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1,6-di-O-alpha-D-glucitol + H2O
D-glucitol
-
-
-
-
?
1,6-di-O-alpha-D-glucopyranosyl-D-fructofuranose + H2O
D-glucose + D-fructose
-
-
-
-
?
1,6-di-O-alpha-D-mannitol + H2O
D-mannitol
-
-
-
-
?
1-O-alpha-D-glucopyranosyl-D-fructopyranose + H2O
D-fructose
-
-
-
-
?
1-O-alpha-D-glucopyranosyl-D-glucitol + H2O
D-glucose + D-glucitol
-
-
-
-
?
1-O-alpha-D-glucopyranosyl-D-mannitol + H2O
D-glucose + D-mannitol
-
-
-
-
?
2'-deoxy-methyl-alpha-isomaltoside + H2O
?
-
-
-
-
?
2-deoxy-methyl-alpha-isomaltoside + H2O
?
-
-
-
-
?
3'-deoxy-methyl-alpha-isomaltoside + H2O
?
-
-
-
-
?
3-deoxy-methyl-alpha-isomaltoside + H2O
?
-
-
-
-
?
4'-deoxy-methyl-alpha-isomaltoside + H2O
?
-
-
-
-
?
4-deoxy-methyl-alpha-isomaltoside + H2O
?
-
-
-
-
?
4-methylumbelliferyl alpha-D-glucoside + H2O
4-methylumbelliferol + alpha-D-glucose
-
-
-
?
4-methylumbelliferyl beta-D-glucoside + H2O
4-methylumbelliferol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl 1-O-alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
4-nitrophenyl alpha-D-glucopyranoside
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
4-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
4-O-alpha-D-glucopyranosyl-D-glucopyranose + H2O
D-glucose
-
-
-
-
?
6'-deoxy-methyl-alpha-isomaltoside + H2O
?
-
-
-
-
?
6(R)-ethyl-alpha-isomaltoside + H2O
?
-
-
-
-
?
6(S)-ethyl-alpha-isomaltoside + H2O
?
-
-
-
-
?
6-O-alpha-D-glucopyranosyl-D-fructofuranose + H2O
D-glucose + D-fructose
-
-
-
-
?
6-O-alpha-D-glucopyranosyl-D-glucitol + H2O
D-glucose + D-glucitol
-
-
-
-
?
6-O-alpha-D-glucopyranosyl-D-glucopyranose + H2O
D-glucose
-
-
-
-
?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-1)-D-glucitol + H2O
D-glucose + D-glucitol
-
-
-
-
?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-1)-D-mannitol + H2O
D-glucose + D-mannitol
-
-
-
-
?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-1)-D-mannitol + H2O
D-glucose + D-mannitol
-
-
-
-
?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-glucitol + H2O
D-glucose + D-glucitol
-
-
-
-
?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-D-fructofuranose + H2O
D-glucose + D-fructose
-
-
-
-
?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-fructofuranose + H2O
D-glucose + D-fructose
-
-
-
-
?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-glucitol + H2O
D-glucose + D-glucitol
-
-
-
-
?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-glucopyranose + H2O
D-glucose
-
-
-
-
?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-D-fructofuranose + H2O
D-glucose + D-fructose
-
-
-
-
?
alpha-D-glucopyranosyl-(1-6)-beta-fructofuranosyl-alpha-D-glucopyranoside + H2O
D-glucose + D-fructose
-
-
-
-
?
alpha-limit dextrin + H2O
?
-
-
-
-
?
alpha-limit dextrins + H2O
D-glucose
amylose + H2O
?
-
n = 18, low activity of wild-type sucrase-isomaltase, very low activity of mutant isomaltase
-
-
?
glycogen + H2O
?
-
substrate from oyster, low activity of wild-type sucrase-isomaltase, very low activity of mutant isomaltase
-
-
?
isomaltohexaose + H2O
6 alpha-D-glucose
isomaltopentaose + H2O
5 alpha-D-glucose
isomaltosaccharides + H2O
D-glucose
isomaltose + H2O
2 D-glucose
isomaltose + H2O
alpha-D-glucose + D-glucose
isomaltotetraose + H2O
4 alpha-D-glucose
isomaltotriose + H2O
3 alpha-D-glucose
isomaltulose + H2O
D-glucose + D-fructose
kojibiose + H2O
2 D-glucose
-
weak activity
-
?
maltodextrin + H2O
?
-
corn maltodextrin
-
-
?
maltoheptaose + H2O
?
-
low activity of mutant isomaltase
-
-
?
maltohexaose + H2O
?
-
low activity of mutant isomaltase
-
-
?
maltopentaose + H2O
?
-
-
-
-
?
maltopentose + H2O
?
-
-
-
-
?
maltose + H2O
2 D-glucose
maltose + H2O
D-glucose + D-glucose
-
-
-
-
?
maltotriitol + H2O
D-glucose + maltitol
-
-
-
?
maltotriose + H2O
maltose + D-glucose
maltulose + H2O
alpha-D-glucose + D-fructose
methyl alpha-D-glucopyranoside + H2O
methanol + alpha-D-glucopyranose
-
-
-
?
methyl-alpha-isomaltoside + H2O
?
-
-
-
-
?
nigerose + H2O
2 D-glucose
nigerose + H2O
alpha-D-glucose + D-glucose
oligosaccharide + H2O
monosaccharide
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
palatinose + H2O
alpha-D-glucose + D-fructose
palatinose + H2O
D-glucose + D-fructose
-
-
-
?
palatinose + H2O
D-glucose + fructose
panitol
glucitol + maltitol
-
-
-
?
panose + H2O
alpha-D-glucose + maltose
preference for the cleavage of the alpha-1,6 linkage
-
-
?
panose + H2O
D-glucose + maltose
panose + H2O
maltose + alpha-D-glucose
phenyl-alpha-D-glucopyranoside + H2O
D-glucose + phenol
pullulan + H2O
?
-
low activity
-
-
?
pullulan + H2O
D-glucose + maltose
-
-
-
?
soluble starch + H2O
?
-
low activity of wild-type sucrase-isomaltase, very low activity of mutant isomaltase
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
trehalose + H2O
2 alpha-D-glucose
-
-
-
?
trehalulose + H2O
alpha-D-glucose + beta-D-fructose
-
-
-
?
turanose + H2O
alpha-D-glucose + beta-D-fructose
-
-
-
?
turanose + H2O
D-glucose + D-fructose
-
-
-
?
additional information
?
-
4-nitrophenyl 1-O-alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl 1-O-alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
?
4-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
alpha-limit dextrins + H2O
D-glucose
-
-
-
?
alpha-limit dextrins + H2O
D-glucose
-
-
-
?
alpha-limit dextrins + H2O
D-glucose
-
-
-
?
alpha-limit dextrins + H2O
D-glucose
-
-
-
?
isomaltohexaose + H2O
6 alpha-D-glucose
-
-
-
-
?
isomaltohexaose + H2O
6 alpha-D-glucose
-
-
-
-
?
isomaltopentaose + H2O
5 alpha-D-glucose
-
-
-
-
?
isomaltopentaose + H2O
5 alpha-D-glucose
-
-
-
-
?
isomaltopentaose + H2O
5 alpha-D-glucose
-
-
-
-
?
isomaltosaccharides + H2O
D-glucose
-
-
-
?
isomaltosaccharides + H2O
D-glucose
-
n = 2-6
-
?
isomaltosaccharides + H2O
D-glucose
-
n = 2-6
-
-
?
isomaltosaccharides + H2O
D-glucose
-
-
-
?
isomaltosaccharides + H2O
D-glucose
-
n = 2-6
-
?
isomaltosaccharides + H2O
D-glucose
-
n = 2, isomaltose
-
?
isomaltosaccharides + H2O
D-glucose
-
n = 2, isomaltose
-
?
isomaltosaccharides + H2O
D-glucose
-
n = 2, isomaltose
-
?
isomaltosaccharides + H2O
D-glucose
-
-
-
?
isomaltosaccharides + H2O
D-glucose
-
n = 3-5
-
-
?
isomaltosaccharides + H2O
D-glucose
-
-
-
?
isomaltosaccharides + H2O
D-glucose
-
n = 2, isomaltose
-
?
isomaltosaccharides + H2O
D-glucose
-
n = 2, isomaltose
-
?
isomaltosaccharides + H2O
D-glucose
-
n = 2, isomaltose
-
?
isomaltosaccharides + H2O
D-glucose
Thermoanaerobium sp.
-
n = 2-3
-
?
isomaltosaccharides + H2O
D-glucose
-
n = 2-6
-
?
isomaltosaccharides + H2O
D-glucose
-
n = 2, isomaltose
-
?
isomaltose + H2O
2 D-glucose
Alkalihalophilus pseudofirmus
-
-
-
-
?
isomaltose + H2O
2 D-glucose
Alkalihalophilus pseudofirmus 703
-
-
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
?
isomaltose + H2O
2 D-glucose
the hydrolysing percentages are 54.06%
-
-
?
isomaltose + H2O
2 D-glucose
the hydrolysing percentages are 54.06%
-
-
?
isomaltose + H2O
2 D-glucose
the hydrolysing percentages are 54.06%
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
?
isomaltose + H2O
2 D-glucose
-
best substrate for the mutant isomaltase
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
?
isomaltose + H2O
2 D-glucose
Thermoanaerobium sp.
-
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
?
isomaltose + H2O
?
-
-
-
-
?
isomaltose + H2O
?
-
-
-
-
?
isomaltose + H2O
?
-
-
-
-
?
isomaltose + H2O
?
-
-
-
-
?
isomaltose + H2O
?
-
-
-
?
isomaltose + H2O
alpha-D-glucose + D-glucose
-
-
-
?
isomaltose + H2O
alpha-D-glucose + D-glucose
-
-
-
?
isomaltose + H2O
alpha-D-glucose + D-glucose
-
-
-
-
?
isomaltose + H2O
alpha-D-glucose + D-glucose
i.e. alpha-D-Glc-(1->6)-D-Glc. Multifunctional enzyme that catalyzes also terminal alpha-1,4-linked, alpha-1,2-linked and alpha-1,3-linked glucose residues (EC 3.2.1.20/kojibiose/EC 3.2.1.84 hydrolase)
-
-
?
isomaltose + H2O
alpha-D-glucose + D-glucose
i.e. alpha-D-Glc-(1->6)-D-Glc. Multifunctional enzyme that catalyzes also terminal alpha-1,4-linked, alpha-1,2-linked and alpha-1,3-linked glucose residues (EC 3.2.1.20/kojibiose/EC 3.2.1.84 hydrolase)
-
-
?
isomaltose + H2O
alpha-D-glucose + D-glucose
-
-
-
-
?
isomaltotetraose + H2O
4 alpha-D-glucose
-
-
-
-
?
isomaltotetraose + H2O
4 alpha-D-glucose
-
-
-
-
?
isomaltotetraose + H2O
4 alpha-D-glucose
-
-
-
-
?
isomaltotriose + H2O
3 alpha-D-glucose
-
-
-
-
?
isomaltotriose + H2O
3 alpha-D-glucose
-
-
-
-
?
isomaltotriose + H2O
3 alpha-D-glucose
-
-
-
?
isomaltotriose + H2O
3 alpha-D-glucose
-
-
-
?
isomaltotriose + H2O
3 alpha-D-glucose
-
-
-
-
?
isomaltotriose + H2O
3 alpha-D-glucose
-
-
-
-
?
isomaltriose + H2O
?
-
-
-
?
isomaltriose + H2O
?
-
-
-
?
isomaltulose + H2O
D-glucose + D-fructose
the hydrolysing percentages are 37.7%
-
-
?
isomaltulose + H2O
D-glucose + D-fructose
the hydrolysing percentages are 37.7%
-
-
?
isomaltulose + H2O
D-glucose + D-fructose
the hydrolysing percentages are 37.7%
-
-
?
maltose + H2O
2 D-glucose
Alkalihalophilus pseudofirmus
-
-
-
-
?
maltose + H2O
2 D-glucose
Alkalihalophilus pseudofirmus 703
-
-
-
-
?
maltose + H2O
2 D-glucose
-
-
-
?
maltose + H2O
2 D-glucose
-
-
-
?
maltose + H2O
2 D-glucose
-
-
-
?
maltose + H2O
2 D-glucose
-
-
-
?
maltose + H2O
2 D-glucose
-
-
-
?
maltose + H2O
2 D-glucose
-
best substrate of the wild-type sucrase-isomaltase
-
-
?
maltose + H2O
2 D-glucose
-
-
-
?
maltose + H2O
2 D-glucose
-
-
-
?
maltotetraose + H2O
?
-
-
-
-
?
maltotetraose + H2O
?
-
low activity of mutant isomaltase
-
-
?
maltotriose + H2O
?
-
-
-
-
?
maltotriose + H2O
?
-
low activity of mutant isomaltase
-
-
?
maltotriose + H2O
maltose + D-glucose
Alkalihalophilus pseudofirmus
-
-
-
-
?
maltotriose + H2O
maltose + D-glucose
Alkalihalophilus pseudofirmus 703
-
-
-
-
?
maltotriose + H2O
maltose + D-glucose
-
-
-
?
maltulose + H2O
alpha-D-glucose + D-fructose
-
-
-
?
maltulose + H2O
alpha-D-glucose + D-fructose
-
-
-
?
nigerose + H2O
2 D-glucose
-
weak activity
-
?
nigerose + H2O
2 D-glucose
-
weak activity
-
?
nigerose + H2O
2 D-glucose
Thermoanaerobium sp.
-
weak activity
-
?
nigerose + H2O
2 D-glucose
-
weak activity
-
?
nigerose + H2O
alpha-D-glucose + D-glucose
-
-
-
?
nigerose + H2O
alpha-D-glucose + D-glucose
-
-
-
?
oligosaccharide + H2O
monosaccharide
-
direct function in maltose and isomaltose metabolism
-
?
oligosaccharide + H2O
monosaccharide
-
role in absorption of sucrose, isomaltose, maltose
-
?
oligosaccharide + H2O
monosaccharide
-
role in starch degradation
-
?
oligosaccharide + H2O
monosaccharide
-
role in digestion of carbohydrates
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
Thermoanaerobium sp.
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
-
-
-
?
palatinose + H2O
alpha-D-glucose + D-fructose
-
-
-
?
palatinose + H2O
alpha-D-glucose + D-fructose
-
-
-
?
palatinose + H2O
D-glucose + fructose
-
-
-
?
palatinose + H2O
D-glucose + fructose
-
-
-
?
palatinose + H2O
D-glucose + fructose
-
-
-
?
palatinose + H2O
D-glucose + fructose
-
-
-
?
palatinose + H2O
D-glucose + fructose
-
-
-
?
palatinose + H2O
D-glucose + fructose
-
-
-
?
palatinose + H2O
D-glucose + fructose
Thermoanaerobium sp.
-
weak aktivity
-
?
palatinose + H2O
D-glucose + fructose
-
weak aktivity
-
?
palatinose + H2O
D-glucose + fructose
-
-
-
?
panose + H2O
D-glucose + maltose
-
-
-
?
panose + H2O
D-glucose + maltose
-
-
-
?
panose + H2O
D-glucose + maltose
-
-
-
?
panose + H2O
D-glucose + maltose
-
-
-
?
panose + H2O
D-glucose + maltose
-
-
-
?
panose + H2O
D-glucose + maltose
Thermoanaerobium sp.
-
-
-
?
panose + H2O
D-glucose + maltose
-
-
-
?
panose + H2O
D-glucose + maltose
-
-
-
?
panose + H2O
maltose + alpha-D-glucose
alpha-D-Glc-(1->6)-alpha-D-Glc-(1->4)-D-Glc. Multifunctional enzyme that catalyzes also terminal alpha-1,4-linked, alpha-1,2-linked and alpha-1,3-linked glucose residues (EC 3.2.1.20/kojibiose/EC 3.2.1.84 hydrolase)
-
-
?
panose + H2O
maltose + alpha-D-glucose
alpha-D-Glc-(1->6)-alpha-D-Glc-(1->4)-D-Glc. Multifunctional enzyme that catalyzes also terminal alpha-1,4-linked, alpha-1,2-linked and alpha-1,3-linked glucose residues (EC 3.2.1.20/kojibiose/EC 3.2.1.84 hydrolase)
-
-
?
phenyl-alpha-D-glucopyranoside + H2O
D-glucose + phenol
-
-
-
-
?
phenyl-alpha-D-glucopyranoside + H2O
D-glucose + phenol
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
small activity
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
wild-type sucrase-isomaltase, no activity with the mutant isomaltase
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
trehalose + H2O
?
-
-
-
-
?
trehalose + H2O
?
-
-
-
-
?
trehalose + H2O
?
low activity
-
-
?
additional information
?
-
Alkalihalophilus pseudofirmus
-
the alpha-glucosidase (EC 3.2.1.20, UniProt ID A0A1S6JYL1) from Bacillus pseudofirmus strain 703 also shows oligo-alpha-1,6-glucosidase activity (EC 3.2.1.10), having both exo-alpha-1,4-glucosidase and oligo-1,6-glucosidase activities, but it shows no transglycosylation activity. The enzyme exhibits high activity against amylopectin from maize and soluble starch, but no activity against amylose from potato, pullulan, carboxymethylcellulose, and beachwood xylan. Amy112 hydrolyzes alpha-1,6-glucosidic linkages less effective than alpha-1,4-glucosidic linkages
-
-
?
additional information
?
-
Alkalihalophilus pseudofirmus 703
-
the alpha-glucosidase (EC 3.2.1.20, UniProt ID A0A1S6JYL1) from Bacillus pseudofirmus strain 703 also shows oligo-alpha-1,6-glucosidase activity (EC 3.2.1.10), having both exo-alpha-1,4-glucosidase and oligo-1,6-glucosidase activities, but it shows no transglycosylation activity. The enzyme exhibits high activity against amylopectin from maize and soluble starch, but no activity against amylose from potato, pullulan, carboxymethylcellulose, and beachwood xylan. Amy112 hydrolyzes alpha-1,6-glucosidic linkages less effective than alpha-1,4-glucosidic linkages
-
-
?
additional information
?
-
-
the enzyme might be involved in degradation for utilization of dextran in the bacterium
-
-
?
additional information
?
-
-
the enzyme might be involved in degradation for utilization of dextran in the bacterium
-
-
?
additional information
?
-
-
tertiary structure overview and evolutionary tree of subfamilies of the alpha-amylase family, including the oligo-1,6-glucosidase subfamily, analysis by comparison of the fifth conserved amino acid sequence region, overview
-
-
?
additional information
?
-
-
tertiary structure overview and evolutionary tree of subfamilies of the alpha-amylase family, including the oligo-1,6-glucosidase subfamily, analysis by comparison of the fifth conserved amino acid sequence region, overview
-
-
?
additional information
?
-
-
evolutionary connection to other alpha-glucosidases in comparison of amino acid sequence and substrate specificity, overview, the alpha-glucosidase, EC 3.2.1.20, of Bacillus sp. strain SAM1606 shows 192fold enhanced activity with trehalose by mutations P273G and T342N
-
-
?
additional information
?
-
-
tertiary structure overview and evolutionary tree of subfamilies of the alpha-amylase family, including the oligo-1,6-glucosidase subfamily, analysis by comparison of the fifth conserved amino acid sequence region, overview
-
-
?
additional information
?
-
-
enzyme is highly specific for alpha-1,6-linkages
-
-
?
additional information
?
-
-
tertiary structure overview and evolutionary tree of subfamilies of the alpha-amylase family, including the oligo-1,6-glucosidase subfamily, analysis by comparison of the fifth conserved amino acid sequence region, overview
-
-
?
additional information
?
-
-
evolutionary connection to other alpha-glucosidases in comparison of amino acid sequence and substrate specificity, overview, the alpha-glucosidase, EC 3.2.1.20, of Bacillus sp. strain SAM1606 shows 192fold enhanced activity with trehalose by mutations P273G and T342N
-
-
?
additional information
?
-
-
enzyme is highly specific for alpha-1,6-linkages
-
-
?
additional information
?
-
tertiary structure overview and evolutionary tree of subfamilies of the alpha-amylase family, including the oligo-1,6-glucosidase subfamily, analysis by comparison of the fifth conserved amino acid sequence region, overview
-
-
?
additional information
?
-
substrate specificity, enzyme is also capable to perform a transglycosylation producing oligosaccharides from trehalose and with low activity from sucrose, but no hydrolytic activity is detected with sucrose
-
-
?
additional information
?
-
-
substrate specificity, enzyme is also capable to perform a transglycosylation producing oligosaccharides from trehalose and with low activity from sucrose, but no hydrolytic activity is detected with sucrose
-
-
?
additional information
?
-
-
tertiary structure overview and evolutionary tree of subfamilies of the alpha-amylase family, including the oligo-1,6-glucosidase subfamily, analysis by comparison of the fifth conserved amino acid sequence region, overview
-
-
?
additional information
?
-
-
phenotype II of congenital enzyme deficiency features the retention of the brush border protein in the cis-Golgi, this transport is blocked by substitution of Gln1098 by proline
-
-
?
additional information
?
-
N-terminal sucrase-isomaltase has a broad specificity for both alpha-1,4- and alpha-1,6-oligosaccharides
-
-
?
additional information
?
-
the enzyme is active with maltose, maltotriose, and sucrose, only the N-terminal catalytic domain acts as alpha-1,6-glucosidase
-
-
?
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
-
-
?
additional information
?
-
the enzyme degrades isomaltose and isomaltulose, but not isomaltrotriose, melibiose, panose and raffinose. The enzyme shows no activity with trehalose, sucrose, turanose or maltose, i.e. sugars with glycosidic bonds other than 1->6, nor with 4-nitrophenyl-beta-D-glucopyranoside. Isomaltose and isomaltulose are the preferred substrates. Under the conditions of the assay, no transglycosylation activity of recombinant His-tagged enzyme MalL is observed with respect to the disaccharides sucrose, maltose, gentibiose, panose and isomaltulose
-
-
?
additional information
?
-
the enzyme degrades isomaltose and isomaltulose, but not isomaltrotriose, melibiose, panose and raffinose. The enzyme shows no activity with trehalose, sucrose, turanose or maltose, i.e. sugars with glycosidic bonds other than 1->6, nor with 4-nitrophenyl-beta-D-glucopyranoside. Isomaltose and isomaltulose are the preferred substrates. Under the conditions of the assay, no transglycosylation activity of recombinant His-tagged enzyme MalL is observed with respect to the disaccharides sucrose, maltose, gentibiose, panose and isomaltulose
-
-
?
additional information
?
-
the enzyme degrades isomaltose and isomaltulose, but not isomaltrotriose, melibiose, panose and raffinose. The enzyme shows no activity with trehalose, sucrose, turanose or maltose, i.e. sugars with glycosidic bonds other than 1->6, nor with 4-nitrophenyl-beta-D-glucopyranoside. Isomaltose and isomaltulose are the preferred substrates. Under the conditions of the assay, no transglycosylation activity of recombinant His-tagged enzyme MalL is observed with respect to the disaccharides sucrose, maltose, gentibiose, panose and isomaltulose
-
-
?
additional information
?
-
Necturus sp.
-
enzyme can also function as a cAMP-dependent chloride channel
-
-
?
additional information
?
-
-
no maltase activity
-
-
?
additional information
?
-
-
no maltase activity
-
-
?
additional information
?
-
-
tertiary structure overview and evolutionary tree of subfamilies of the alpha-amylase family, including the oligo-1,6-glucosidase subfamily, analysis by comparison of the fifth conserved amino acid sequence region, overview
-
-
?
additional information
?
-
-
N-terminal domain alpha/beta motifs are probably recognized by the endogenous GroEL protein, leading to binding and stabilization
-
-
?
additional information
?
-
-
no maltase activity
-
-
?
additional information
?
-
-
no maltase activity
-
-
?
additional information
?
-
-
N-terminal domain alpha/beta motifs are probably recognized by the endogenous GroEL protein, leading to binding and stabilization
-
-
?
additional information
?
-
-
stereochemistry and -specificity, overview
-
-
?
additional information
?
-
-
substrate specificities of isozymes IMA1 to IMA5, overview
-
-
?
additional information
?
-
the best substrate for oligo-1,6-glucosidase is isomaltotriose, other, longer-chain oligosaccharides are also good substrates. Isomaltase shows the highest activity towards isomaltose and very little activity towards longer oligosaccharides, because the entrance to the active site pocket of isomaltose is severely narrowed by Tyr158, His280, and loop 310315, and because the isomaltase pocket is shallower than that of other oligo-1,6-glucosidases, isomaltase substrate specificity, overview
-
-
?
additional information
?
-
-
the best substrate for oligo-1,6-glucosidase is isomaltotriose, other, longer-chain oligosaccharides are also good substrates. Isomaltase shows the highest activity towards isomaltose and very little activity towards longer oligosaccharides, because the entrance to the active site pocket of isomaltose is severely narrowed by Tyr158, His280, and loop 310315, and because the isomaltase pocket is shallower than that of other oligo-1,6-glucosidases, isomaltase substrate specificity, overview
-
-
?
additional information
?
-
isoforms Ima1, Ima2, Ima3 and Ima5 exhibit a preference for the alpha-(1,6) disaccharides isomaltose and palatinose, with Michaelis-Menten kinetics and inhibition at high substrates concentration. They are also able to hydrolyze trisaccharides bearing an alpha-(1,6) linkage, but also alpha-(1,2), alpha-(1,3) and alpha-(1,5) disaccharides including sucrose, highlighting their substrate ambiguity. No substrate: melibiose
-
-
?
additional information
?
-
isoforms Ima1, Ima2, Ima3 and Ima5 exhibit a preference for the alpha-(1,6) disaccharides isomaltose and palatinose, with Michaelis-Menten kinetics and inhibition at high substrates concentration. They are also able to hydrolyze trisaccharides bearing an alpha-(1,6) linkage, but also alpha-(1,2), alpha-(1,3) and alpha-(1,5) disaccharides including sucrose, highlighting their substrate ambiguity. No substrate: melibiose
-
-
?
additional information
?
-
isoforms Ima1, Ima2, Ima3 and Ima5 exhibit a preference for the alpha-(1,6) disaccharides isomaltose and palatinose, with Michaelis-Menten kinetics and inhibition at high substrates concentration. They are also able to hydrolyze trisaccharides bearing an alpha-(1,6) linkage, but also alpha-(1,2), alpha-(1,3) and alpha-(1,5) disaccharides including sucrose, highlighting their substrate ambiguity. No substrate: melibiose
-
-
?
additional information
?
-
isoforms Ima1, Ima2, Ima3 and Ima5 exhibit a preference for the alpha-(1,6) disaccharides isomaltose and palatinose, with Michaelis-Menten kinetics and inhibition at high substrates concentration. They are also able to hydrolyze trisaccharides bearing an alpha-(1,6) linkage, but also alpha-(1,2), alpha-(1,3) and alpha-(1,5) disaccharides including sucrose, highlighting their substrate ambiguity. No substrate: melibiose
-
-
?
additional information
?
-
isoforms Ima1, Ima2, Ima3 and Ima5 exhibit a preference for the alpha-(1,6) disaccharides isomaltose and palatinose, with MichaelisMenten kinetics and inhibition at high substrates concentration. They are also able to hydrolyze trisaccharides bearing an alpha-(1,6) linkage, but also alpha-(1,2), alpha-(1,3) and alpha-(1,5) disaccharides including sucrose, highlighting their substrate ambiguity. No substrate: melibiose
-
-
?
additional information
?
-
isoforms Ima1, Ima2, Ima3 and Ima5 exhibit a preference for the alpha-(1,6) disaccharides isomaltose and palatinose, with MichaelisMenten kinetics and inhibition at high substrates concentration. They are also able to hydrolyze trisaccharides bearing an alpha-(1,6) linkage, but also alpha-(1,2), alpha-(1,3) and alpha-(1,5) disaccharides including sucrose, highlighting their substrate ambiguity. No substrate: melibiose
-
-
?
additional information
?
-
isoforms Ima1, Ima2, Ima3 and Ima5 exhibit a preference for the alpha-(1,6) disaccharides isomaltose and palatinose, with MichaelisMenten kinetics and inhibition at high substrates concentration. They are also able to hydrolyze trisaccharides bearing an alpha-(1,6) linkage, but also alpha-(1,2), alpha-(1,3) and alpha-(1,5) disaccharides including sucrose, highlighting their substrate ambiguity. No substrate: melibiose
-
-
?
additional information
?
-
isoforms Ima1, Ima2, Ima3 and Ima5 exhibit a preference for the alpha-(1,6) disaccharides isomaltose and palatinose, with MichaelisMenten kinetics and inhibition at high substrates concentration. They are also able to hydrolyze trisaccharides bearing an alpha-(1,6) linkage, but also alpha-(1,2), alpha-(1,3) and alpha-(1,5) disaccharides including sucrose, highlighting their substrate ambiguity. No substrate: melibiose
-
-
?
additional information
?
-
-
substrate specificities of mutant isomaltase and wild-type sucrase-isomaltase, overview
-
-
?
additional information
?
-
-
substrate specificities of the 2 enzyme activities with the different substrate variants, overview, the active site of the sucrase subunit cleaves alpha,beta(1-2)-glycosidic bonds, and only 2 monomer units of the substrates bind with favourable affinity, while the isomaltase subunit possesses more than 2 subsites and cleaves oligosaccharides and reduced oligosaccharides with alpha(1-6)- and alpha(1-1)-glycosidic bonds, the isomaltase has binding sites for various aglycons
-
-
?
additional information
?
-
Thermoanaerobium sp.
-
no degradation of p-nitrophenyl-beta-D-glucose, p-nitrophenyl-alpha-D-galactose, p-nitrophenyl-beta-D-galactose, p-nitrophenyl-beta-D-xylose, p-nitrophenyl-alpha-L-arabinose, N-acetyl-alpha-D-glucosamine at 1 mM under standard conditions
-
-
?
additional information
?
-
-
no degradation of p-nitrophenyl-beta-D-glucose, p-nitrophenyl-alpha-D-galactose, p-nitrophenyl-beta-D-galactose, p-nitrophenyl-beta-D-xylose, p-nitrophenyl-alpha-L-arabinose, N-acetyl-alpha-D-glucosamine at 1 mM under standard conditions
-
-
?
additional information
?
-
-
tertiary structure overview and evolutionary tree of subfamilies of the alpha-amylase family, including the oligo-1,6-glucosidase subfamily, analysis by comparison of the fifth conserved amino acid sequence region, overview
-
-
?
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(-)-1-azafagomine
-
i.e.(3R,4R,5R)-4,5-dihydroxy-3-hydroxymethylhexahydropyridazine, competitive, slow inhibition process, difference in Ki values depend almost entirely on changes in the binding rate constant, direct binding model, some analogues of the compound are also inhibitory with less efficiency
(2R,3S,4S)-1-[(2S,3S)-2,4-dihydroxy-3-(tridecyloxy)butyl]-3,4-dihydroxy-2-(hydroxymethyl)tetrahydrothiophenium
-
-
(2R,3S,4S)-1-[(2S,3S)-2,4-dihydroxy-3-methoxybutyl]-3,4-dihydroxy-2-(hydroxymethyl)tetrahydrothiophenium
-
-
(2R,3S,4S)-1-[(2S,3S)-3-(benzyloxy)-2,4-dihydroxybutyl]-3,4-dihydroxy-2-(hydroxymethyl)tetrahydrothiophenium
-
-
(2R,3S,4S)-1-[(2S,3S)-3-ethoxy-2,4-dihydroxybutyl]-3,4-dihydroxy-2-(hydroxymethyl)tetrahydrothiophenium
-
-
(2S,3S,4S,5S)-2-(hydroxymethyl)-5-[3-(4-methylphenyl)propyl]pyrrolidine-3,4-diol
-
-
(2S,3S,4S,5S)-2-(hydroxymethyl)-5-[4-(4-methoxyphenyl)butyl]pyrrolidine-3,4-diol
-
-
(2S,3S,4S,5S)-2-[4-(3,5-difluorophenyl)butyl]-5-(hydroxymethyl)pyrrolidine-3,4-diol
-
good inhibition activities against intestinal isomaltase and sucrase
1,2,3-tri-O-galloyl-beta-D-glucose
-
about 20% inhibition at 1 mM
1,4-anhydro-4-thio-D-arabinitol
-
-
1,4-dideoxy-1,4-((S)-[(2S,3S)-2,4-dihydroxy-3-butyl]episulfoniumylidene)-D-arabinitol
-
-
1,4-dideoxy-1,4-(hydroxyethyliminiumyl)-D-arabinitol
-
-
1,4-dideoxy-1,4-imino-D-arabinitol
-
-
1,4-dideoxy-1,4-imino-L-arabinitol
-
-
1,4-dideoxy-1,4-[(S)-[(2S,3S)-2,4-dihydroxy-3-(sulfooxy)butyl]episulfoniumylidene]-D-arabinitol
-
-
1,4-dideoxy-1,4-[(S)-[(2S,3S)-2,4-dihydroxy-3-butyl]episulfoniumylidene]-D-arabinitol
-
-
1,4-imino-1,2,4-trideoxy-D-arabinitol
-
-
1-O-Galloyl-beta-D-glucose
-
about 15% inhibition at 1 mM, 34.4% inhibition at 5 mM
1-O-methyl-2,3-di-O-galloyl-beta-D-glucose
-
about 10% inhibition at 1 mM
1-O-methyl-alpha-D-glucose
Thermoanaerobium sp.
-
42% inhibition by 62 mM
1-O-methyl-beta-D-glucose
Thermoanaerobium sp.
-
52% inhibition by 62 mM
2,5-dideoxy-2,5-imino-D-glucitol
-
-
2,5-dideoxy-2,5-imino-D-mannitol
-
-
2,5-dideoxy-2,5-imino-L-mannitol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
80% inhibition of isomaltase activity by 50 mM
2-amino-2-methyl-1,3-propanediol
-
almost complete inhibition of isomaltase activity by 50 mM
3'-O-methylponkoranol
-
inhibits the different subunits to different extents, with extraordinary selectivity for C-terminal subunit of the enzyme
4-nitrophenyl alpha-D-glucopyranoside
-
blintol
selenium analogue of salacinol
Ca2+
-
29% inhibition by 2 mM CaCl2
casuarictin
-
ellagtannin, from flower buds of Syzygium aromaticum, about 16% inhibition at 1 mM
Cd2+
-
complete inhibition
chymotrypsin
-
almost 25% of palatinase activity after incubation with 0.1 mg/ml for 30 min
-
de-O-sulfonated kotalanol
de-O-sulfonated ponkoranol
-
-
de-O-sulfonated salacinol
-
-
diethanolamine
-
about 80% inhibition of isomaltase activity by 50 mM
DnaJ
-
the coexpression of the Hsp70 team chaperone protein leads to reduced activity
-
DnaK
-
the coexpression of the Hsp70 team chaperone protein leads to reduced activity
-
Elastase
-
almost 50% of palatinase activity after incubation with 0.1 mg/ml for 30 min
-
eugeniin
-
ellagtannin, from flower buds of Syzygium aromaticum, about 18% inhibition at 1 mM
Fe3+
-
86% inhibition by 2 mM FeCl3
gallic acid
-
8% inhibition at 5mM
GrpE
-
the coexpression of the Hsp70 team chaperone protein leads to reduced activity
-
hepatocyte nuclear factor-1alpha
-
gene expression of HNF-1alpha exhibits a positive correlation with that of sucrase-isomaltase regulated by glucose
-
isofagomine
-
stereoisomer of (-)-1-azafagomine, racemic, competitive
KCl
-
40% inhibition by 1 M
methyl alpha-D-glucopyranoside
-
Mg2+
-
42% inhibition by 2 mM MgCl2
Monoethanolamine
-
about 70% inhibition of isomaltase activity by 50 mM
monoiodoacetate
-
77% inhibition by 1 mM
mutant hepatocyte nuclear factor-1alpha
-
in the wild HNF-1alpha cells SI gene expression and enzyme activity is not significantly diminished
-
mutant hepatocyte nuclear factor-1beta
-
in the wild HNF-1beta cells SI gene expression and enzyme activity is not significantly diminished
-
N-ethylmaleimide
Thermoanaerobium sp.
-
70% inactivation by 3.3 mM at room temperature after 10 min
NaCl
-
50% inhibition by 500 mM
Ni2+
-
94% inhibition by 2 mM NiCl2
penta-O-galloyl-beta-D-glucose
-
about 40% inhibition at 1-5 mM
phenol
-
in combination with Tris most potent inhibitor
Phenyl alpha-maltoside
-
92% inhibition by 10 mM, noncompetitive
SDS
Thermoanaerobium sp.
-
96% inhibition by 3.5 mM under standard conditions
Sn2+
-
complete inhibition
triethanolamine
-
about 80% inhibition of isomaltase activity by 50 mM
Ba2+
-
-
Ba2+
-
72% inhibition by 2 mM BaCl2
Co2+
-
-
Co2+
-
96% inhibition by 2 mM in 20 mM borate buffer, pH 7.5 with p-nitrophenyl-alpha-D-glucopyranoside as substrate
Co2+
-
complete inhibition
conduritol-B-epoxide
-
complete inactivation by 0.024 mM
conduritol-B-epoxide
-
complete inactivation by 0.024 mM
Cu2+
-
-
Cu2+
-
95% inhibition by 2 mM in 20 mM borate buffer, pH 7.5 with p-nitrophenyl-alpha-D-glucopyranoside as substrate
Cu2+
-
complete inhibition by 1 mM CuCl2
Cu2+
-
96% inhibition by 2 mM CuCl2
D-glucose
-
-
D-glucose
-
sucrase-isomaltase gene expression is negatively regulated by glucose
D-glucose
22% inhibition at 0.7 mM, glucose product inhibition regulates the activities of both enzyme SI subunits
D-glucose
Thermoanaerobium sp.
-
product inhibition, inhibition of 70.1% of activity by 110 mM
D-glucose
-
52% inhibition by 10 mM, competitive
de-O-sulfonated kotalanol
isolated from Salacia reticulata
de-O-sulfonated kotalanol
-
-
EDTA
Alkalihalophilus pseudofirmus
-
-
EDTA
-
no inhibition by 2 mM at pH 7.5
EDTA
Thermoanaerobium sp.
-
rapid loss of activity at 1 mM, pH 5.6, 76°C
EDTA
-
no inhibition by 2 mM at pH 7.5
Fe2+
-
complete inhibition by 2 mM in 20 mM borate buffer, pH 7.5 with p-nitrophenyl-alpha-D-glucopyranoside as substrate
Fe2+
-
90% inhibition by 1 mM FeCl2
glucono-delta-lactone
-
-
glucono-delta-lactone
-
57% inhibition by 10 mM, competitive
Hg2+
-
-
Hg2+
-
complete inhibition by 2 mM in 20 mM borate buffer, pH 7.5 with p-nitrophenyl-alpha-D-glucopyranoside as substrate
Hg2+
-
complete inhibition by 1 mM HgCl2
Hg2+
-
99% inhibition by 2 mM HgCl2
kotalanol
-
kotalanol
isolated from Salacia reticulata
maltose
competitive inhibitor
maltose
competitive; competitive; mixed
Mn2+
-
40% inhibition by 2 mM in 20 mM borate buffer, pH 7.5 with p-nitrophenyl-alpha-D-glucopyranoside as substrate
Mn2+
-
92% inhibition by 2 mM MbCl2
p-chloromercuribenzoate
-
no inhibition by 2 mM with p-nitrophenyl-alpha-D-glucopyranoside as substrate
p-chloromercuribenzoate
-
complete inhibition by 0.1 mM
p-nitrophenol
-
-
p-nitrophenol
-
complete inhibition by 2 mM
papain
-
proteolytic inactivation at 35°C, pH 6.8
-
papain
-
proteolytic inactivation at 35°C, pH 6.8
-
Pb2+
-
-
Pb2+
-
90% inhibition by 2 mM in 20 mM borate buffer, pH 7.5 with p-nitrophenyl-alpha-D-glucopyranoside as substrate
Pb2+
-
complete inhibition by 1 mM PbCl2
Pb2+
-
complete inhibition
phenyl alpha-D-glucoside
-
-
phenyl alpha-D-glucoside
-
58% inhibition by 10 mM
pronase E
-
proteolytic inactivation at 35°C, pH 6.8
-
pronase E
-
proteolytic inactivation at 35°C, pH 6.8
-
salacinol
isolated from Salacia reticulata
subtilisin BPN'
-
proteolytic inactivation at 35°C, pH 6.8
-
subtilisin BPN'
-
proteolytic inactivation at 35°C, pH 6.8
-
Tris
-
-
Tris
-
93% inhibition by 5 mM
Tris
-
complete inhibition of isomaltase activity by 50 mM
Tris
-
89% inhibition by 5 mM, competitive
Trypsin
-
proteolytic inactivation at 35°C, pH 6.8
-
Trypsin
-
proteolytic inactivation at 35°C, pH 6.8
-
Trypsin
-
almost 25% of palatinase activity after incubation with 0.1 mg/ml for 30 min
-
Urea
-
-
Urea
-
50% inactivation after treatment with 1.42 M at 25°C or 0.74 M at 35°C for 5 h
Urea
-
50% inactivation after treatment with 8.7 M for 5 h at 25°C or 2.4 M at 60°C and pH 6.8
Urea
-
50% inactivation after treatment with 9.2 M for 5 h at 25°C or 2.7 M at 60°C and pH 6.8
Urea
Thermoanaerobium sp.
-
26% inhibition by 4 mM under standard conditions
Urea
-
50% inactivation after treatment with 4.6 M for 5 h at 25°C and pH 6.8
Zn2+
-
-
Zn2+
-
96% inhibition by 2 mM in 20 mM borate buffer, pH 7.5 with p-nitrophenyl-alpha-D-glucopyranoside as substrate
Zn2+
-
99% inhibition by 1 mM ZnCl2
Zn2+
Thermoanaerobium sp.
-
rapid inactivation by 1 mM possibly through interaction with free thiol groups of the enzyme
Zn2+
-
complete inhibition
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
-
additional information
-
structure-activity relationship study of inhibitors, inhibitory effect of the inhibitors on the different enzyme activities, such as maltase, sucrase and isomaltase activity, overview, an increasing number of galloyl units in the molecule leads to an increase in inhibitory potency
-
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-
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-
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-
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-
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1979
Parageobacillus thermoglucosidasius, Parageobacillus thermoglucosidasius KP 1006
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Oryctolagus cuniculus
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-
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Homo sapiens
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G1302-G1314
2007
Mus musculus
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2007
Homo sapiens
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Histone H3 modifications and Cdx-2 binding to the sucrase-isomaltase (SI) gene is involved in induction of the gene in the transition from the crypt to villus in the small intestine of rats
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369
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2008
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-
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Crystallization and preliminary X-ray analysis of isomaltase from Saccharomyces cerevisiae
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Saccharomyces cerevisiae
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Similarities and differences in the biochemical and enzymological properties of the four isomaltases from Saccharomyces cerevisiae
FEBS Open Bio
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200-212
2014
Saccharomyces cerevisiae (P0CW40), Saccharomyces cerevisiae (P40884), Saccharomyces cerevisiae (P53051), Saccharomyces cerevisiae (Q08295)
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Rodriguez, D.; Ramsay, A.J.; Quesada, V.; Garabaya, C.; Campo, E.; Freije, J.M.; Lopez-Otin, C.
Functional analysis of sucrase-isomaltase mutations from chronic lymphocytic leukemia patients
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2013
Homo sapiens (P14410)
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Diaz-Sotomayor, M.; Quezada-Calvillo, R.; Avery, S.E.; Chacko, S.K.; Yan, L.K.; Lin, A.H.; Ao, Z.H.; Hamaker, B.R.; Nichols, B.L.
Maltase-glucoamylase modulates gluconeogenesis and sucrase-isomaltase dominates starch digestion glucogenesis
J. Pediatr. Gastroenterol. Nutr.
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2013
Mus musculus
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Wang, S.; Wang, Q.; Zhou, Y.; Lu, Z.; Zhang, G.; Ma, Y.
A new GH13 alpha-glucosidase from alkaliphilic Bacillus pseudofirmus 703 with both exo-alpha-1, 4-glucosidase and oligo-1, 6-glucosidase activities toward amylopectin
Int. J. Biol. Macromol.
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Alkalihalophilus pseudofirmus, Alkalihalophilus pseudofirmus 703
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Delgado, S.; Florez, A.B.; Guadamuro, L.; Mayo, B.
Genetic and biochemical characterization of an oligo-alpha-1,6-glucosidase from Lactobacillus plantarum
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Lactiplantibacillus plantarum subsp. plantarum (D7VFY4), Lactiplantibacillus plantarum subsp. plantarum ATCC 149917 (D7VFY4), Lactiplantibacillus plantarum subsp. plantarum LL441 (D7VFY4)
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Gericke, B.; Schecker, N.; Amiri, M.; Naim, H.Y.
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Homo sapiens (P14410)
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