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
-
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
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
Advanced search results
Engineering
Engineering on EC 3.2.1.48 - sucrose alpha-glucosidase
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C1229Y
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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
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
F1093A/F1095A/F1099A
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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
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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
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heterozygous mutation found in patients with congenital sucrase-isomaltase deficiency. Recombinant mutant protein is misfolded and can not exit the endoplasmic reticulum
Q1098P
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
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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
additional information
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
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
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
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
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
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
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
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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
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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
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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
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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
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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