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Literature summary extracted from

  • Rossi, E.J.; Sim, L.; Kuntz, D.A.; Hahn, D.; Johnston, B.D.; Ghavami, A.; Szczepina, M.G.; Kumar, N.S.; Sterchi, E.E.; Nichols, B.L.; Pinto, B.M.; Rose, D.R.
    Inhibition of recombinant human maltase glucoamylase by salacinol and derivatives (2006), FEBS J., 273, 2673-2683.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.3 expression of active MGA N-terminal catalytic domain MGAnt, residues 87-955, in COS-1 cells, and overexpression of MGAnt in Drosophila S2 cells, secretion of recombinant proteins Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.3 acarbose a salacinol derivative, inhibition of the isolated recombinant N-terminal catalytic domain Homo sapiens
3.2.1.3 kotalanol a salacinol derivative, inhibition of the isolated recombinant N-terminal catalytic domain Homo sapiens
3.2.1.3 miglitol a salacinol derivative, inhibition of the isolated recombinant N-terminal catalytic domain Homo sapiens
3.2.1.3 salacinol isolated from Salacia reticulata, a plant native to Sri Lanka and India that has been used in the Ayurvedic system of medicine for the treatment of diabetes, inhibition of the isolated recombinant N-terminal catalytic domain Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.3 membrane the enzyme is anchored in the membrane of small intestinal epithelial cells Homo sapiens 16020
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.3 105360
-
 x * 105360, recombinant N-terminal catalytic domain, MALDI-TOF mass spectrometry Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.3 starch + H2O Homo sapiens the enzyme is responsible for the final step of mammalian starch digestion leading to the release of D-glucose D-glucose + ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.3 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.3 secreted, recombinant N-terminal catalytic domain from Drosophila S2 cell culture supernatant by chelating resin and anion exchange chromatography Homo sapiens

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.2.1.3 epithelial cell
-
 Homo sapiens
-
3.2.1.3 small intestine
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.3 4-nitrophenyl D-glucose
-
 Homo sapiens 4-nitrophenol + D-glucose
-
 ?
3.2.1.3 starch + H2O
-
 Homo sapiens D-glucose + ?
-
 ?
3.2.1.3 starch + H2O the enzyme is responsible for the final step of mammalian starch digestion leading to the release of D-glucose Homo sapiens D-glucose + ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.3 ? x * 105360, recombinant N-terminal catalytic domain, MALDI-TOF mass spectrometry Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
3.2.1.3 maltase glucoamylase
-
 Homo sapiens
3.2.1.3 MGA
-
 Homo sapiens
3.2.1.3 More the enzyme is a family 31 glycoside hydrolase Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.3 37
-
 assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.3 6.5
-
 assay at Homo sapiens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.2.1.3 0.00019
-
 salacinol pH 6.5, 37°C, recombinant N-terminal catalytic domain Homo sapiens
3.2.1.3 0.062
-
 acarbose pH 6.5 37°C, recombinant N-terminal catalytic domain Homo sapiens