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Literature summary for 3.2.1.3 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)

Cloned (Comment) Organism
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

Inhibitors Comment Organism Structure
acarbose a salacinol derivative, inhibition of the isolated recombinant N-terminal catalytic domain Homo sapiens
kotalanol a salacinol derivative, inhibition of the isolated recombinant N-terminal catalytic domain Homo sapiens
miglitol a salacinol derivative, inhibition of the isolated recombinant N-terminal catalytic domain Homo sapiens
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

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
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

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

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

Source Tissue

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

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl D-glucose
-
Homo sapiens 4-nitrophenol + D-glucose
-
?
starch + H2O
-
Homo sapiens D-glucose + ?
-
?
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

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

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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

Ki Value [mM]

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