Any feedback?
Information on EC 3.2.1.48 - sucrose alpha-glucosidase and Organism(s) Homo sapiens and UniProt Accession P14410
for references in articles please use BRENDA:EC3.2.1.48Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.2.1.48 sucrose alpha-glucosidaseIUBMB Comments
This enzyme is isolated from intestinal mucosa as a single polypeptide chain that also displays activity towards isomaltose (EC 3.2.1.10 oligo-1,6-glucosidase).
Specify your search results
Word Map
- 3.2.1.48
- border
-
brush
- lactase
- enterocytes
- disaccharidase
-
caco-2
- mucosal
-
crypt
- jejunal
- starch
- maltase-glucoamylase
-
brush-border
- glucoamylase
- maltose
-
lactase-phlorizin
- ileum
- trehalase
- microvillus
- acarbose
-
basolateral
-
postprandial
-
dipeptidyl
- villin
-
suckling
-
dipeptidylpeptidase
- malabsorption
-
goblet
-
3.2.1.20
-
enterocyte-like
- isomaltose
-
3.4.11.2
-
intestine-specific
-
carbohydrase
-
small-intestinal
- aminopeptidase-n
-
postconfluent
-
crypt-villus
-
paneth
- 1-deoxynojirimycin
-
bloating
- dextrin
- agriculture
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
sucrase-isomaltase, isomaltase, intestinal sucrase, sucrase isomaltase, sucrose hydrolase, sucrase/isomaltase, sucrose alpha-glucosidase, sucrose alpha-glucohydrolase, sucrase-isomaltase enzyme complex, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glucosidase, sucrose alpha-
-
-
-
-
intestinal sucrase
-
-
-
-
sucrase
-
-
-
-
sucrase-invertase
-
-
-
-
sucrase-isomaltase
sucrose alpha-glucohydrolase
-
-
-
-
sucrase-isomaltase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -
SYSTEMATIC NAME
IUBMB Comments
sucrose-alpha-D-glucohydrolase
This enzyme is isolated from intestinal mucosa as a single polypeptide chain that also displays activity towards isomaltose (EC 3.2.1.10 oligo-1,6-glucosidase).
CAS REGISTRY NUMBER
COMMENTARY
37288-39-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl-alpha-D-glucoside + H2O
4-nitrophenol + alpha-D-glucose
-
-
-
?
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
-
-
?
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
?
-
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
?
-
-
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
-
-
?
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
kotalanol
binding structure, strong structural conservation of -1 subsite residues, overview
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
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
transcription factors HNF-1alpha and HNF-1beta induce constitutive enzyme expression by direct binding to sites SIF2 and SIF3 of the SI gene promoter
-
additional information
-
transcription factors HNF-1alpha and HNF-1beta transactivate enzyme expression in the small intestine, reduced activation activity of 13 HNF mutants, overview
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
19.6
sucrose
recombinant wild-type enzyme, pH 6.2, 37°C, in presence of 0.7 mM glucose
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics, overview
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme is sorted with high fidelity to the apical membrane via O-linked glycans that mediate its association with lipid rafts or detergent-resistant membranes
additional information
-
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, probably the quality control system is involved in retention induced by a retention signal or folding determinant, i.e. the extracellular folding motif F1093-X-F1095-X-X-X-F1099, of the temperature-sensitive Q1098P mutant enzyme
-
-
the isomaltase subunit is membrane associated and the sucrase subunit is hydrophilic
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme belongs to the glycoside hydrolase family 31 (GH31). All GH31 enzymes share a consensus sequence harboring an aspartic acid residue as a catalytic nucleophile
malfunction
metabolism
sucrase-isomaltase (SI) catalyzes the final step of carbohydrate digestion by breaking disaccharides and oligosaccharides to absorbable monosaccharides
physiological function
sucrase-isomaltase (SI, EC 3.2.1.48 and 3.2.1.10) is an intestinal membrane-associated alpha-glucosidase that breaks down di- and oligosaccharides to absorbable monosaccharides. The enzyme has two homologous functional subunits (sucrase and isomaltase) that both belong to the glycoside hydrolase family 31 (GH31) and differ in substrate specificity. Glucose product inhibition regulates the activities of both SI subunits
physiological function
-
core2 1,6-N-acetylglucosaminyltransferase-2 knockdown significantly reduces cell surface expression of sucrase isomaltase and dipeptidyl peptidase-IV in Caco-2 cells. Overexpression of the core3 structure in HT-29 cells attenuates cell surface expression of both enzymes
additional information
malfunction
congenital sucrase-isomaltase deficiency is a rare genetic form of disaccharide malabsorption characterised by diarrhoea, abdominal pain and bloating, which are features common to irritable bowel syndrome. Sucrase-isomaltase gene variants are tested for their potential relevance in irritable bowel syndrome. Sucrase-isomaltase gene variants coding for disaccharidases with defective or reduced enzymatic activity predispose to irritable bowel syndrome
malfunction
reduced or absent enzymatic levels of sucrase-isomaltase (SI) can lead to carbohydrate malabsorption with gastrointestinal symptoms, such as osmotic diarrhea, bloating, flatulence, and vomiting. SI deficiencies can occur primarily as a consequence of mutations in the coding region of the SI gene, referred to as congenital sucrase-isomaltase deficiency (CSID). Deleterious mutations are associated with alterations in the intracellular trafficking, functional deficits, and missorting of SI. Secondary SI deficiencies, on the other hand, arise collaterally to other organ pathologies in the intestine, in which the integrity and/or the normal physiology of the intestinal epithelium is severely affected, for example in intestinal ulcers or infections and inflammatory bowel disease. Inactivation of one subunit of SI by mutagenesis is not paralleled by loss or reduction in the functional capacity of the other
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). SUIS_HUMAN
1827
1
209453
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
130000
-
gel filtration, density gradient, equilibrium centrifugation, sucrase subunit
280000
-
gel filtration, density gradient equilibrium centrifugation, human, sucrase-isomaltase complex
additional information
-
The enzyme complex is a pseudo-dimeric assembly of a correctly folded and an enzymatically active pro-SI. The sucrase subunit functions as an intramolecular chaperone implicated in the folding of isomaltase subunit. After acquisition of a correct folding in the sucrase subunit this mature form binds tightly to the isomaltase, disrupting its interaction with calnexin. The consequence is that the isomaltase subunit acquires correct folding and sucrase subunit is no longer secreted into the external milieu.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
additional information
human maltase-glucoamylase and sucrase-isomaltase are composed of duplicated catalytic domains, N- and C-terminal, which display overlapping substrate specificities
additional information
-
human maltase-glucoamylase and sucrase-isomaltase are composed of duplicated catalytic domains, N- and C-terminal, which display overlapping substrate specificities
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
the individual expression of isomaltase subunit in COS-1 cells results in a malfolded and transport-incompetent glycoprotein, during the sucrase subunit a transport-competent protein
glycoprotein
-
the enzyme is highly glycosylated, glycosylation is inhibited by benzyl-GalNAc. Modulation of the glycosylation pattern of the enzyme with benzyl-2-acetamido-2-deoxy-alpha-D-galactopyranoside and deoxymannojirimycin, overview. N- and O-glycosylation and detergent-resistant membranes are implicated in the regulation of the function of the enzyme in intestinal Caco-2 cells
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
free enzyme and enzyme in complex with the inhibitor kotalanol, hanging drop vapor diffusion method, 0.001 ml of reservoir solution containing 0.5 M NaCl, 0.1 M bis tris propane, pH 7.0, and 18% PEG 4000, is equilibrated over 0.0015 ml of protein solution and 0.003 ml of reservoir solution, containing 0.1 M MgCl2, 0.1 M bis tris propane, pH 7.0, 15% PEG 4000, X-ray diffraction structure determination and analysis at 3.2 and 2.15 A resolution, respectively, molecular replacement
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D1394E
D1500E
site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type
D1500N
D1500S
site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type
D1500Y
D1700S
about 95% decrease in hydrolysis of sucrose, about 40% decrease in hydrolysis of maltose, about 30% increase in hydrolysis of isomaltulose
D505E
D604E
site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type
D604N
D604S
D604Y
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
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
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
Q1098P
V577G
-
heterozygous mutation found in patients with congenital sucrase-isomaltase deficiency. Recombinant mutant protein is misfolded and can not exit the endoplasmic reticulum
additional information
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
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
-
overexpression of transcription factors HNF-1alpha and HNF-1beta mutants HNF-1lphaT539fsdelC and HNF-1betaR177X in Caco-2 cells reduces the sucrase-isomaltase activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene SI, sequence comparisons, recominant expression of wild-type and mutant enzymes in COS-1 cells
expression of fluorescence-labeled wild-type and mutant enzymes in COS-1 cells
-
expression of the cDNA constructs encoding the sucrase and isomaltase domains in transfected cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
sucrase-isomaltase SI is a marker enzyme of the absorptive villose cells in adult small intestine, human intestinal sucrase-isomaltase help develop a specific inhibitor of sucrase, to retard the absorption of sucrose in the intestinal tract of diabetic patients
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Trugnan, G.; Rousset, M.; Zweibaum, A.
Castanospermine: a potent inhibitor of sucrase from the human enterocyte-like cell line Caco-2
FEBS Lett.
195
28-32
1986
Homo sapiens
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
J. Biol. Chem.
250
5735-5741
1975
Homo sapiens
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
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
J. Cell Biol.
115
45-47
1991
Homo sapiens
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
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
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
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
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
719-731
2004
Homo sapiens
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
J. Cell Sci.
118
2775-2784
2005
Homo sapiens
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
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
Naumoff, D.G.
Structure and evolution of the mammalian maltase-glucoamylase and sucrase-isomaltase genes
Mol. Biol.
41
962-973
2007
Homo sapiens (P14410)
-
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
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
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
J. Biol. Chem.
285
17763-17770
2010
Homo sapiens (P14410), Homo sapiens
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
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
J. Biol. Chem.
285
37683-37692
2010
Homo sapiens, Mus musculus
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
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
EXTERNAL LINKS (specific for EC-Number 3.2.1.48)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
