 6.5, 37°C
0.051
1,4-dideoxy-1,4-[(1-octyl)-(R)-episulfoniumylidene]-D-arabinitol chloride
-
pH 6.5, 37°C
0.006
1,4-dideoxy-1,4-[(1-tetradecyl)-(R)-episulfoniumylidene]-D-arabinitol chloride
-
pH 6.5, 37°C
0.01
1,4-dideoxy-1,4-[(1-tetradecyl)-(R)-episulfoniumylidene]-D-arabinitol triflate
-
pH 6.5, 37°C
0.0001
1,4-dideoxy-1,4-[[(2S,3R,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]episelenoniumylidene]-D-arabinitol
-
pH 6.5, 37°C
0.00015
1,4-dideoxy-1,4-[[(2S,3R,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]episulfoniumylidene]-D-arabinitol
-
pH 6.5, 37°C
0.035
1,4-dideoxy-1,4-[[(2S,3R,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]iminonium]-D-arabinitol
-
pH 6.5, 37°C
0.00014
1,4-dideoxy-1,4-[[(2S,3S,4R,5R)-2,4,5,6-tetrahydroxy-3-(sulfooxy)hexyl]-(R)-epi-seleniumylidene]-D-arabinitol inner salt
-
pH 6.5, 37°C
0.00065
1,4-dideoxy-1,4-[[(2S,3S,4R,5R)-2,4,5,6-tetrahydroxy-3-(sulfooxy)hexyl]-(R)-epi-sulfoniumylidene]-D-arabinitol inner salt
-
pH 6.5, 37°C
0.0101
1,4-dideoxy-1,4-[[(2S,3S,4R,5R)-2,4,5,6-tetrahydroxy-3-(sulfooxy)hexyl]-(S)-epi-seleniumylidene]-D-arabinitol inner salt
-
pH 6.5, 37°C
0.0001
1,4-dideoxy-1,4-[[(2S,3S,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]episelenoniumylidene]-D-arabinitol
-
pH 6.5, 37°C
0.00017
1,4-dideoxy-1,4-[[(2S,3S,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]episulfoniumylidene]-D-arabinitol
-
pH 6.5, 37°C
0.008
1,4-dideoxy-1,4-[[(2S,3S,4R,5S)-2,4,5,6-tetrahydroxy-3-(sulfoxy)hexyl]iminonium]-D-arabinitol
-
pH 6.5, 37°C
0.067
1,4-dideoxy-1,4-[[1-(3-methyl)-butyl]-(R)-episulfoniumylidene]-D-arabinitol chloride
-
pH 6.5, 37°C
0.052
1,4-dideoxy-1,4-[[1-(6-ethoxy)-hexyl]-(R)-episulfoniumylidene]-D-arabinitol chloride
-
pH 6.5, 37°C
0.033
1,4-dideoxy-1,4-[[1-(9-methoxy)-nonyl]-(R)-episulfoniumylidene]-D-arabinitol chloride
-
pH 6.5, 37°C
0.006
2-deoxy-2-fluorosalacinol
-
-
0.000074 - 16
acarbose
0.00049
blintol
-
pH 6.5, 37°C
86.9
maltose
-
ntMGAM, N-terminal subunit of MGAM
0.58 - 67.6
maltotetraose
0.24 - 35
maltotriose
0.00019 - 0.021
salacinol
additional information
additional information
-
Ki-value: 12.7 g/l with corn maltodextrin as a substrate for the immunoprecipitated maltase-glucoamylase. Ki-value: 37.6 g/l with alpha-limit dextrin as a substrate for immunoprecipitated maltase-glucoamylase
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.15
2-deoxy-1-ene-salacinol
Homo sapiens
-
-
additional information
acarviostatin 103
Homo sapiens
-
IC50 value is 1.25 microg/ml, pH not specified in the publication, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 7
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
small intestinal
Manually annotated by BRENDA team
-
the enzyme is anchored in the membrane of small intestinal epithelial cells
Manually annotated by BRENDA team
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
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
105360
-
x * 105360, recombinant N-terminal catalytic domain, MALDI-TOF mass spectrometry
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 105360, recombinant N-terminal catalytic domain, MALDI-TOF mass spectrometry
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
recombinant N-terminal catalytic subunit secreted from transformed S2 cells
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant secreted His-tagged N-terminal subunit of human small intestinal enzyme from S2 cell culture medium by nickel affinity and anion exchange chromatography, followed by dialysis
-
secreted, recombinant N-terminal catalytic domain from Drosophila S2 cell culture supernatant by chelating resin and anion exchange chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of the N-terminal catalytic subunit in Drosophila melanogaster S2 cells and secretion of the recombinant protein from the cells
expression of active MGA N-terminal catalytic domain MGAnt, residues 87-955, in COS-1 cells, and overexpression of MGAnt in Drosophila S2 cells, secretion of recombinant proteins
-
expression of His-tagged N-terminal subunit of human small intestinal enzyme in S2 cells, secretion to the cell culture medium
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
enzyme inhibitors are very effective in controlling blood glucose levels, and thus are lead candidates for the treatment of type 2 diabetes
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Chen, W.; Sim, L.; Rose, D.R.; Pinto, B.M.
Synthesis of analogues of salacinol containing a carboxylate inner salt and their inhibitory activities against human maltase glucoamylase
Carbohydr. Res.
342
1661-1667
2007
Homo sapiens
Manually annotated by BRENDA team
Mohan, S.; Sim, L.; Rose, D.R.; Pinto, B.M.
Synthesis of S-alkylated sulfonium-ions and their glucosidase inhibitory activities against recombinant human maltase glucoamylase
Carbohydr. Res.
342
901-912
2007
Homo sapiens
Manually annotated by BRENDA team
Choubdar, N.; Sim, L.; Rose, D.R.; Pinto, B.M.
Synthesis of 2-deoxy-2-fluoro and 1,2-ene derivatives of the naturally occurring glycosidase inhibitor, salacinol, and their inhibitory activities against recombinant human maltase glucoamylase
Carbohydr. Res.
343
951-956
2008
Homo sapiens
Manually annotated by BRENDA team
Rossi, E.J.; Sim, L.; Kuntz, D.A.; Hahn, D.; Johnston, B.D.; Ghavami, A.; Szczepina, M.G.; Kumar, N.S.; Sterchi, E.E.; Nichols, B.L.; Pinto, B.M.; Rose, D.R.
Inhibition of recombinant human maltase glucoamylase by salacinol and derivatives
FEBS J.
273
2673-2683
2006
Homo sapiens
Manually annotated by BRENDA team
Ao, Z.; Quezada-Calvillo, R.; Sim, L.; Nichols, B.L.; Rose, D.R.; Sterchi, E.E.; Hamaker, B.R.
Evidence of native starch degradation with human small intestinal maltase-glucoamylase (recombinant)
FEBS Lett.
581
2381-2388
2007
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), Homo sapiens
Manually annotated by BRENDA team
Nasi, R.; Sim, L.; Rose, D.R.; Pinto, B.M.
New chain-extended analogues of salacinol and blintol and their glycosidase inhibitory activities. Mapping the active-site requirements of human maltase glucoamylase
J. Org. Chem.
72
180-186
2007
Homo sapiens
Manually annotated by BRENDA team
Liu, H.; Nasi, R.; Jayakanthan, K.; Sim, L.; Heipel, H.; Rose, D.R.; Pinto, B.M.
New synthetic routes to chain-extended selenium, sulfur, and nitrogen analogues of the naturally occurring glucosidase inhibitor salacinol and their inhibitory activities against recombinant human maltase glucoamylase
J. Org. Chem.
72
6562-6572
2007
Homo sapiens
Manually annotated by BRENDA team
Quezada-Calvillo, R.; Sim, L.; Ao, Z.; Hamaker, B.R.; Quaroni, A.; Brayer, G.D.; Sterchi, E.E.; Robayo-Torres, C.C.; Rose, D.R.; Nichols, B.L.
Luminal starch substrate "brake" on maltase-glucoamylase activity is located within the glucoamylase subunit
J. Nutr.
138
685-692
2008
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), Homo sapiens
Manually annotated by BRENDA team
Meng, P.; Xie, C.; Geng, P.; Qi, X.; Zheng, F.; Bai, F.
Inhibitory effect of components from Streptomyces species on alpha-glucosidase and alpha-amilase of different origin
Prikl. Biokhim. Mikrobiol.
49
181-189
2013
Homo sapiens
Manually annotated by BRENDA team