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1,6-di-O-alpha-D-glucopyranosyl-D-fructofuranose + H2O
alpha-D-glucose + D-fructose
-
99% cleavage compared to 1,6-di-O-alpha-D-glucopyranosyl-D-fructofuranose
-
-
?
1-O-alpha-D-glucopyranosyl-D-glucitol + H2O
alpha-D-glucose + D-glucitol
-
68% cleavage compared to 1-O-alpha-D-glucopyranosyl-D-glucitol
-
-
?
1-O-alpha-D-glucopyranosyl-D-mannitol + H2O
alpha-D-glucose + D-mannitol
-
25% cleavage compared to 1-O-alpha-D-glucopyranosyl-D-mannitol
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
?
4-nitrophenyl-alpha-D-glucoside + H2O
4-nitrophenol + alpha-D-glucose
-
-
-
?
6-bromo-2-naphthyl-alpha-D-glucoside + H2O
6-bromonaphthol + alpha-D-glucose
-
-
-
?
6-O-alpha-D-glucopyranosyl-D-glucitol + H2O
alpha-D-glucose + D-glucitol
-
35% cleavage compared to 6-O-alpha-D-glucopyranosyl-D-glucitol
-
-
?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-fructofuranose + H2O
alpha-D-glucose + D-fructose
-
97% cleavage compared to alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-fructofuranose
-
-
?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-fructopyranose + H2O
alpha-D-glucose + D-fructose
-
92% cleavage compared to alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-fructopyranose
-
-
?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-glucopyranose + H2O
alpha-D-glucose
-
-
-
-
?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-glucopyranosyl-(1-6)-D-fructofuranose + H2O
alpha-D-glucose + D-fructose
-
100% cleavage compared to alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-glucopyranosyl-(1-6)-D-fructofuranose
-
-
?
alpha-D-glucopyranosyl-(1-6)-beta-fructofuranosyl-alpha-D-glucopyranoside + H2O
alpha-D-glucose + beta-D-fructose
-
29% cleavage compared to alpha-D-glucopyranosyl-(1-6)-beta-fructofuranosyl-alpha-D-glucopyranoside
-
-
?
dextran + H2O
D-glucose
-
-
-
?
isomaltose + H2O
2 alpha-D-glucose
-
-
-
?
isomaltose + H2O
2 D-glucose
isomaltose + H2O
?
-
-
-
?
isomaltulose + H2O
alpha-D-glucose + D-fructose
-
-
-
?
L-ascorbic acid alpha-glucoside + H2O
?
-
-
-
-
?
maltopentaose + H2O
?
-
-
-
-
?
maltose + H2O
2 D-glucose
maltose + H2O
?
comparable catalytic efficiencies for panose and maltose
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
maltose + L-ascorbic acid
L-ascorbic acid alpha-D-glucoside
-
-
enzyme form L-ascorbic acid alpha-glucoside by splitting maltose among the disaccharides
r
maltotetraose + H2O
?
-
-
-
-
?
maltotriose + H2O
?
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + alpha-D-glucopyranose
-
-
-
?
p-nitrophenyl-alpha-glucoside + H2O
p-nitrophenol + D-glucose
panose + H2O
?
comparable catalytic efficiencies for panose and maltose
-
-
?
sucrose + glucan
?
SUH active site structure analysis, overview
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
sucrose + H2O
D-glucose + D-fructose
additional information
?
-
inulin + H2O
?
-
-
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
?
isomaltose + H2O
glucose
-
-
-
?
isomaltose + H2O
glucose
-
-
-
-
?
isomaltose + H2O
glucose
-
-
-
?
levan + H2O
?
-
-
-
-
?
maltose + H2O
2 D-glucose
-
-
-
-
?
maltose + H2O
2 D-glucose
-
-
-
-
?
maltose + H2O
2 D-glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
2 glucose
-
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
-
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
-
-
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
-
-
-
?
maltose + H2O
alpha-D-glucose + D-glucose
-
-
-
?
p-nitrophenyl-alpha-glucoside + H2O
p-nitrophenol + D-glucose
-
-
-
?
p-nitrophenyl-alpha-glucoside + H2O
p-nitrophenol + D-glucose
-
-
-
?
raffinose + H2O
?
-
-
-
-
?
raffinose + H2O
?
-
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
-
the enzyme is involved in osmoregulation in the gut and hemolymph of pea aphids in response to the diet, analysis of honeydew sugar composition
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
-
the absolute enzyme exhibits a flat negative trough, indicating the presence of alpha-helices and beta-sheet structures in the enzyme
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
-
substrate binding site and structure, overview
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
additional information
?
-
-
enzyme mutation can cause the congenital sucrase-isomaltase deficiency phenotype II, overview
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
the enzyme expression is transactivated by transcription factors hepatocyte nuclear factors 1alpha and 1beta, HNF-1alpha and HNF-1beta, molecular mechanism and responsible amino acids of HNFs, overview
-
-
?
additional information
?
-
-
the enzyme expression is transactivated by transcription factors hepatocyte nuclear factors 1alpha and 1beta, HNF-1alpha and HNF-1beta, molecular mechanism and responsible amino acids of HNFs, overview
-
-
?
additional information
?
-
hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products
-
-
?
additional information
?
-
-
hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products
-
-
?
additional information
?
-
human maltase-glucoamylase and sucrase-isomaltase are composed of duplicated catalytic domains, N- and C-terminal, which display overlapping substrate specificities. The N-terminal catalytic domain of human MGAM has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides
-
-
?
additional information
?
-
-
human maltase-glucoamylase and sucrase-isomaltase are composed of duplicated catalytic domains, N- and C-terminal, which display overlapping substrate specificities. The N-terminal catalytic domain of human MGAM has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides
-
-
?
additional information
?
-
the enzyme performs hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action (EC 3.2.1.48), and hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose (EC 3.2.1.10), reaction mechanism
-
-
?
additional information
?
-
-
the enzyme performs hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action (EC 3.2.1.48), and hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose (EC 3.2.1.10), reaction mechanism
-
-
?
additional information
?
-
pullulan is likely degraded extracellularly by an amylopullulanase and further hydrolyzed by the PF0132 protein after intracellular transport
-
-
?
additional information
?
-
-
pullulan is likely degraded extracellularly by an amylopullulanase and further hydrolyzed by the PF0132 protein after intracellular transport
-
-
?
additional information
?
-
-
Additional substrates are mixtures of isomers containing mannitol and glucitol, e.g. alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-1)-D-mannitol and alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-1)-D-glucitol in a ratio 2:3, alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-alpha-D-gluco-pyranosyl-(1-1)-D-mannitol and alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-alpha-D-gluco-pyranosyl-(1-1)-D-glucitol in a ratio 2:3, 1,6-di-O-alpha-D-glucopyranosyl-D-mannitol and 1,6-di-O-alpha-D-glucopyranosyl-D-glucitol, alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-1)-D-mannitol and alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-1)-D-glucitol. The end products are glucose, mannose and glucitol in accordance with the composition of the initial substrate.
-
-
?
additional information
?
-
-
the enzyme activity influences the development of size and digestive capacity of the jejunum and small intestine
-
-
?
additional information
?
-
-
the enzyme is involved in regulating the secretion of cellobiase through co-aggregation
-
-
?
additional information
?
-
not: alpha-D-glucopyranosyl-(1-4)-D-glucopyranose, alpha-D-glucopyranosyl-(1-6)-D-glucopyranose, alpha-D-glucopyranosyl alpha-D-glucopyranoside, alpha-D-galactopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-2)-beta-D-fructofuranoside, alpha-D-galactopyranosyl-(1-6)-alpha-D-galactopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-2)-beta-D-fructofuranoside
-
-
?
additional information
?
-
-
not: alpha-D-glucopyranosyl-(1-4)-D-glucopyranose, alpha-D-glucopyranosyl-(1-6)-D-glucopyranose, alpha-D-glucopyranosyl alpha-D-glucopyranoside, alpha-D-galactopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-2)-beta-D-fructofuranoside, alpha-D-galactopyranosyl-(1-6)-alpha-D-galactopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-2)-beta-D-fructofuranoside
-
-
?
additional information
?
-
the enzyme is identified as NpAS, i.e. Neisseria polysaccharea amylosucrase, homolog, involved in regulation of the utilization of plant sucrose in phytopathogenic bacteria. But the enzyme is exclusively a hydrolase and not a glucosyltransferase and is termed sucrose hydrolase, SUH, overview
-
-
?
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(-)-epigallocatechin gallate
2,4,6-tribromophenol
-
purified from the red alga Grateloupia elliptica
2,4-Dibromophenol
-
purified from the red alga Grateloupia elliptica
2-Amino-2-ethyl-1,3-propanediol
-
-
2-amino-2-methyl-1,3-propanediol
-
-
2-amino-2-methyl-1-propanol
-
-
6-Bromo-2-naphthyl-alpha-glucoside
-
-
castanospermine
-
no effect on the biosynthesis of sucrase
CdCl2
-
0.0056 mM 50% inactivation
CuSO4
-
0.0028 mM 50% inactivation
D-glucose
22% inhibition at 0.7 mM, glucose product inhibition regulates the activities of both enzyme SI subunits
deoxygalactonojirimycin
-
IC50: 71.1 mM
H+
-
competitive inhibitor in the interaction of sucrase with sucrose and sodium
HgCl2
-
0.0022 mM 50% inactivation
isomaltose
-
competitive inhibition
kotalanol
binding structure, strong structural conservation of -1 subsite residues, overview
Li+
-
high concentration, 300 mM Li+, pH dependent inhibition, complete at pH 8
p-Nitrophenyl-alpha-glucoside
-
competitive inhibitor, inhibits both sucrase and isomaltase
PbCl2
-
0.0079 mM 50% inactivation
ranitidine
-
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
sucrose
-
high concentration
Tannic acid
-
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
-
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
ZnCl2
-
0.0133 mM 50% inactivation
(+)-catechin
noncompetitive
(+)-catechin
noncompetitive
(-)-epigallocatechin gallate
noncompetitive
(-)-epigallocatechin gallate
noncompetitive
acarbose
-
IC50: 0.000059 mM; in vitro and in vivo
acarbose
binding structure,overview
caffeic acid
noncompetitive
caffeic acid
noncompetitive
chlorogenic acid
noncompetitive
chlorogenic acid
noncompetitive
deoxynojirimycin
-
IC50: 0.034 mM
gallic acid
noncompetitive
gallic acid
-
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
gallic acid
noncompetitive
Na+
-
high concentration
Scopolamine
-
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
-
concentration-dependent biphasic effect, first causing activation, fully competitive inhibition above pH 6.8, inhibition is stronger at alkaline pH values
Tris
-
concentration-dependent biphasic effect, first causing activation, fully competitive inhibition above pH 6.8, inhibition is stronger at alkaline pH values
Tris
-
concentration-dependent biphasic effect, first causing activation, fully competitive inhibition above pH 6.8, inhibition is stronger at alkaline pH values
additional information
-
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
-
additional information
-
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
-
additional information
-
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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C1229Y
-
heterozygous mutation within the sucrose domain, found in patients with congenital sucrase-isomaltase deficiency. Recombinant mutant protein is transported only to the Golgi apparatus. Isomaltase activity is not affected by the mutation
D1500E
site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type
D1500S
site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type
D1700S
about 95% decrease in hydrolysis of sucrose, about 40% decrease in hydrolysis of maltose, about 30% increase in hydrolysis of isomaltulose
D604E
site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type
F1093A/F1095A/F1099A
-
site-directed mutagenesis, mutation of the extracellular folding signal motif, CSID-phenotype II-like temperature-sensitive mutant enzyme which undergoes transport arrest in the endoplasmic reticulum/cis-Golgi intermediate and cis-Golgi compartments and acquires correct folding and function at reduced temperatures as a consequence of anterograde and retrograde transport between endoplasmic reticulum and cis-Golgi, overview
F1745C
-
heterozygous mutation within the sucrose domain, found in patients with congenital sucrase-isomaltase deficiency. Recombinant mutant protein is misfolded and can not exit the endoplasmic reticulum. Isomaltase activity is not affected by the mutation
G1073D
-
heterozygous mutation found in patients with congenital sucrase-isomaltase deficiency. Recombinant mutant protein is misfolded and can not exit the endoplasmic reticulum
V15F
35% reduced enzymatic activity in vitro compared with wild-type enzyme. The mutation is detected in 6/7 sequenced familial cases of congenital sucrase-isomaltase deficiency
V577G
-
heterozygous mutation found in patients with congenital sucrase-isomaltase deficiency. Recombinant mutant protein is misfolded and can not exit the endoplasmic reticulum
E322Q
site-directed mutagenesis, a catalytically inactive Xag SUH mutant
G219R
site-directed mutagenesis, the mutant shows increased catalytic activity compared to the wild-type enzyme
G219R/G444R
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
G219R/L414R
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
G444R
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
L414R
site-directed mutagenesis, the mutant shows slightly reduced catalytic activity compared to the wild-type enzyme
L414R/G444R
site-directed mutagenesis, the mutant shows reduced catalytic activity compared to the wild-type enzyme
D1394E
about 95% decrease in hydrolysis of sucrose, about 50% decrease in hydrolysis of maltose, about 20% decrease in hydrolysis of isomaltulose
D1394E
site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type
D1500N
about 95% decrease in hydrolysis of sucrose, about 40% decrease in hydrolysis of maltose, about 5% decrease in hydrolysis of isomaltulose
D1500N
about 95% decrease in hydrolysis of sucrose, about 45% decrease in hydrolysis of maltose, about 10% increase in hydrolysis of isomaltulose
D1500N
site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type
D1500Y
about 95% decrease in hydrolysis of sucrose, about 35% decrease in hydrolysis of maltose, about 10% increase in hydrolysis of isomaltulose
D1500Y
site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type
D505E
about 5% increase in hydrolysis of sucrose, about 30% decrease in hydrolysis of maltose, about 95% decrease in hydrolysis of isomaltulose
D505E
site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type
D604N
about 10% increase in hydrolysis of sucrose, about 25% decrease in hydrolysis of maltose, about 95% decrease in hydrolysis of isomaltulose
D604N
site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type
D604S
about 10% decrease in hydrolysis of sucrose, about 10% decrease in hydrolysis of maltose, about 95% decrease in hydrolysis of isomaltulose
D604S
site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type
D604Y
about 20% decrease in hydrolysis of sucrose, about 30% decrease in hydrolysis of maltose, about 90% decrease in hydrolysis of isomaltulose
D604Y
about 5% increase in hydrolysis of sucrose, about 20% decrease in hydrolysis of maltose, about 95% decrease in hydrolysis of isomaltulose
D604Y
site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type
Q1098P
-
the mutation causes a temperature-sensitive arrest of enzyme in the endoplasmic reticulum and cis-Golgi, at 20°C the mutant shows 93% activity in comparison to 100% activity of wild-type enzyme. At 37°C the mutant shows 10% activity in comparison to 100% activity of wild-type enzyme
Q1098P
-
naturally occurring mutation, phenotype II of the congenital sucrase-isomaltase deficiency, CSID, the mutation generates a temperature-sensitive and activity-impaired mutant enzyme, congenital enzyme deficiency results in a transport block and retention of the enzyme of the brush border enzyme in the endoplasmic reticulum/cis-Golgi intermediate compartment and the cis-Golgi
additional information
-
overexpression of transcription factors HNF-1alpha and HNF-1beta mutants HNF-1lphaT539fsdelC and HNF-1betaR177X in Caco-2 cells reduces the sucrase-isomaltase activity
additional information
investigation of the implication of the motif HWLGDN in the functional capacities of isomaltase and sucrase with particular emphasis on the two aspartic acid residues predicted to participate in the alpha-glucosidase activity as proton donors. The study utilizes site-directed mutagenesis of the individual aspartate residues. The generated mutants provide a model to study enzymatic characteristics of isomaltase and sucrase without the functional overlapping of the other subunit
additional information
-
investigation of the implication of the motif HWLGDN in the functional capacities of isomaltase and sucrase with particular emphasis on the two aspartic acid residues predicted to participate in the alpha-glucosidase activity as proton donors. The study utilizes site-directed mutagenesis of the individual aspartate residues. The generated mutants provide a model to study enzymatic characteristics of isomaltase and sucrase without the functional overlapping of the other subunit
additional information
mutagenesis of the proton donor residues and the nucleophilic catalyst residues in each SI subunit of the enzyme. All of the mutants reveal expression levels and maturation rates comparable with those of the wild-type species and the corresponding nonmutated subunits are functionally active. Inactivation of one subunit of SI by mutagenesis is not paralleled by loss or reduction in the functional capacity of the other
additional information
-
mutagenesis of the proton donor residues and the nucleophilic catalyst residues in each SI subunit of the enzyme. All of the mutants reveal expression levels and maturation rates comparable with those of the wild-type species and the corresponding nonmutated subunits are functionally active. Inactivation of one subunit of SI by mutagenesis is not paralleled by loss or reduction in the functional capacity of the other
additional information
conformational changes in the SUH active site du to mutational alterations, overview
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Houck, C.M.; Pear, J.R.; Elliott, R.; Perchorowicz, J.T.
Isolation of DNA encoding sucrase genes from Streptococcus salivarius and partial characterization of the enzymes expressed in Escherichia coli
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3679-3684
1987
Streptococcus salivarius
brenda
Abe, M.; Yamada, K.; Hosoya, N.; Moriuchi, S.
Some properties of luminal sucrase and sucrase-isomaltase complex in rat small intestine
J. Nutr. Sci. Vitaminol.
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1985
Rattus rattus
brenda
Matsushita, S.
Purification and partial characterization of chick intestinal sucrase
Comp. Biochem. Physiol. B
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1983
Gallus gallus
brenda
Vasseur, M.; Van Melle, G.; Frangne, R.; Alvarado, F.
Alkali-metal-ion- and H+-dependent activation and/or inhibition of intestinal brush-border sucrase. A model involving three functionally distinct key prototropic groups
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Oryctolagus cuniculus
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Trugnan, G.; Rousset, M.; Zweibaum, A.
Castanospermine: a potent inhibitor of sucrase from the human enterocyte-like cell line Caco-2
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Homo sapiens
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Vasseur, M.; Tellier, Ch.; Alvarado, F.
Sodium-dependent activation of intestinal brush-border sucrase: correlation with activation by deprotonation from pH 5 to 7
Arch. Biochem. Biophys.
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1982
Oryctolagus cuniculus
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Montgomery, R.K.; Sybicki, M.A.; Forcier, A.G.; Grand, R.J.
Rat intestinal microvillus membrane sucrase-isomaltase is a single high molecular weight protein and fully active enzyme in the absence of luminal factors
Biochim. Biophys. Acta
661
346-349
1981
Rattus rattus
brenda
Hanozet, G.; Pircher, H.P.; Vanni, P.; Oesch, B.; Semenza, G.
An example of enzyme hysteresis. The slow and tight interaction of some fully competitive inhibitors with small intestinal sucrase
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1981
Oryctolagus cuniculus
brenda
Conklin, K.A.; Yamashiro, K.M.; Gray, G.M.
Human intestinal sucrase-isomaltase. Identification of free sucrase and isomaltase and cleavage of the hybrid into active distinct subunits
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1975
Homo sapiens
brenda
Hauri, H.P.; Quaroni, A.; Isselbacher, K.J.
Biogenesis of intestinal plasma membrane: posttranslational route and cleavage of sucrase-isomaltase
Proc. Natl. Acad. Sci. USA
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1979
Rattus rattus
brenda
Sigrist, H.; Ronner, P.; Semenza, G.
A hydrophobic form of the small-intestinal sucrase-isomaltase complex
Biochim. Biophys. Acta
406
433-446
1975
Oryctolagus cuniculus
brenda
Sjstrm, H.; Noren, O.; Christiansen, L.; Wacker, H.; Semenza, G.
A fully active, two-active-site, single-chain sucrase-isomaltase from pig small intestine. Implications for the biosynthesis of a mammalian integral stalked membrane protein
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255
11332-11338
1980
Sus scrofa
brenda
Kolinska, J.; Kraml, J.
Separation and characterization of sucrose-isomaltase and of glucoamylase of rat intestine
Biochim. Biophys. Acta
284
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1972
Rattus rattus
brenda
Muto, N.; Nakamura, T.; Yamamoto, I.
Enzymatic formation of a nonreducing L-ascorbic acid alpha-glucoside: purification and properties of alpha-glucosidases catalyzing site-specific transglucosylation from rat small intestine
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1990
Rattus rattus
brenda
Vasseur, M.; Frangne, R.; Cauzac, M.; Mahmood, A.; Alvarado, F.
pH-Dependent inhibitory effects of tris and lithium ion on intestinal brush-border sucrase
J. Enzyme Inhib.
4
15-26
1990
Oryctolagus cuniculus
brenda
Galand, G.
First purification and characterization of a sucrase-isomaltase from goose kidney microvillous membrane
Biochim. Biophys. Acta
1033
35-40
1990
Anser anser
brenda
Beaulieu, J.F.; Weiser, M.M.; Herrera, L.; Quaroni, A.
Detection and characterization of sucrase-isomaltase in adult human colon and in colonic polyps
Gastroenterology
98
1467-1477
1990
Homo sapiens
brenda
Teo, L.H.; Lateef, Z.; Ip, Y.K.
Some properties of the sucrase from the digestive gland of the green mussel Perna viridis L.
Comp. Biochem. Physiol. B
96
47-51
1990
Lissachatina fulica, Arion ater, Perna viridis
-
brenda
Sandhu, M.; Mahmood, A.
Kinetic characteristics of soluble and brush border alkaline phosphatase and sucrase activities in developing rat intestine: Effect of hormones
Indian J. Biochem. Biophys.
27
88-92
1990
Rattus rattus
brenda
Kapadia, H.A.; Sivakami, S.
Some properties of monkey intestinal sucrase
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27
93-97
1990
Platyrrhini
brenda
Fransen, J.A.M.; Hauri, H.P.; Ginsel, L.A.; Naim, H.Y.
Naturally occuring mutations in intestinal sucrase-isomaltase provide evidence for the existence of an intracellular sorting signal in the isomaltase subunit
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1991
Homo sapiens
brenda
Quezada-Calvillo, R.; Markowitz, A.J.; Traber, P.G.; Underdown, B.J.
Murine intestinal disaccharidases: identification of structural variants of sucrase-isomaltose complex
Am. J. Physiol.
265
1142-1149
1993
Mus musculus
-
brenda
Norman, J.M.; Bunny, K.L.; Giffard, P.M.
Characterization of levJ, a sucrase/fructanase-encoding gene from Actinomyces naeslundii T14V, and comparison of its product with other sucrose-cleaving enzymes
Gene
152
93-98
1995
Actinomyces naeslundii, Actinomyces naeslundii T14V
brenda
Kano, T.; Usami, Y.; Adachi, T.; Tatematsu, M.; Hirano, K.
Inhibition of purified human sucrase and isomaltase by ethanolamine derivatives
Biol. Pharm. Bull.
19
341-344
1996
Homo sapiens
brenda
Holt, S.M.; Cote, G.L.
Cloning and characterization of a sucrase from Leuconostoc mesenteroides
Biotechnol. Lett.
19
903-907
1997
Leuconostoc mesenteroides
-
brenda
Schnert, S.; Buder, T.; Dahl, M.K.
Identification and enzymatic characterization of the maltose-inducible alpha-glucosidase MalL (sucrase-isomaltase-maltase) of Bacillus subtilis
J. Bacteriol.
180
2574-2578
1998
Bacillus subtilis
brenda
Hertel, S.; Heinz, F.; Vogel, M.
Hydrolysis of low-molecular-weight oligosaccharides and oligosaccharide alditols by pig intestinal sucrase/isomaltase and glucosidase/maltase
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326
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2000
Sus scrofa
brenda
Mukherjee, S.; Khowala, S.
Regulation of cellobiase secretion in Termitomyces clypeatus by co-aggregation with sucrase
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45
70-73
2002
Termitomyces clypeatus
brenda
Finn, A.L.; Kuzhikandathil, E.V.; Oxford, G.S.; Itoh-Lindstrom, Y.
Sucrase-isomaltase is an adenosine 3',5'-cyclic monophosphate-dependent epithelial chloride channel
Gastroenterology
120
117-125
2001
Necturus maculosus
brenda
Kaur, N.; Kaur, J.; Mahmood, A.
Effect of harmaline on rat intestinal brush border sucrase activity
INDIAN J. Biochem. Biophys.
39
119-123
2002
Rattus norvegicus
brenda
Kim, H.S.; Park, H.J.; Heu, S.; Jung, J.
Molecular and functional characterization of a unique sucrose hydrolase from Xanthomonas axonopodis pv. glycines
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186
411-418
2004
Xanthomonas axonopodis (Q6UVM5), Xanthomonas axonopodis
brenda
Jacob, R.; Purschel, B.; Naim, H.Y.
Sucrase is an intramolecular chaperone located at the C-terminal end of the sucrase-isomaltase enzyme complex
J. Biol. Chem.
277
32141-32148
2002
Homo sapiens
brenda
Proepsting, M.J.; Jacob, R.; Naim, H.Y.
A glutamine to proline exchange at amino acid residue 1098 in sucrase causes a temperature-sensitive arrest of sucrase-isomaltase in the endoplasmic reticulum and cis-Golgi
J. Biol. Chem.
278
16310-16314
2003
Homo sapiens
brenda
Petersen, Y.M.; Elnif, J.; Schmidt, M.; Sangild, P.T.
Glucagon-like peptide 2 enhances maltase-glucoamylase and sucrase-isomaltase gene expression and activity in parenterally fed premature neonatal piglets
Pediatr. Res.
52
498-503
2002
Sus scrofa
brenda
Gu, N.; Suzuki, N.; Takeda, J.; Adachi, T.; Tsujimoto, G.; Aoki, N.; Ishihara, A.; Tsuda, K.; Yasuda, K.
Effect of mutations in HNF-1alpha and HNF-1beta on the transcriptional regulation of human sucrase-isomaltase in Caco-2 cells
Biochem. Biophys. Res. Commun.
325
308-313
2004
Homo sapiens
brenda
Martin-Latil, S.; Cotte-Laffitte, J.; Beau, I.; Quero, A.M.; Geniteau-Legendre, M.; Servin, A.L.
A cyclic AMP protein kinase A-dependent mechanism by which rotavirus impairs the expression and enzyme activity of brush border-associated sucrase-isomaltase in differentiated intestinal Caco-2 cells
Cell. Microbiol.
6
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2004
Homo sapiens
brenda
Zheng, Y.; Shentu, X.; Shen, Y.
Inhibition of porcine small intestinal sucrase by valienamine
Chin. J. Chem. Engin.
13
429-432
2005
Sus scrofa
-
brenda
Adeola, O.; King, D.E.
Developmental changes in morphometry of the small intestine and jejunal sucrase activity during the first nine weeks of postnatal growth in pigs
J. Anim. Sci.
84
112-118
2006
Sus scrofa
brenda
Proepsting, M.J.; Kanapin, H.; Jacob, R.; Naim, H.Y.
A phenylalanine-based folding determinant in intestinal sucrase-isomaltase that functions in the context of a quality control mechanism beyond the endoplasmic reticulum
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118
2775-2784
2005
Homo sapiens
brenda
Karley, A.J.; Ashford, D.A.; Minto, L.M.; Pritchard, J.; Douglas, A.E.
Significance of gut sucrase activity for osmoregulation in the pea aphid Acyrthosiphon pisum
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51
1313-1319
2005
Acyrthosiphon pisum
brenda
Gu, N.; Adachi, T.; Takeda, J.; Aoki, N.; Tsujimoto, G.; Ishihara, A.; Tsuda, K.; Yasuda, K.
Sucrase-isomaltase gene expression is inhibited by mutant hepatocyte nuclear factor (HNF)-1alpha and mutant HNF-1beta in Caco-2 cells
J. Nutr. Sci. Vitaminol.
52
105-112
2006
Homo sapiens
brenda
Gu, N.; Adachi, T.; Matsunaga, T.; Tsujimoto, G.; Ishihara, A.; Yasuda, K.; Tsuda, K.
HNF-1alpha participates in glucose regulation of sucrase-isomaltase gene expression in epithelial intestinal cells
Biochem. Biophys. Res. Commun.
353
617-622
2007
Homo sapiens
brenda
Honma, K.; Mochizuki, K.; Goda, T.
Carbohydrate/fat ratio in the diet alters histone acetylation on the sucrase-isomaltase gene and its expression in mouse small intestine
Biochem. Biophys. Res. Commun.
357
1124-1129
2007
Mus musculus
brenda
Suzuki, T.; Mochizuki, K.; Goda, T.
Histone H3 modifications and Cdx-2 binding to the sucrase-isomaltase (SI) gene is involved in induction of the gene in the transition from the crypt to villus in the small intestine of rats
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369
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2008
Rattus norvegicus
brenda
Naumoff, D.G.
Structure and evolution of the mammalian maltase-glucoamylase and sucrase-isomaltase genes
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41
962-973
2007
Homo sapiens (P14410)
-
brenda
Kim, M.I.; Kim, H.S.; Jung, J.; Rhee, S.
Crystal structures and mutagenesis of sucrose hydrolase from Xanthomonas axonopodis pv. glycines: insight into the exclusively hydrolytic amylosucrase fold
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380
636-647
2008
Xanthomonas axonopodis (Q6UVM5)
brenda
Kim, K.Y.; Nam, K.A.; Kurihara, H.; Kim, S.M.
Potent alpha-glucosidase inhibitors purified from the red alga Grateloupia elliptica
Phytochemistry
69
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2008
Rattus norvegicus
brenda
Alfalah, M.; Keiser, M.; Leeb, T.; Zimmer, K.P.; Naim, H.Y.
Compound heterozygous mutations affect protein folding and function in patients with congenital sucrase-isomaltase deficiency
Gastroenterology
136
883-892
2009
Homo sapiens
brenda
Wetzel, G.; Heine, M.; Rohwedder, A.; Naim, H.Y.
Impact of glycosylation and detergent-resistant membranes on the function of intestinal sucrase-isomaltase
Biol. Chem.
390
545-549
2009
Homo sapiens
brenda
Sim, L.; Willemsma, C.; Mohan, S.; Naim, H.Y.; Pinto, B.M.; Rose, D.R.
Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains
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285
17763-17770
2010
Homo sapiens (P14410), Homo sapiens
brenda
Champion, E.; Remaud-Simeon, M.; Skov, L.K.; Kastrup, J.S.; Gajhede, M.; Mirza, O.
The apo structure of sucrose hydrolase from Xanthomonas campestris pv. campestris shows an open active-site groove
Acta Crystallogr. Sect. D
65
1309-1314
2009
Xanthomonas campestris pv. campestris
brenda
Gupta, S.; Mahmood, S.; Khan, R.H.; Mahmood, A.
Inhibition of brush border sucrase by polyphenols in mouse intestine
Biosci. Rep.
30
111-117
2010
Mus musculus
brenda
Minai-Tehrani, D.; Fooladi, N.; Minoui, S.; Sobhani-Damavandifar, Z.; Aavani, T.; Heydarzadeh, S.; Attar, F.; Ghaffari, M.; Nazem, H.
Structural changes and inhibition of sucrase after binding of scopolamine
Eur. J. Pharmacol.
635
23-26
2010
Saccharomyces cerevisiae, Homo sapiens
brenda
Singh, A.; Mandal, D.
A novel sucrose/H+ symport system and an intracellular sucrase in Leishmania donovani
Int. J. Parasitol.
41
817-826
2011
Leishmania donovani, Leishmania donovani MHOM/IN/1978/UR6
brenda
Lee, S.H.; Yu, S.Y.; Nakayama, J.; Khoo, K.H.; Stone, E.L.; Fukuda, M.N.; Marth, J.D.; Fukuda, M.
Core2 O-glycan structure is essential for the cell surface expression of sucrase isomaltase and dipeptidyl peptidase-IV during intestinal cell differentiation
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285
37683-37692
2010
Homo sapiens, Mus musculus
brenda
Comfort, D.A.; Chou, C.J.; Conners, S.B.; VanFossen, A.L.; Kelly, R.M.
Functional-genomics-based identification and characterization of open reading frames encoding alpha-glucoside-processing enzymes in the hyperthermophilic archaeon Pyrococcus furiosus
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74
1281-1283
2008
Pyrococcus furiosus (Q8U4F6), Pyrococcus furiosus
brenda
Henstroem, M.; Diekmann, L.; Bonfiglio, F.; Hadizadeh, F.; Kuech, E.M.; von Koeckritz-Blickwede, M.; Thingholm, L.B.; Zheng, T.; Assadi, G.; Dierks, C.; Heine, M.; Philipp, U.; Distl, O.; Money, M.E.; Belheouane, M.; Heinsen, F.A.; Rafter, J.; Nardone, G.; Cuomo, R.; Usai-Satta, P.; Galeazzi, F.; Ne, N.e.r.
Functional variants in the sucrase-isomaltase gene associate with increased risk of irritable bowel syndrome
Gut
67
263-270
2018
Homo sapiens (P14410), Homo sapiens
brenda
Simsek, M.; Quezada-Calvillo, R.; Ferruzzi, M.G.; Nichols, B.L.; Hamaker, B.R.
Dietary phenolic compounds selectively inhibit the individual subunits of maltase-glucoamylase and sucrase-isomaltase with the potential of modulating glucose release
J. Agric. Food Chem.
63
3873-3879
2015
Mus musculus (B5THE3), Mus musculus, Homo sapiens (P14410), Homo sapiens
brenda
Gericke, B.; Schecker, N.; Amiri, M.; Naim, H.Y.
Structure-function analysis of human sucrase-isomaltase identifies key residues required for catalytic activity
J. Biol. Chem.
292
11070-11078
2017
Homo sapiens (P14410), Homo sapiens
brenda