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Literature summary extracted from

  • Jones, K.; Sim, L.; Mohan, S.; Kumarasamy, J.; Liu, H.; Avery, S.; Naim, H.Y.; Quezada-Calvillo, R.; Nichols, B.L.; Pinto, B.M.; Rose, D.R.
    Mapping the intestinal alpha-glucogenic enzyme specificities of starch digesting maltase-glucoamylase and sucrase-isomaltase (2011), Bioorg. Med. Chem., 19, 3929-3934.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.10 recombinant expression of N-terminally His-tagged enzyme in Drosophila melanogaster S2 cells Homo sapiens
3.2.1.20 N- and C-terminal catalytic subunits, expression of His6-tagged N-terminal subunit ntMGAM in Drosophila S2 cells, expression of His6-tagged C-terminal subunits ctMGAMN2 and ctMGAMN20 in Spodoptera frugiperda Sf9 cells Homo sapiens
3.2.1.20 recombinant expression of N-terminally His-tagged N-terminal domain in Drosophila melanogaster S2 cells Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.10 acarbose
-
Homo sapiens
3.2.1.10 blintol selenium analogue of salacinol Homo sapiens
3.2.1.10 de-O-sulfonated kotalanol isolated from Salacia reticulata Homo sapiens
3.2.1.10 kotalanol isolated from Salacia reticulata Homo sapiens
3.2.1.10 miglitol
-
Homo sapiens
3.2.1.10 additional information inhibition profiles of the individual N- and C-terminal catalytic subunits of the enzyme by clinical glucosidase inhibitors, acarbose and miglitol, and glucosidase inhibitors from an Ayurvedic remedy used for the treatment of type II diabetes, overview Homo sapiens
3.2.1.10 salacinol isolated from Salacia reticulata Homo sapiens
3.2.1.20 acarbose
-
Homo sapiens
3.2.1.20 blintol selenium analogue of salacinol Homo sapiens
3.2.1.20 de-O-sulfonated kotalanol isolated from Salacia reticulata Homo sapiens
3.2.1.20 kotalanol isolated from Salacia reticulata Homo sapiens
3.2.1.20 maltotriose exhibits strong substrate inhibition; strong substrate inhibition Homo sapiens
3.2.1.20 miglitol
-
Homo sapiens
3.2.1.20 additional information inhibition profiles of the individual N- and C-terminal catalytic subunits of the enzyme by clinical glucosidase inhibitors, acarbose and miglitol, and glucosidase inhibitors from an Ayurvedic remedy used for the treatment of type II diabetes, overview; inhibition profiles of the individual N- and C-terminal catalytic subunits of the enzyme, overview Homo sapiens
3.2.1.20 salacinol isolated from Salacia reticulata Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.20 1.59
-
maltose catalytic subunit ctMGAMN2, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 1.91
-
maltose catalytic subunit ctMGAMN20, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 4.3
-
maltose catalytic subunit ntMGAM, pH and temperature not specified in the publication Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.20 maltose + H2O Homo sapiens
-
2 D-glucose
-
?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.10 recombinant N-terminally His-tagged enzyme from Drosophila melanogaster S2 cells by copper affinity chromatography and ion exchange chromatography Homo sapiens
3.2.1.20 recombinant His6-tagged C-terminal subunits ctMGAMN2 and ctMGAMN20 from Spodoptera frugiperda Sf9 cells by nickel affinity chromatography, recombinant His6-tagged N-terminal subunit ntMGAM from Drosophila S2 by cobalt affinity chromatography and ion exchange chromatography Homo sapiens
3.2.1.20 recombinant N-terminally His-tagged N-terminal domain from Drosophila melanogaster S2 cells by copper affinity chromatography and ion exchange chromatography Homo sapiens

Source Tissue

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.10 additional information the enzyme is active with maltose, maltotriose, and sucrose, only the N-terminal catalytic domain acts as alpha-1,6-glucosidase Homo sapiens ?
-
?
3.2.1.20 maltose + H2O
-
Homo sapiens 2 D-glucose
-
?
3.2.1.20 additional information the enzyme is active with maltose, maltotriose, and sucrose Homo sapiens ?
-
?

Synonyms

EC Number Synonyms Comment Organism
3.2.1.10 More the enzyme belongs to the family 31 of glycoside hydrolases Homo sapiens
3.2.1.10 sucrase-isomaltase
-
Homo sapiens
3.2.1.20 maltase-glucoamylase
-
Homo sapiens
3.2.1.20 MGAM
-
Homo sapiens
3.2.1.20 More the enzyme is a family 31 glycoside hydrolase Homo sapiens
3.2.1.20 More the enzyme belongs to the family 31 of glycoside hydrolases Homo sapiens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
3.2.1.10 0.000012
-
de-O-sulfonated kotalanol N-terminal cataklytic domain, pH and temperature not specified in the publication Homo sapiens
3.2.1.10 0.000148
-
miglitol N-terminal cataklytic domain, pH and temperature not specified in the publication Homo sapiens
3.2.1.10 0.00016
-
blintol N-terminal cataklytic domain, pH and temperature not specified in the publication Homo sapiens
3.2.1.10 0.000277
-
salacinol N-terminal cataklytic domain, pH and temperature not specified in the publication Homo sapiens
3.2.1.10 0.0006
-
kotalanol N-terminal cataklytic domain, pH and temperature not specified in the publication Homo sapiens
3.2.1.10 0.014
-
acarbose N-terminal cataklytic domain, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.000009
-
acarbose C-terminal catalytic domain N2, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.000009
-
acarbose catalytic subunit ctMGAMN2, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.000013
-
blintol C-terminal catalytic domain N20, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.000013
-
blintol catalytic subunit ctMGAMN20, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.000018
-
blintol C-terminal catalytic domain N2, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.000018
-
blintol catalytic subunit ctMGAMN2, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.000026
-
de-O-sulfonated kotalanol C-terminal catalytic domain N2, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.000026
-
de-O-sulfonated kotalanol catalytic subunit ctMGAMN2, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.000028
-
acarbose C-terminal catalytic domain N20, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.000028
-
acarbose catalytic subunit ctMGAMN20, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.00003
-
de-O-sulfonated kotalanol catalytic subunit ntMGAM, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.00003
-
de-O-sulfonated kotalanol N-terminal catalytic domain, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.000058
-
salacinol C-terminal catalytic domain N20, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.000058
-
salacinol catalytic subunit ctMGAMN20, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.000064
-
kotalanol C-terminal catalytic domain N2, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.000064
-
kotalanol catalytic subunit ctMGAMN2, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.000078
-
de-O-sulfonated kotalanol C-terminal catalytic domain N20, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.000078
-
de-O-sulfonated kotalanol catalytic subunit ctMGAMN20, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.000092
-
kotalanol C-terminal catalytic domain N20, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.000092
-
kotalanol catalytic subunit ctMGAMN20, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.00019
-
salacinol catalytic subunit ntMGAM, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.00019
-
kotalanol catalytic subunit ntMGAM, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.00019
-
salacinol N-terminal catalytic domain, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.00019
-
kotalanol N-terminal catalytic domain, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.000211
-
miglitol C-terminal catalytic domain N2, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.000211
-
miglitol catalytic subunit ctMGAMN2, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.000213
-
salacinol C-terminal catalytic domain N2, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.000213
-
salacinol catalytic subunit ctMGAMN2, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.00023
-
miglitol C-terminal catalytic domain N20, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.00023
-
miglitol catalytic subunit ctMGAMN20, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.00049
-
blintol catalytic subunit ntMGAM, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.00049
-
blintol N-terminal catalytic domain, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.001
-
miglitol catalytic subunit ntMGAM, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.001
-
miglitol N-terminal catalytic domain, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.062
-
acarbose catalytic subunit ntMGAM, pH and temperature not specified in the publication Homo sapiens
3.2.1.20 0.062
-
acarbose N-terminal catalytic domain, pH and temperature not specified in the publication Homo sapiens

General Information

EC Number General Information Comment Organism
3.2.1.20 metabolism the enzyme is responsible for the final step of starch hydrolysis Homo sapiens