3.2.1.48: sucrose alpha-glucosidase
This is an abbreviated version!
For detailed information about sucrose alpha-glucosidase, go to the full flat file.
Word Map on EC 3.2.1.48
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3.2.1.48
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border
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brush
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lactase
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enterocytes
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disaccharidase
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caco-2
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mucosal
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crypt
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jejunal
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starch
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maltase-glucoamylase
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brush-border
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glucoamylase
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maltose
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lactase-phlorizin
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ileum
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trehalase
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microvillus
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acarbose
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basolateral
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postprandial
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dipeptidyl
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villin
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suckling
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dipeptidylpeptidase
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malabsorption
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goblet
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3.2.1.20
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enterocyte-like
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isomaltose
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3.4.11.2
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intestine-specific
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carbohydrase
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small-intestinal
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aminopeptidase-n
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postconfluent
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crypt-villus
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paneth
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1-deoxynojirimycin
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bloating
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dextrin
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agriculture
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medicine
- 3.2.1.48
- border
-
brush
- lactase
- enterocytes
- disaccharidase
-
caco-2
- mucosal
-
crypt
- jejunal
- starch
- maltase-glucoamylase
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brush-border
- glucoamylase
- maltose
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lactase-phlorizin
- ileum
- trehalase
- microvillus
- acarbose
-
basolateral
-
postprandial
-
dipeptidyl
- villin
-
suckling
-
dipeptidylpeptidase
- malabsorption
-
goblet
-
3.2.1.20
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enterocyte-like
- isomaltose
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3.4.11.2
-
intestine-specific
-
carbohydrase
-
small-intestinal
- aminopeptidase-n
-
postconfluent
-
crypt-villus
-
paneth
- 1-deoxynojirimycin
-
bloating
- dextrin
- agriculture
- medicine
Reaction
Synonyms
alpha-glucosidase, glucosidase, sucrose alpha-, intestinal sucrase, isomaltase, More, PF0132, pro-SI, SI, sucrase, sucrase isomaltase, sucrase-invertase, sucrase-isomaltase, sucrase-isomaltase enzyme complex, sucrase/isomaltase, sucrose alpha-glucohydrolase, sucrose hydrolase, SUH
ECTree
3.2.1.48 sucrose alpha-glucosidaseAdvanced search results
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results (Inhibitors
Inhibitors on EC 3.2.1.48 - sucrose alpha-glucosidase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
D-glucose
22% inhibition at 0.7 mM, glucose product inhibition regulates the activities of both enzyme SI subunits
H+
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competitive inhibitor in the interaction of sucrase with sucrose and sodium
kotalanol
binding structure, strong structural conservation of -1 subsite residues, overview
Li+
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high concentration, 300 mM Li+, pH dependent inhibition, complete at pH 8
p-Nitrophenyl-alpha-glucoside
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competitive inhibitor, inhibits both sucrase and isomaltase
ranitidine
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noncompetitive. Ranitidine can bind to both free enzyme and enzyme-substrate complex, which is accompanied by reduction of emission intensity and red shift of fluorescence spectra
Tannic acid
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inhibition of brush border sucrase by polyphenols in mouse intestine. Sucrase inhibition by tannic acid is a pure K effect at acidic pH and uncompetitive type in the alkaline pH range
valienamine
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an aminocyclitol, isolated from the enzymolysis broth of validamycins, configuration is similar to alpha-D-glucose, IC50 in vitro is 1.17 mM, the inhibition is pH-dependent and competitive, 80% inhibition at 2.5 mM and pH 6.6
gallic acid
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inhibition of brush border sucrase by polyphenols in mouse intestine. Inhibition by gallic acid is a pure V effect at pH 5.0, which changes to mixed type at pH 7.2, and pure K effect at pH 8.5
Scopolamine
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i.e. hyoscine, is commonly used as an anticholinergic drug to relieve nausea, vomiting and dizziness of amotion sickness as well as recovery from anesthesia and surgery. It shows non-competitive inhibition at different concentrations of 0.6-3.6 mM
Tris
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concentration-dependent biphasic effect, first causing activation, fully competitive inhibition above pH 6.8, inhibition is stronger at alkaline pH values
Tris
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concentration-dependent biphasic effect, first causing activation, fully competitive inhibition above pH 6.8, inhibition is stronger at alkaline pH values
Tris
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concentration-dependent biphasic effect, first causing activation, fully competitive inhibition above pH 6.8, inhibition is stronger at alkaline pH values
additional information
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rhesus monkey rotavirus impairs expression and activity of the brush border-associated enzyme in Caco-2 cells, the inhibition is not due to virus-induced, Ca2+-dependent disassembly of the F-actin cytoskeleton, but to a mechanism involving cAMP protein kinase A, PKA, EC 2.7.11.11, signalling and hyperphosphorylation of cytokeratin 18, the effect is antagonized by PKA blockers, e.g. H-89
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additional information
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inhibition of mice sucrase by polyphenols is pH-dependent, and is associated with conformational modifications of the enzyme. At pH 4.8, the polyphenols inhibit sucrase activity by 85-96%, which is reduced to 51 and 64%, respectively, at pH 7.2. However, at pH 8.5, 60 and 76% inhibition of enzyme activity
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additional information
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compounds with alpha-glucosidase inhibitory activity are preliminarily screened and purified from ten different seaweeds (two green, four brown, and four red). The alpha-glucosidase inhibitory activity of the MeOH H2O (4:1, v/v) extract of Polyopes lancifolia at 5 mg/ml is highest at 52.2%, followed by Grateloupia elliptica (42.0%), Sargassum thunbergii (24.3%), and Grateloupia. lanceolata (22.0%) in decreasing order
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