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Literature summary extracted from

  • Gericke, B.; Schecker, N.; Amiri, M.; Naim, H.Y.
    Structure-function analysis of human sucrase-isomaltase identifies key residues required for catalytic activity (2017), J. Biol. Chem., 292, 11070-11078 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.10 gene SI, sequence comparisons, recominant expression of wild-type and mutant enzymes in COS-1 cells Homo sapiens
3.2.1.48 expression of enzyme variants in COS-1 cells Homo sapiens
3.2.1.48 gene SI, sequence comparisons, recominant expression of wild-type and mutant enzymes in COS-1 cells Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.10 D1394E site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type Homo sapiens
3.2.1.10 D1500E site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type Homo sapiens
3.2.1.10 D1500N site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type Homo sapiens
3.2.1.10 D1500S site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type Homo sapiens
3.2.1.10 D1500Y site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type Homo sapiens
3.2.1.10 D505E site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type Homo sapiens
3.2.1.10 D604E site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type Homo sapiens
3.2.1.10 D604N site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type Homo sapiens
3.2.1.10 D604S site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type Homo sapiens
3.2.1.10 D604Y site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type Homo sapiens
3.2.1.10 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 Homo sapiens
3.2.1.48 D1394E about 95% decrease in hydrolysis of sucrose, about 50% decrease in hydrolysis of maltose, about 20% decrease in hydrolysis of isomaltulose Homo sapiens
3.2.1.48 D1394E site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type Homo sapiens
3.2.1.48 D1500E site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type Homo sapiens
3.2.1.48 D1500N about 95% decrease in hydrolysis of sucrose, about 40% decrease in hydrolysis of maltose, about 5% decrease in hydrolysis of isomaltulose Homo sapiens
3.2.1.48 D1500N about 95% decrease in hydrolysis of sucrose, about 45% decrease in hydrolysis of maltose, about 10% increase in hydrolysis of isomaltulose Homo sapiens
3.2.1.48 D1500N site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type Homo sapiens
3.2.1.48 D1500S site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type Homo sapiens
3.2.1.48 D1500Y about 95% decrease in hydrolysis of sucrose, about 35% decrease in hydrolysis of maltose, about 10% increase in hydrolysis of isomaltulose Homo sapiens
3.2.1.48 D1500Y site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type Homo sapiens
3.2.1.48 D1700S about 95% decrease in hydrolysis of sucrose, about 40% decrease in hydrolysis of maltose, about 30% increase in hydrolysis of isomaltulose Homo sapiens
3.2.1.48 D505E about 5% increase in hydrolysis of sucrose, about 30% decrease in hydrolysis of maltose, about 95% decrease in hydrolysis of isomaltulose Homo sapiens
3.2.1.48 D505E site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type Homo sapiens
3.2.1.48 D604E site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type Homo sapiens
3.2.1.48 D604N about 10% increase in hydrolysis of sucrose, about 25% decrease in hydrolysis of maltose, about 95% decrease in hydrolysis of isomaltulose Homo sapiens
3.2.1.48 D604N site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type Homo sapiens
3.2.1.48 D604S about 10% decrease in hydrolysis of sucrose, about 10% decrease in hydrolysis of maltose, about 95% decrease in hydrolysis of isomaltulose Homo sapiens
3.2.1.48 D604S site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type Homo sapiens
3.2.1.48 D604Y about 20% decrease in hydrolysis of sucrose, about 30% decrease in hydrolysis of maltose, about 90% decrease in hydrolysis of isomaltulose Homo sapiens
3.2.1.48 D604Y about 5% increase in hydrolysis of sucrose, about 20% decrease in hydrolysis of maltose, about 95% decrease in hydrolysis of isomaltulose Homo sapiens
3.2.1.48 D604Y site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type Homo sapiens
3.2.1.48 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 Homo sapiens
3.2.1.48 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 Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.10 D-glucose 22% inhibition at 0.7 mM, glucose product inhibition regulates the activities of both enzyme SI subunits Homo sapiens
3.2.1.48 D-glucose 22% inhibition at 0.7 mM, glucose product inhibition regulates the activities of both enzyme SI subunits Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.10 additional information
-
additional information Michaelis-Menten kinetics Homo sapiens
3.2.1.10 8.9
-
isomaltose recombinant wild-type enzyme, pH 6.2, 37°C Homo sapiens
3.2.1.10 9.8
-
isomaltose recombinant wild-type enzyme, pH 6.2, 37°C, in presence of 0.7 mM glucose Homo sapiens
3.2.1.48 additional information
-
additional information Michaelis-Menten kinetics Homo sapiens
3.2.1.48 1.55
-
maltose pH 6.2, 37°C, wild-type enzyme Homo sapiens
3.2.1.48 3.45
-
maltose pH 6.2, 37°C, mutant enzyme D604Y Homo sapiens
3.2.1.48 4.26
-
maltose pH 6.2, 37°C, mutant enzyme D1500Y Homo sapiens
3.2.1.48 15.6
-
sucrose recombinant wild-type enzyme, pH 6.2, 37°C Homo sapiens
3.2.1.48 19.6
-
sucrose recombinant wild-type enzyme, pH 6.2, 37°C, in presence of 0.7 mM glucose Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.10 brush border membrane
-
Homo sapiens 31526
-
3.2.1.10 membrane membrane-associated Homo sapiens 16020
-
3.2.1.48 brush border membrane
-
Homo sapiens 31526
-
3.2.1.48 membrane
-
Homo sapiens 16020
-
3.2.1.48 membrane membrane-associated Homo sapiens 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.10 isomaltose + H2O Homo sapiens
-
2 D-glucose
-
?
3.2.1.48 sucrose + H2O Homo sapiens
-
D-glucose + D-fructose
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.10 Homo sapiens P14410
-
-
3.2.1.48 Homo sapiens P14410
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.10 small intestine
-
Homo sapiens
-
3.2.1.48 intestine
-
Homo sapiens
-
3.2.1.48 small intestine
-
Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.10 isomaltose + H2O
-
Homo sapiens 2 D-glucose
-
?
3.2.1.10 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 Homo sapiens ?
-
?
3.2.1.48 isomaltulose + H2O
-
Homo sapiens alpha-D-glucose + D-fructose
-
?
3.2.1.48 maltose + H2O
-
Homo sapiens alpha-D-glucose + D-glucose
-
?
3.2.1.48 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 Homo sapiens ?
-
?
3.2.1.48 sucrose + H2O
-
Homo sapiens D-glucose + D-fructose
-
?
3.2.1.48 sucrose + H2O
-
Homo sapiens alpha-D-glucose + D-fructose
-
?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.10 sucrase-isomaltase
-
Homo sapiens
3.2.1.48 sucrase-isomaltase
-
Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.10 37
-
assay at Homo sapiens
3.2.1.48 37
-
assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.10 6.2
-
assay at Homo sapiens
3.2.1.48 6.2
-
assay at Homo sapiens

General Information

EC Number General Information Comment Organism
3.2.1.10 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 Homo sapiens
3.2.1.10 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 Homo sapiens
3.2.1.10 metabolism sucrase-isomaltase (SI) catalyzes the final step of carbohydrate digestion by breaking disaccharides and oligosaccharides to absorbable monosaccharides Homo sapiens
3.2.1.10 additional information enzyme structure-function analysis, overview Homo sapiens
3.2.1.10 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 Homo sapiens
3.2.1.48 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 Homo sapiens
3.2.1.48 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 Homo sapiens
3.2.1.48 metabolism sucrase-isomaltase (SI) catalyzes the final step of carbohydrate digestion by breaking disaccharides and oligosaccharides to absorbable monosaccharides Homo sapiens
3.2.1.48 additional information enzyme structure-function analysis, overview Homo sapiens
3.2.1.48 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 Homo sapiens