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Information on EC 3.2.1.10 - oligo-1,6-glucosidase
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EC Tree
3.2.1.10 oligo-1,6-glucosidaseIUBMB Comments
This enzyme, like EC 3.2.1.33 (amylo-alpha-1,6-glucosidase), can release an alpha-1->6-linked glucose, whereas the shortest chain that can be released by EC 3.2.1.41 (pullulanase), EC 3.2.1.142 (limit dextrinase), and EC 3.2.1.68 (isoamylase) is maltose. It also hydrolyses isomaltulose (palatinose), isomaltotriose and panose, but has no action on glycogen or phosphorylase limit dextrin. The enzyme from intestinal mucosa is a single polypeptide chain that also catalyses the reaction of EC 3.2.1.48 (sucrose alpha-glucosidase). Differs from EC 3.2.1.33 (amylo-alpha-1,6-glucosidase) in its preference for short-chain substrates and in its not requiring the 6-glucosylated residue to be at a branch point, i.e. linked at both C-1 and C-4.
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Word Map
- 3.2.1.10
- lactase
- mucosal
- jejunal
- border
-
brush
- gastrointestinal
- bowel
- children
- villus
- enterocytes
- ileum
-
crypt
- malabsorption
-
diarrhea
- infant
- duodenal
- trehalase
- disaccharide
-
piglets
-
brush-border
-
suckling
- malnutrition
- enteropathy
-
parenteral
-
small-intestinal
- giardiasis
-
lactase-phlorizin
- hypolactasia
- isomaltose
- maltase-glucoamylase
-
3.2.1.20
-
coeliac
- glucoamylase
- acarbose
- microvillus
- cellobiase
-
flatulence
-
small-bowel
-
bloating
-
maldigestion
- nutrition
-
3.4.11.2
- medicine
- lactulose
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
disaccharidase, oligo-1,6-glucosidase, sucrase-isomaltase complex, limit-dextrinase, intestinal sucrase/isomaltase, sea lion isomaltase, amy112, oligo-1,4-1,6-alpha-glucosidase, alpha-glucosidase 2, exo-oligo-1,6-glucosidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-glucosidase
alpha-glucosidase 2
Amy112
dextrin 6-alpha-D-glucanohydrolase
dextrin 6-alpha-glucanohydrolase
exo-oligo-1,6-glucosidase
HMPREF0531_13057
isomaltase
limit-dextrinase
MalA
MalL
O16G
oligo-1, 6-glucosidase
oligo-1,6-glucosidase
oligo-alpha-1,6-glucosidase
Oligosaccharide alpha-1,6-glucosidase
-
-
-
-
Saci1160
SI
sucrase-isomaltase
SUIS
additional information
Amy112
Alkalihalophilus pseudofirmus 703
-
-
-
dextrin 6-alpha-D-glucanohydrolase
-
-
dextrin 6-alpha-D-glucanohydrolase
-
-
oligo-1, 6-glucosidase
Alkalihalophilus pseudofirmus 703
-
-
-
sucrase-isomaltase
-
-
sucrase-isomaltase
-
two separate enzymes, probably occur bound together in complex
additional information
Alkalihalophilus pseudofirmus 703
-
cf. EC 3.2.1.20
-
additional information
-
oligo-1,6-glucosidases are a subfamily of the alpha-amylase family, classification
additional information
-
oligo-1,6-glucosidases are a subfamily of the alpha-amylase family, classification
additional information
-
enzyme belongs to the family 13 of glycosyl hydrolases
additional information
-
oligo-1,6-glucosidases are a subfamily of the alpha-amylase family, classification
additional information
-
oligo-1,6-glucosidases are a subfamily of the alpha-amylase family, classification
-
additional information
Bacillus sp. (in: Bacteria) SAM1606
-
enzyme belongs to the family 13 of glycosyl hydrolases
-
additional information
oligo-1,6-glucosidases are a subfamily of the alpha-amylase family, classification
additional information
the enzyme belongs to family 13 of glycosyl gydrolases
additional information
-
oligo-1,6-glucosidases are a subfamily of the alpha-amylase family, classification
additional information
the enzyme belongs to the family 31 of glycoside hydrolases
additional information
-
oligo-1,6-glucosidases are a subfamily of the alpha-amylase family, classification
additional information
-
the enzyme belongs to the glycosyl hydrolase family 13
additional information
-
the enzyme belongs to the glycosyl hydrolase family 13
-
additional information
-
enzyme belongs to alpha-glucoside hydrolase family 13
additional information
-
oligo-1,6-glucosidases are a subfamily of the alpha-amylase family, classification
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alpha-D-glucopyranosyl-(1-4)-[alpha-D-glucopyranosyl-(1-6)]-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose + H2O = alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose + D-glucose
alpha-D-glucopyranosyl-(1-4)-[alpha-D-glucopyranosyl-(1-6)]-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose + H2O = alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose + D-glucose
-
-
-
-
alpha-D-glucopyranosyl-(1-4)-[alpha-D-glucopyranosyl-(1-6)]-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose + H2O = alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose + D-glucose
enzyme from intestinal mucosa also catalyzes the reaction of sucrase alpha-glucosidase, EC 3.2.1.48
-
alpha-D-glucopyranosyl-(1-4)-[alpha-D-glucopyranosyl-(1-6)]-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose + H2O = alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose + D-glucose
enzyme from intestinal mucosa also catalyzes the reaction of sucrase alpha-glucosidase, EC 3.2.1.48
-
alpha-D-glucopyranosyl-(1-4)-[alpha-D-glucopyranosyl-(1-6)]-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose + H2O = alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose + D-glucose
enzyme from intestinal mucosa also catalyzes the reaction of sucrase alpha-glucosidase, EC 3.2.1.48
-
alpha-D-glucopyranosyl-(1-4)-[alpha-D-glucopyranosyl-(1-6)]-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose + H2O = alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose + D-glucose
enzyme from intestinal mucosa also catalyzes the reaction of sucrase alpha-glucosidase, EC 3.2.1.48
-
alpha-D-glucopyranosyl-(1-4)-[alpha-D-glucopyranosyl-(1-6)]-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose + H2O = alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose + D-glucose
enzyme from intestinal mucosa also catalyzes the reaction of sucrase alpha-glucosidase, EC 3.2.1.48
-
alpha-D-glucopyranosyl-(1-4)-[alpha-D-glucopyranosyl-(1-6)]-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose + H2O = alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose + D-glucose
enzyme from intestinal mucosa also catalyzes the reaction of sucrase alpha-glucosidase, EC 3.2.1.48
-
alpha-D-glucopyranosyl-(1-4)-[alpha-D-glucopyranosyl-(1-6)]-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose + H2O = alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose + D-glucose
enzyme from intestinal mucosa also catalyzes the reaction of sucrase alpha-glucosidase, EC 3.2.1.48
-
alpha-D-glucopyranosyl-(1-4)-[alpha-D-glucopyranosyl-(1-6)]-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose + H2O = alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose + D-glucose
active sites residues are Asp199, Glu255, and Asp329, substrate binding residues are His103, and His328, catalytic mechanism from comparison with other enzymes' primary and crystal enzyme structures
-
alpha-D-glucopyranosyl-(1-4)-[alpha-D-glucopyranosyl-(1-6)]-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose + H2O = alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranosyl-(1-4)-alpha-D-glucopyranose + D-glucose
stereochemistry, molecular substrate recognition mechanism, catayltic mechanism
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
hydrolysis of O-glycosyl bond
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
oligosaccharide 6-alpha-glucohydrolase
This enzyme, like EC 3.2.1.33 (amylo-alpha-1,6-glucosidase), can release an alpha-1->6-linked glucose, whereas the shortest chain that can be released by EC 3.2.1.41 (pullulanase), EC 3.2.1.142 (limit dextrinase), and EC 3.2.1.68 (isoamylase) is maltose. It also hydrolyses isomaltulose (palatinose), isomaltotriose and panose, but has no action on glycogen or phosphorylase limit dextrin. The enzyme from intestinal mucosa is a single polypeptide chain that also catalyses the reaction of EC 3.2.1.48 (sucrose alpha-glucosidase). Differs from EC 3.2.1.33 (amylo-alpha-1,6-glucosidase) in its preference for short-chain substrates and in its not requiring the 6-glucosylated residue to be at a branch point, i.e. linked at both C-1 and C-4.
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CAS REGISTRY NUMBER
COMMENTARY
9032-15-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,6-di-O-alpha-D-glucopyranosyl-D-fructofuranose + H2O
D-glucose + D-fructose
-
-
-
-
?
4-methylumbelliferyl alpha-D-glucoside + H2O
4-methylumbelliferol + alpha-D-glucose
-
-
-
?
4-methylumbelliferyl beta-D-glucoside + H2O
4-methylumbelliferol + beta-D-glucose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
6-O-alpha-D-glucopyranosyl-D-fructofuranose + H2O
D-glucose + D-fructose
-
-
-
-
?
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
-
-
-
-
?
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
-
-
?
methyl alpha-D-glucopyranoside + H2O
methanol + alpha-D-glucopyranose
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
-
?
palatinose + H2O
D-glucose + D-fructose
-
-
-
?
panose + H2O
alpha-D-glucose + maltose
preference for the cleavage of the alpha-1,6 linkage
-
-
?
soluble starch + H2O
?
-
low activity of wild-type sucrase-isomaltase, very low activity of mutant isomaltase
-
-
?
trehalulose + H2O
alpha-D-glucose + beta-D-fructose
-
-
-
?
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
Bacillus sp. (in: Bacteria) SAM1606
-
-
-
-
?
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
Lactiplantibacillus plantarum subsp. plantarum ATCC 149917
-
-
-
?
4-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
isomaltosaccharides + H2O
D-glucose
-
-
-
?
isomaltose + H2O
2 D-glucose
the hydrolysing percentages are 54.06%
-
-
?
isomaltose + H2O
2 D-glucose
Lactiplantibacillus plantarum subsp. plantarum ATCC 149917
the hydrolysing percentages are 54.06%
-
-
?
isomaltose + H2O
2 D-glucose
the hydrolysing percentages are 54.06%
-
-
?
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)
-
-
?
isomaltulose + H2O
D-glucose + D-fructose
the hydrolysing percentages are 37.7%
-
-
?
isomaltulose + H2O
D-glucose + D-fructose
Lactiplantibacillus plantarum subsp. plantarum ATCC 149917
the hydrolysing percentages are 37.7%
-
-
?
isomaltulose + H2O
D-glucose + D-fructose
the hydrolysing percentages are 37.7%
-
-
?
maltose + H2O
2 D-glucose
-
best substrate of the wild-type sucrase-isomaltase
-
-
?
maltulose + H2O
alpha-D-glucose + D-fructose
-
-
-
?
nigerose + H2O
2 D-glucose
-
weak activity
-
?
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 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
D-glucose + fructose
-
weak aktivity
-
?
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)
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
-
wild-type sucrase-isomaltase, no activity with the mutant isomaltase
-
-
?
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
?
-
Bacillus sp. (in: Bacteria) SAM1606
-
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
?
-
Bacillus sp. (in: Bacteria) SAM1606
-
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
?
-
Lactiplantibacillus plantarum subsp. plantarum ATCC 149917
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
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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 digestion of carbohydrates
-
?
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
?
-
-
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
?
-
Bacillus sp. (in: Bacteria) SAM1606
-
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
?
-
-
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
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
Alkalihalophilus pseudofirmus
-
Li+, Ca2+, and Mg2+ ions show no significant effect on enzyme activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(-)-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
1,4-dideoxy-1,4-((S)-[(2S,3S)-2,4-dihydroxy-3-butyl]episulfoniumylidene)-D-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-O-Galloyl-beta-D-glucose
-
about 15% inhibition at 1 mM, 34.4% inhibition at 5 mM
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
-
casuarictin
-
ellagtannin, from flower buds of Syzygium aromaticum, about 16% inhibition at 1 mM
chymotrypsin
-
almost 25% of palatinase activity after incubation with 0.1 mg/ml for 30 min
-
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
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
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
Co2+
-
96% inhibition by 2 mM in 20 mM borate buffer, pH 7.5 with p-nitrophenyl-alpha-D-glucopyranoside as substrate
Cu2+
-
95% inhibition by 2 mM in 20 mM borate buffer, pH 7.5 with p-nitrophenyl-alpha-D-glucopyranoside as substrate
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
Fe2+
-
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 2 mM in 20 mM borate buffer, pH 7.5 with p-nitrophenyl-alpha-D-glucopyranoside as substrate
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
p-chloromercuribenzoate
-
no inhibition by 2 mM with p-nitrophenyl-alpha-D-glucopyranoside as substrate
Pb2+
-
90% inhibition by 2 mM in 20 mM borate buffer, pH 7.5 with p-nitrophenyl-alpha-D-glucopyranoside as substrate
subtilisin BPN'
-
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
-
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
-
50% inactivation after treatment with 4.6 M for 5 h at 25°C and pH 6.8
Zn2+
-
96% inhibition by 2 mM in 20 mM borate buffer, pH 7.5 with p-nitrophenyl-alpha-D-glucopyranoside as substrate
Zn2+
Thermoanaerobium sp.
-
rapid inactivation by 1 mM possibly through interaction with free thiol groups of the enzyme
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
GroEL
-
heat shock protein of the Hsp60 team, GenBank accession number AB025944, activates 1.56fold, revives the thermally denatured enzyme, stabilizes and improve the recombinant expression level in Escherichia coli
-
GroES
-
heat shock protein of the Hsp60 team, GenBank accession number AB025944, activates 1.44fold, revives the thermally denatured enzyme, stabilizes and improve the recombinant expression level in Escherichia coli
-
additional information
-
gene expression and enzyme activity are changed by nutritional conditions
-
additional information
-
gene expression and enzyme activity are changed by nutritional conditions
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
244.5
isomaltulose
pH 5.5, 30°C, recombinant His-tagged enzyme
0.012
4-nitrophenyl alpha-D-glucopyranoside
-
recombinant mutant D199N, pH 7.0, 35°C
0.015
4-nitrophenyl alpha-D-glucopyranoside
-
recombinant mutant E255Q, pH 7.0, 35°C
0.35
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
0.48
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
0.58
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
0.8
4-nitrophenyl alpha-D-glucopyranoside
-
recombinant wild-type enzyme, pH 7.0, 35°C
0.89
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
0.99
4-nitrophenyl alpha-D-glucopyranoside
-
recombinant mutant H103N, pH 7.0, 35°C
1.3
4-nitrophenyl alpha-D-glucopyranoside
in 100 mM MES buffer, pH 6.5, at 37°C
13.3
4-nitrophenyl alpha-D-glucopyranoside
-
recombinant mutant H328N, pH 7.0, 35°C
6.22
isomaltose
pH 5.5, 30°C, recombinant His-tagged enzyme
9.8
isomaltose
recombinant wild-type enzyme, pH 6.2, 37°C, in presence of 0.7 mM glucose
15
methyl alpha-D-glucopyranoside
pH 7.0, 30°C
27
methyl alpha-D-glucopyranoside
pH 7.0, 30°C
28
methyl alpha-D-glucopyranoside
pH 7.0, 30°C
additional information
additional information
-
kinetics, transition state stabilization energy
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Km-value: 9.89 g/l with corn maltodextrin as a substrate for the immunoprecipitated human sucrase-isomaltase complex. Km-value: 5.78 g/l with alpha-limit dextrin as a substrate for the immunoprecipitated human sucrase-isomaltase complex. Km-value: 0.02 g/l with corn maltodextrin as a substrate for the supernatant after immunoprecipitation of sucrase-isomaltase complex (Sup-SI). Km-value: 0.29 g/l with alpha-limit dextrin as a substrate for the supernatant after immunoprecipitation of sucrase-isomaltase complex (Sup-SI)
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.18
4-nitrophenyl alpha-D-glucopyranoside
-
recombinant mutant D199N, pH 7.0, 35°C
0.39
4-nitrophenyl alpha-D-glucopyranoside
-
recombinant mutant E255Q, pH 7.0, 35°C
3.11
4-nitrophenyl alpha-D-glucopyranoside
-
recombinant mutant H328N, pH 7.0, 35°C
7.1
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
8.7
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
14
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
17
4-nitrophenyl alpha-D-glucopyranoside
in 100 mM MES buffer, pH 6.5, at 37°C
352
4-nitrophenyl alpha-D-glucopyranoside
-
recombinant mutant H103N, pH 7.0, 35°C
483
4-nitrophenyl alpha-D-glucopyranoside
-
recombinant wild-type enzyme, pH 7.0, 35°C
14
methyl alpha-D-glucopyranoside
pH 7.0, 30°C
84
methyl alpha-D-glucopyranoside
pH 7.0, 30°C
88
methyl alpha-D-glucopyranoside
pH 7.0, 30°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
13
4-nitrophenyl alpha-D-glucopyranoside
in 100 mM MES buffer, pH 6.5, at 37°C
15
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
16
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
20
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
28
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
0.9
methyl alpha-D-glucopyranoside
pH 7.0, 30°C
3.1
methyl alpha-D-glucopyranoside
pH 7.0, 30°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00016
blintol
N-terminal cataklytic domain, pH and temperature not specified in the publication
0.000012
de-O-sulfonated kotalanol
N-terminal cataklytic domain, pH and temperature not specified in the publication
0.000148
miglitol
N-terminal cataklytic domain, pH and temperature not specified in the publication
0.000277
salacinol
N-terminal cataklytic domain, pH and temperature not specified in the publication
0.000007
3'-O-methylponkoranol
-
versus the C-terminal subunit, pH and temperature not specified in the publication
0.000035
3'-O-methylponkoranol
-
versus the N-terminal subunit, pH and temperature not specified in the publication
2 - 5
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
9.8
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
12
4-nitrophenyl alpha-D-glucopyranoside
pH 7.0, 30°C
0.014
acarbose
N-terminal cataklytic domain, pH and temperature not specified in the publication
0.000103
de-O-sulfonated ponkoranol
-
versus the C-terminal subunit, pH and temperature not specified in the publication
0.000302
de-O-sulfonated ponkoranol
-
versus the N-terminal subunit, pH and temperature not specified in the publication
0.0006
kotalanol
N-terminal cataklytic domain, pH and temperature not specified in the publication
574
methyl alpha-D-glucopyranoside
pH 7.0, 30°C
600
methyl alpha-D-glucopyranoside
pH 7.0, 30°C
additional information
additional information
-
inhibition kinetics
-
additional information
additional information
-
Ki-value: 13.1 g/l with corn maltodextrin as a substrate for the supernatant after immunoprecipitation of sucrase-isomaltase complex (Sup-SI). Ki-value: 70.5 g/l with alpha-limit dextrin as a substrate for the supernatant after immunoprecipitation of sucrase-isomaltase complex (Sup-SI)
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.95
(2R,3S,4S)-1-[(2S,3S)-2,4-dihydroxy-3-(tridecyloxy)butyl]-3,4-dihydroxy-2-(hydroxymethyl)tetrahydrothiophenium
Homo sapiens
-
pH and temperature not specified in the publication
0.39
(2R,3S,4S)-1-[(2S,3S)-2,4-dihydroxy-3-methoxybutyl]-3,4-dihydroxy-2-(hydroxymethyl)tetrahydrothiophenium
Homo sapiens
-
pH and temperature not specified in the publication
0.14
(2R,3S,4S)-1-[(2S,3S)-3-(benzyloxy)-2,4-dihydroxybutyl]-3,4-dihydroxy-2-(hydroxymethyl)tetrahydrothiophenium
Homo sapiens
-
pH and temperature not specified in the publication
0.27
(2R,3S,4S)-1-[(2S,3S)-3-ethoxy-2,4-dihydroxybutyl]-3,4-dihydroxy-2-(hydroxymethyl)tetrahydrothiophenium
Homo sapiens
-
pH and temperature not specified in the publication
0.00063
(2S,3S,4S,5S)-2-(hydroxymethyl)-5-[3-(4-methylphenyl)propyl]pyrrolidine-3,4-diol
Rattus norvegicus
-
pH 6.8, 37°C
0.0018
(2S,3S,4S,5S)-2-(hydroxymethyl)-5-[4-(4-methoxyphenyl)butyl]pyrrolidine-3,4-diol
Rattus norvegicus
-
pH 6.8, 37°C
0.00022
(2S,3S,4S,5S)-2-[4-(3,5-difluorophenyl)butyl]-5-(hydroxymethyl)pyrrolidine-3,4-diol
Rattus norvegicus
-
pH 6.8, 37°C
0.0057
1,4-dideoxy-1,4-((S)-[(2S,3S)-2,4-dihydroxy-3-(sulfooxy)butyl]episulfoniumylidene)-D-arabinitol
Rattus sp.
-
-
0.64
1,4-dideoxy-1,4-((S)-[(2S,3S)-2,4-dihydroxy-3-butyl]episulfoniumylidene)-D-arabinitol
Rattus sp.
-
-
0.3
de-O-sulfonated salacinol
Homo sapiens
-
pH and temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.4
1.6
10
11
substrate methyl alpha-D-glucopyranoside, pH 7.0, 30°C
3.9
substrate 4-nitrophenyl alpha-D-glucopyranoside, pH 7.0, 30°C
313
-
purified enzyme after expression in Escherichia coli, p-nitrophenyl-alpha-D-glucopyranoside as substrate
5.1
-
purified recombinant enzyme + coexpressed DnaJ, DnaK, and GrpE
5.19
Thermoanaerobium sp.
-
purified enzyme, p-nitrophenyl-alpha-D-glucopyranoside as substrate
5.8
substrate 4-nitrophenyl alpha-D-glucopyranoside, pH 7.0, 30°C
52
55
substrate methyl alpha-D-glucopyranoside, pH 7.0, 30°C
7.2
substrate isomaltose, pH 7.0, 30°C
7.6
substrate isomaltriose, pH 7.0, 30°C
7.7
substrate 4-nitrophenyl alpha-D-glucopyranoside, pH 7.0, 30°C
7.9
substrate isomaltriose, pH 7.0, 30°C
8.6
9.46
-
purified recombinant enzyme + coexpressed GroES and GroEL
additional information
10
substrate 4-nitrophenyl alpha-D-glucopyranoside, pH 7.0, 30°C
52
substrate methyl alpha-D-glucopyranoside, pH 7.0, 30°C
8.6
substrate isomaltriose, pH 7.0, 30°C
additional information
Vmax is 0.4789 mM/mg/min
additional information
-
catalytic efficiency with different substrates, substrate specificity
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2 - 8.6
Alkalihalophilus pseudofirmus
-
over 50% of maximal activity within this range, profile overview
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
35
37
60
additional information
-
mutant SIQ/P is temperature-sensitive with a permissive temperature for catalysis of 20°C, at 37°C intracellular degradation of the mutant protein occurs
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
activity range, recombinant enzyme, activity declines sharply above 40°C
30 - 50
Alkalihalophilus pseudofirmus
-
profile overview, 50% of maximal activity at 50°C, maximal activity at 30-40°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
brenda
enzyme complex of sucrase and isomaltase integrated into the intestinal alpha-glucosidase function with the complex of maltase-glucoamylase
-
-
brenda
several strains, 5 genes IMA1 to IMA5, i.e. YGR287c, YIL172c, YJL216c, YJL221c and YOL157c. Gene IMA1/YGR287c encodes the major isomaltase
-
-
brenda
house musk shrew, contains 2 enzyme forms: a sucrase-free isomaltase and a sucrase-isomaltase
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
the transcription level of malA is increased 3fold upon the addition of maltose or starch to the medium. The alpha-glucosidase activity for maltose as a substrate in cell extracts is 11fold higher during growth in YT medium (Brocks mineral salts, 0.1% (w/v) tryptone, and 0.005% (w/v) yeast extract) containing maltose, than during growth on other sugars
brenda
-
the transcription level of malA is increased 3fold upon the addition of maltose or starch to the medium. The alpha-glucosidase activity for maltose as a substrate in cell extracts is 11fold higher during growth in YT medium (Brocks mineral salts, 0.1% (w/v) tryptone, and 0.005% (w/v) yeast extract) containing maltose, than during growth on other sugars
-
brenda
the transcription level of malA is increased 3fold upon the addition of maltose or starch to the medium. The alpha-glucosidase activity for starch as a substrate in cell extracts is 10fold higher during growth in YT medium (Brocks mineral salts, 0.1% (w/v) tryptone, and 0.005% (w/v) yeast extract) containing starch, than during growth on other sugars
brenda
-
the transcription level of malA is increased 3fold upon the addition of maltose or starch to the medium. The alpha-glucosidase activity for starch as a substrate in cell extracts is 10fold higher during growth in YT medium (Brocks mineral salts, 0.1% (w/v) tryptone, and 0.005% (w/v) yeast extract) containing starch, than during growth on other sugars
-
brenda
-
expression of the sucrase-isomaltase gene is induced in cells transitioning from the crypt to the villus of jejunum
brenda
-
jejunal sucrase-isomaltase gene is induced during postnatal development
brenda
-
jejunal sucrase-isomaltase gene is induced during postnatal development
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
of the small intestinal absorptive cells of the villus and the crypts
brenda
-
the enzyme is anchored to brush border epithelial cells
brenda
no predicted signal peptide is observed, suggesting an intracellular localization for the enzyme
brenda
Lactiplantibacillus plantarum subsp. plantarum ATCC 149917
-
no predicted signal peptide is observed, suggesting an intracellular localization for the enzyme
-
brenda
-
no predicted signal peptide is observed, suggesting an intracellular localization for the enzyme
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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
metabolism
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
additional information
evolution
-
sequence polymorphisms among the alpha-glucosidase family lead to interesting variability of gene expression patterns and of catalytic efficiencies on different substrates, which altogether account for the absence of functional redundancy for growth on isomaltose
evolution
Alkalihalophilus pseudofirmus
-
the enzyme belongs to the glycoside hydrolase family 13, GH13
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
evolution
the enzyme is a member of the alpha-amylase (AmyAC) superfamily of the glycosyl hydrolases (GH) family 13 (GH13), subfamily 31 (GH13_31)
evolution
Lactiplantibacillus plantarum subsp. plantarum ATCC 149917
-
the enzyme is a member of the alpha-amylase (AmyAC) superfamily of the glycosyl hydrolases (GH) family 13 (GH13), subfamily 31 (GH13_31)
-
evolution
-
the enzyme is a member of the alpha-amylase (AmyAC) superfamily of the glycosyl hydrolases (GH) family 13 (GH13), subfamily 31 (GH13_31)
-
evolution
Alkalihalophilus pseudofirmus 703
-
the enzyme belongs to the glycoside hydrolase family 13, GH13
-
metabolism
-
expression of the IMAx genes is regulated by carbon sources, putative binding sites of transcriptional regulators, overview. Ima1p isomaltase and Agt1p transporter are essential for isomaltose assimilation
metabolism
sucrase-isomaltase (SI) catalyzes the final step of carbohydrate digestion by breaking disaccharides and oligosaccharides to absorbable monosaccharides
additional information
catalytic residues are Glu277 and Asp352, isomaltase active site structure, role of the water chains in the active site pocket, the hydrogen bond network in the active site of isomaltase, overview
additional information
-
catalytic residues are Glu277 and Asp352, isomaltase active site structure, role of the water chains in the active site pocket, the hydrogen bond network in the active site of isomaltase, overview
additional information
Alkalihalophilus pseudofirmus
-
enzyme structure homology modeling, the predicted catalytic triad is comprised by Asp200, Glu257, and Asp327 in Amy112
additional information
Alkalihalophilus pseudofirmus 703
-
enzyme structure homology modeling, the predicted catalytic triad is comprised by Asp200, Glu257, and Asp327 in Amy112
-
Show AA Sequence and Transmembrane Helices (2024 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
106000
-
1 * 106000, isomaltase subunit of the wild-type enzyme, + 1 * 115000, sucrase subunit of the wild-type enzyme, SDS-PAGE
115000
-
1 * 106000, isomaltase subunit of the wild-type enzyme, + 1 * 115000, sucrase subunit of the wild-type enzyme, SDS-PAGE
140000 - 150000
-
SDS-PAGE, intact pancreatic duct, 2 polypeptide chains, 140000 + 150000
150000
60000 - 62000
71000
1 * 71000, SDS-PAGE, 1 * 72138, recombinant fusion protein, amino acid sequence calculation
72138
1 * 71000, SDS-PAGE, 1 * 72138, recombinant fusion protein, amino acid sequence calculation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
1 * 106000, isomaltase subunit of the wild-type enzyme, + 1 * 115000, sucrase subunit of the wild-type enzyme, SDS-PAGE
dodecamer
monomer
additional information
?
x * 66310, sequence calculation, x * 68000, recombinant His-tagged enzyme, SDS-PAGE
?
Lactiplantibacillus plantarum subsp. plantarum ATCC 149917
-
x * 66310, sequence calculation, x * 68000, recombinant His-tagged enzyme, SDS-PAGE
-
?
-
x * 66310, sequence calculation, x * 68000, recombinant His-tagged enzyme, SDS-PAGE
-
monomer
1 * 71000, SDS-PAGE, 1 * 72138, recombinant fusion protein, amino acid sequence calculation
additional information
-
amino acid sequence and tertiary structure analysis
additional information
-
amino acid sequence and tertiary structure analysis
additional information
-
amino acid sequence and tertiary structure analysis
-
additional information
amino acid sequence and tertiary structure analysis
additional information
-
amino acid sequence and tertiary structure analysis
additional information
tertiary structure prediction of MalL from Lactobacillus plantarum LL441
additional information
Lactiplantibacillus plantarum subsp. plantarum ATCC 149917
-
tertiary structure prediction of MalL from Lactobacillus plantarum LL441
-
additional information
-
tertiary structure prediction of MalL from Lactobacillus plantarum LL441
-
additional information
-
amino acid sequence and tertiary structure analysis
additional information
isomaltase contains three domains, namely, A, B, and C. Domain A consists of the (b eta?alpha)8-barrel common to glycoside hydrolase family 13. However, the folding of domain C is rarely seen in other glycoside hydrolase family 13 enzymes
additional information
-
isomaltase contains three domains, namely, A, B, and C. Domain A consists of the (b eta?alpha)8-barrel common to glycoside hydrolase family 13. However, the folding of domain C is rarely seen in other glycoside hydrolase family 13 enzymes
additional information
-
amino acid sequence and tertiary structure analysis
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
glycoprotein
-
enzyme, especially the mutant enzyme, contains probably carbohydrates with terminal L-fucose, determined by lectin affinity, overview
proteolytic modification
-
pro-sucrase-isomaltase precursor, complex glycosylated sucrase-isomaltase precursor, high-mannose sucrase-isomaltase precursor
proteolytic modification
-
extracellular proteolysis of single-chain pro-sucrase-isomaltase
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sucrase-isomaltase in apo form and in complex with kotalanol, hanging drop vapor diffusion method, using 0.1 M MgCl2, 0.1 M bis-Tris propane, pH 7.0, 15% (w/v) polyethylene glycol 4000
hanging-drop vapour-diffusion method with PEG 3350 as the precipitant
-
isomaltase free and in complex with inhibitor maltose, hanging drop vapor diffusion method, 0.003 ml of protein solution containing 4.5 mg/ml protein is mixed with an equal volume of reservoir solution containing 50 mM HEPES, pH 7.3, 0.2 M lithium acetate, and 19% w?v PEG3350, 2 weeks, X-ray diffraction structure determination and analysis at 1.3 A and 1.6 A resolution, respectively
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E257A
D199N
-
site-directed mutagenesis, active site mutant, highly reduced activity compared to the wild-type enzyme
D329N
-
site-directed mutagenesis, active site mutant, catalytically inactive mutant
E255Q
-
site-directed mutagenesis, active site mutant, highly reduced activity compared to the wild-type enzyme
H103N
-
site-directed mutagenesis, substrate binding mutant, about 50% reduced activity compared to the wild-type enzyme
H328N
-
site-directed mutagenesis, substrate binding mutant, highly reduced activity compared to the wild-type enzyme
N342T
-
site-directed mutagenesis, reduced activity with isomaltose, altered substrate specificity
P273G
-
site-directed mutagenesis, increased activity with trehalose, reduced activity with isomaltose, altered substrate specificity
P273G/N342T
-
site-directed mutagenesis, reduced activity with isomaltose, altered substrate specificity
N342T
Bacillus sp. (in: Bacteria) SAM1606
-
site-directed mutagenesis, reduced activity with isomaltose, altered substrate specificity
-
P273G
Bacillus sp. (in: Bacteria) SAM1606
-
site-directed mutagenesis, increased activity with trehalose, reduced activity with isomaltose, altered substrate specificity
-
P273G/N342T
Bacillus sp. (in: Bacteria) SAM1606
-
site-directed mutagenesis, reduced activity with isomaltose, altered substrate specificity
-
D1193N
mutation identified in chronic lymphocytic leukemia patient. Mutation is located in the C-terminal sucrase domain and results in a 25% decrease in activity and decrease of complex glycosylated forms of the mature enzyme
D1394E
site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type
D1500E
site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type
D1500N
site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type
D1500S
site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type
D1500Y
site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type
D505E
site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type
D604E
site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type
D604N
site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type
D604S
site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type
D604Y
site-directed mutagenesis of a catalytic residue, the mutant shows reduced maltase activity compared to wild-type
Q1098P
-
congenital enzyme deficiency causes phenotype II featuring retention of the brush border enzyme in the cis-Golgi, which is blocked by additional mutantion Q1098P, expression of the resulting mutant SIQ/P in the enzyme deficient mutant cell line can partially restore correct folding, competent intracellular transport, and full enzyme activity at 20°C instead of 37°C due to evolved temperature-sensitivity of the mutant
R91T
mutation identified in chronic lymphocytic leukemia patient. Mutation is inserted in a trefoil motif situated N-terminal to the isomaltase domain and results in a 75% decrease in activity and decrease of complex glycosylated forms of the mature enzyme
T1680I
mutation identified in chronic lymphocytic leukemia patient. Mutation is located in the C-terminal sucrase domain, leads to decrease of complex glycosylated forms of the mature enzyme
W1493C
mutation identified in chronic lymphocytic leukemia patient. Mutation is located in the C-terminal sucrase domain with almost complete loss of activity and decrease of complex glycosylated forms of the mature enzyme
R279Q
displays substrate specificities and specific activities close to those of isoform Ima2
additional information
E257A
Alkalihalophilus pseudofirmus
-
site-directed mutagenesis, mutation of a catalytic residue, inactive mutant
E257A
Alkalihalophilus pseudofirmus 703
-
site-directed mutagenesis, mutation of a catalytic residue, inactive mutant
-
additional information
-
congenital enzyme deficient mutant SI shows phenotype II featuring retention of the brush border enzyme in the cis-Golgi, which is blocked by additional mutantion Q1098P, expression of the resulting mutant SIQ/P in the enzyme deficient mutant cell line can partially restore correct folding, competent intracellular transport, and full enzyme activity at 20°C instead of 37°C due to evolved temperature-sensitivity of the mutant
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
additional information
-
the sucrase-free mutant lacks the entire sucrase domain and 69 amino acids of the C-terminus of isomaltase domain, the isomaltase function is unaffected by the mutation, sucrase function is missing
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 11.3
-
50% inactivation at pH 3.5 and 11.3 after incubation at 34°C for 15 h
326244
4.3 - 10.7
-
50% inactivation at pH 4.3 and 10.7 after incubation at 34°C for 15 h
326244
5 - 9.1
-
50% inactivation at pH 5.0 and 9.1 after incubation at 34°C for 15 h
326244, 326246
6.5 - 7.3
-
50% inactivation at pH 6.5 and 7.3 after incubation at 34°C for 15 h
326244, 326246
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
13 - 55
-
heating for 10 min in 33.3 mM phosphate buffer, pH 6.8: no loss of activity from 13 to 40°C, 87% of activity at 45°C, 56% at 48°C, 25% at 50°C, no activity at 55°C
25 - 55
-
stable for 15 h at pH 5.5-10.3 at 25°C, at pH 6.4-10.1 at 34°C, at pH 6.8-8.4 at 55°C, no activity after 15 h at pH 2.8 and 11.4 at 25°C, at pH 3.1 and 11.1 at 34°C, at pH 3.8 and 9.9 at 55°C
30 - 85
-
stable from 30 to 70°C, 50% inactivation at 71°C after 10 min
37
4 - 60
-
stable activity for 10 min at pH 6.8, 50% inactivation after 10 min at 70°C
40
60
-
almost no loss of activity for 5 min at 60°C, potassium phosphate buffer, pH 6.0
70
additional information
70
-
50% inactivation after 10 min incubation at pH 6.8
additional information
-
thermostability rises with proline content
additional information
-
thermostability rises with proline content
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
modulation of O-glycosylation by benzyl-2-acetamido-2-deoxy-alpha-D-galactopyranoside and N-glycosylation by deoxymannojirimycin is linked to a decreased capacity of sucrose-isomaltase to associate with detergent-resistant membranes
-
N-terminal domain alpha/beta motifs are probably recognized by the endogenous GroEL protein, leading to binding and stabilization
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ethanol
Ethanol
-
fairly stable for 5 h at 4°C in 20% ethanol , 50% inactivation after 5 h treatment with 17% ethanol at 25°C and pH 6.8
Ethanol
-
50% inactivation after 5 h treatment with 41% ethanol at 25°C and pH 6.8
Ethanol
-
50% inactivation after 5 h treatment with 49% ethanol at 25°C and pH 6.8
Ethanol
-
50% inactivation after 5 h treatment with 32% ethanol at 25°C and pH 6.8
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, stored for at least 6 months without any loss of activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification of the enzyme complex from rat intestinal acetone powder, by solubilization with Triton X-100, gel filtration, dialysis, ion exchange chromatography, and preparative PAGE
-
recombinant His-tagged enzyme by nickel affinity chromatography to homogeneity
recombinant His-tagged wild-type enzyme 5.72fold and of mutant enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, desalting gel filtration, and anion exchange chromatography, to homogeneity
Alkalihalophilus pseudofirmus
-
recombinant N-terminally His-tagged enzyme from Drosophila melanogaster S2 cells by copper affinity chromatography and ion exchange chromatography
sucrase-free isomaltase and a sucrase-isomaltase from a wild-type and a sucrase-deficient mutant line, from intestine, by temperature adsorption-desorption affinity chromatography on Sephadex gel
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning the region including the C-terminus of isomaltase and the N-terminus of sucrase subunit
-
construction of genetic library, DNA sequence determination and analysis of gene aglA, amino acid sequence determination, expression of the truncated enzyme fused to the N-terminus of lacZ in Escherichia coli XL1-Blue
DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli
-
DNA and amino acid sequence determination, functional expression in CHO cells and in Xenopus laevis oocytes, in vitro translation
Necturus sp.
-
expressed in Sulfolobus acidocaldarius. Attempts to obtain soluble enzyme from Escherichia coli strains are unsuccessful
expression in Escherichia coli
expression of wild-type and mutant enzymes in Escherichia coli strain W3110
-
gene amy112, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
Alkalihalophilus pseudofirmus
-
gene malL, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic tree, recombinant expression of His-tagged enzyme
gene SI, sequence comparisons, recominant expression of wild-type and mutant enzymes in COS-1 cells
genes IMA1 to IMA5, DNA and aminmo acid sequence determination and analysis, transcriptional patterns, overexpression of the 5 genes in Saccharomyces cerevisiae strain JF1811
-
optimization of recombinant overproduction in Escherichia coli BL21(DE3) by coexpression with various Bacillus thermoglucosidarius chaperone proteins, i.e. Hsp60 team proteins GroES and GroEL, as well as Hsp70 team proteins GrpE, DnaK, and DnaJ, thereof the Hsp70 proteins have no effect on expression level, while the Hsp60 proteins, especially GroEL, increase the expression level by 3.8fold
-
recombinant expression of N-terminally His-tagged enzyme in Drosophila melanogaster S2 cells
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the transcription level of malA is increased 3fold upon the addition of maltose or starch to the medium
the transcription level of malA is increased 3fold upon the addition of maltose or starch to the medium
the transcription level of malA is increased 3fold upon the addition of maltose or starch to the medium
-
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
nutrition
-
feeding of maltase-glucoamylase null and wild-type mice with starch diets ad libitum and ad limitum. After ad libitum meals, null and wild-type mice have similar increases of blood glucose concentration. At low intakes, null mice have less fractional glucogenesis than wild-type mice. Null mice do not reduce fractional glucogenesis responses to ad libitum intakes demonstrating the dominant role of sucrose-isomaltase activity during full feeding
medicine
-
possibility for use as molecular marker in diagnosis of colon adenocarcinoma
medicine
-
in type 2 diabetic patients enhanced SI enzyme activity may cause hyperglycemia, and aggravates diabetic conditions, the results of the study could be important for development of inhibitors
medicine
-
the enzyme can serve as therapeutic target for the treatment of digestive disorders or their sequelae
medicine
metabolic enzyme sucrase-isomaltase is one of the most frequently mutated genes in a cohort of 105 chronic lymphocytic leukemia patients. Mutations result in loss of enzyme function by preventing the biosynthesis of catalytically competent sucrase-isomaltase at the cell surface. Mutations impair enzyme function by altering its trafficking along the secretory pathway. Loss-of-function mutations in sucrase-isomaltase result in gene expression patterns that depict ample metabolic reprogramming, pinpointing sucrase-isomaltase as a putative player in the cancer-associated metabolic switch
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hauri, H.P.; Quaroni, A.; Isselbacher, K.J.
Biogenesis of intestinal plasma membrane: posttranslational route and cleavage of sucrase-isomaltase
Proc. Natl. Acad. Sci. USA
76
5183-5186
1979
Rattus norvegicus
brenda
Sjstrm, H.; Noren, O.; Christiansen, L.; Wacker, H.; Semenza, G.
A fully active, two-active-site, single-chain sucrase-isomaltase from pig small intestine. Implications for the biosynthesis of a mammalian integral stalked membrane protein
J. Biol. Chem.
255
11332-11338
1980
Sus scrofa
brenda
Galand, G.
First purification and characterization of a sucrase-isomaltase from goose kidney microvillous membrane
Biochim. Biophys. Acta
1033
35-40
1990
Anser anser
brenda
Beaulieu, J.F.; Weiser, M.M.; Herrera, L.; Quaroni, A.
Detection and characterization of sucrase-isomaltase in adult human colon and in colonic polyps
Gastroenterology
98
1467-1477
1990
Homo sapiens
brenda
Kano, T.; Usami, Y.; Adachi, T.; Tatematsu, M.; Hirano, K.
Inhibition of purified human sucrase and isomaltase by ethanolamine derivatives
Biol. Pharm. Bull.
19
341-344
1996
Homo sapiens
brenda
Schnert, S.; Buder, T.; Dahl, M.K.
Identification and enzymatic characterization of the maltose-inducible alpha-glucosidase MalL (sucrase-isomaltase-maltase) of Bacillus subtilis
J. Bacteriol.
180
2574-2578
1998
Bacillus subtilis
brenda
Watanabe, K.; Iha, H.; Ohashi, A.; Suzuki, Y.
Cloning and expression in Escherichia coli of an extremely thermostable oligo-1,6-glucosidase gene from Bacillus thermoglucosidasius
J. Bacteriol.
171
1219-1222
1989
Parageobacillus thermoglucosidasius, Parageobacillus thermoglucosidasius KP 1006
brenda
Plant, A.R.; Parratt, S.; Daniel, R.M.; Morgan, H.W.
A cell-associated oligo-1,6-alpha-glucosidase from an extremely thermophilic anaerobic bacterium, Thermoanaerobium Tok6-B1
Biochem. J.
255
865-868
1988
Thermoanaerobium sp., Thermoanaerobium sp. Tok6-B1
brenda
Lecommandeur, D.; MacGregor, A.W.; Daussant, J.
Purification of germinated barley alpha-amylase isoenzymes and limit dextrinase by chromatofocusing and affinity chromatography
J. Chromatogr.
441
436-442
1988
Hordeum vulgare
-
brenda
Suzuki, Y.; Oishi, K.; Nakano, H.; Nagayama, T.
A strong correlation between the increase in number of proline residues and the rise in thermostability of five Bacillus oligo-1,6-glucosidases
Appl. Microbiol. Biotechnol.
26
546-551
1987
Bacillus cereus, Weizmannia coagulans, Bacillus flavocaldarius, Bacillus thermoamyloliquefaciens KP1071, Parageobacillus thermoglucosidasius
-
brenda
Kakefuda, G.; Duke, S.H.; Hostak, M.S.
Chloroplast and extrachloroplast starch-degrading enzymes in Pisum sativum L.
Planta
168
175-182
1986
Pisum sativum
brenda
Suzuki, Y.; Tomura, Y.
Purification and characterization of Bacillus coagulans oligo-1,6-glucosidase
Eur. J. Biochem.
158
77-83
1986
Bacillus cereus, Weizmannia coagulans
brenda
Yoshigi, N.; Chikano, T.; Kamimura, M.
Production of alpha-glucosidases I and II from Bacillus cereus NY-14
Agric. Biol. Chem.
50
1335-1337
1986
Bacillus cereus, Bacillus cereus NY-14
-
brenda
Suzuki, Y.; Tamagawa, S.
The lack of identity between Bacillus stearothermophilus and Bacillus thermoglucosidases in serological patterns of exo-oligo-1,6-glucosidase and exo-alpha-1,4-glucosidase
Appl. Microbiol. Biotechnol.
20
218-220
1984
Geobacillus stearothermophilus, Parageobacillus thermoglucosidasius, Parageobacillus thermoglucosidasius KP 1006
-
brenda
Wacker, H.; Aggeler, R.; Kretchmer, N.; O'Neill, B.; Takesue, Y.; Semenza, G.
A two-active site one-polypeptide enzyme: the isomaltase from sea lion small intestinal brush-border membrane. Its possible phylogenetic relationship with sucrase-isomaltase
J. Biol. Chem.
259
4878-4884
1984
Callorhinus ursinus, Zalophus californianus
brenda
Suzuki, Y.; Takii, Y.; Taguchi, H.
A simplified method of the purification of Bacillus cereus ATCC 7064 exo-oligo-1,6-glucosidase by the use of immunosorbent
Eur. J. Appl. Microbiol. Biotechnol.
18
254-256
1983
Bacillus cereus
-
brenda
Suzuki, Y.; Aoki, R.; Hayashi, H.
Assignment of a p-nitrophenyl-alpha-D-glucopyranoside hydrolyzing alpha-glucosidase of Bacillus cereus ATCC 7064 to an exo-oligo-1,6-glucosidase
Biochim. Biophys. Acta
704
476-483
1982
Bacillus cereus
-
brenda
Suzuki, Y.; Imai, T.
Abnormally high tolerance against proteolysis of an exo-oligo-1,6-glucosidase from a thermophile Bacillus thermoglucosidius KP 1006, compared with its mesophilic counterpart from Bacillus cereus ATCC 7064
Biochim. Biophys. Acta
705
124-126
1982
Bacillus cereus, Parageobacillus thermoglucosidasius, Parageobacillus thermoglucosidasius KP 1006
brenda
Skovbjerg, H.; Sjoestroem, H.; Noren, O.
Does sucrase-isomaltase always exist as a complex in human intestine?
FEBS Lett.
108
399-402
1979
Homo sapiens
brenda
Suzuki, Y.; Ueda, Y.; Nakamura, N.; Abe, S.
Hydrolysis of low molecular weight isomaltosaccharides by a p-nitrophenyl-alpha-D-glucopyranoside-hydrolyzing alpha-glucosidase from a thermophile, Bacillus thermoglucosidius KP 1006
Biochim. Biophys. Acta
566
62-66
1979
Parageobacillus thermoglucosidasius, Parageobacillus thermoglucosidasius KP 1006
brenda
Marshall, J.J.; Sturgeon, C.M.; Whelan, W.J.
Solubilization of porcine intestinal alpha-glucosidases and evidence for the separate identities of isomaltase and limit dextrinase
Anal. Biochem.
82
435-444
1977
Sus scrofa
brenda
Quaroni, A.; Gershon, E.; Semenza, G.
Affinity labeling of the active sites in the sucrase-isomaltase complex from small intestine
J. Biol. Chem.
249
6424-6433
1974
Oryctolagus cuniculus
brenda
Asp, N.G.; Dahlqvist, A.
Separation of human small-intestinal sucrase from isomaltase
FEBS Lett.
35
303-305
1973
Homo sapiens
brenda
Yamamoto, M.; Horikoshi, K.
Purification and properties of an oligo-1,6-glucosidase from alkalophilic Bacillus species
Carbohydr. Res.
197
227-235
1990
Bacillus sp. F5
brenda
Watanabe, K.; Kitamura, K.; Hata, Y.; Katsube, Y.; Suzuki, Y.
Overproduction, purification and crystallization of Bacillus cereus oligo-1,6-glucosidase
FEBS Lett.
290
221-223
1991
Bacillus cereus
brenda
Wu, G.D.; Wang, W.; Traber, P.G.
Isolation and characterization of the human sucrase-isomaltase gene and demonstration of intestine-specific transcriptional elements
J. Biol. Chem.
267
7863-7870
1992
Homo sapiens
brenda
Watanabe, K.; Hata, Y.; Kizaki, K; Katsube, Y.; Suzuki, Y.
The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 A resolution. Structural characterization of proline-substitution sites for protein thermostabilization
J. Mol. Biol.
269
142-153
1997
Bacillus cereus
brenda
Broyart, J.P.; Hugot, J.P.; Perret, C.; Porteu, A.
Molecular cloning and characterization of a rat intestinal sucrase-isomaltase cDNA. Regulation of sucrase-isomaltase gene expression by sucrose feeding
Biochim. Biophys. Acta
1087
61-67
1990
Rattus norvegicus
brenda
Wiltz, O.; O'Hara, C.J.; Steele, G.D.; Mercurio, A.M.
Expression of enzymatically active sucrase-isomaltase is a ubiquitous property of colon adenocarcinomas
Gastroenterology
100
1266-1278
1991
Homo sapiens
brenda
Khan, N.A.; Eaton, N.R.
Purification and characterization of maltase and alpha-methyl glucosidase from yeast
Biochim. Biophys. Acta
146
173-180
1967
Saccharomyces cerevisiae
brenda
van den Broek, L.A.M.; Struijs, K.; Verdoes, J.C.; Beldman, G.; Voragen, A.G.J.
Cloning and characterization of two alpha-glucosidases from Bifidobacterium adolescentis DSM20083
Appl. Microbiol. Biotechnol.
61
55-60
2003
Bifidobacterium adolescentis (Q9AF93), Bifidobacterium adolescentis
brenda
Lohse, A.; Hardlei, T.; Jensen, A.; Plesner, I.W.; Bols, M.
Investigation of the slow inhibition of almond beta-glucosidase and yeast isomaltase by 1-azasugar inhibitors: evidence for the 'direct binding' model
Biochem. J.
349
211-215
2000
Saccharomyces cerevisiae
brenda
Takesue, Y.; Yokota, K.; Oda, S.; Takesue, S.
Comparison of sucrase-free isomaltase with sucrase-isomaltase purified from the house musk shrew Suncus murinus
Biochim. Biophys. Acta
1544
341-349
2001
Suncus murinus
brenda
Watanabe, K.; Miyake, K.; Suzuki, Y.
Identification of catalytic and substrate-binding site residues in Bacillus cereus ATCC7064 oligo-1,6-glucosidase
Biosci. Biotechnol. Biochem.
65
2058-2064
2001
Bacillus cereus
brenda
Toda, M.; Kawabata, J.; Kasai, T.
Inhibitory effects of ellagi- and gallotannins on rat intestinal alpha-glucosidase complexes
Biosci. Biotechnol. Biochem.
65
542-547
2001
Rattus norvegicus
brenda
Watanabe, K.; Fujiwara, H.; Inui, K.; Suzuki, Y.
Oligo-1,6-glucosidase from a thermophile, Bacillus thermoglucosidasius KP1006, was efficiently produced by combinatorial expression of GroEL in Escherichia coli
Biotechnol. Appl. Biochem.
35
35-43
2002
Parageobacillus thermoglucosidasius, Parageobacillus thermoglucosidasius KP1006
brenda
Hertel, S.; Heinz, F.; Vogel, M.
Hydrolysis of low-molecular-weight oligosaccharides and oligosaccharide alditols by pig intestinal sucrase/isomaltase and glucosidase/maltase
Carbohydr. Res.
326
264-276
2000
Sus scrofa
brenda
Oslancova, A.; Janecek, A.
Oligo-1,6-glucosidase and neopullulanase enzyme subfamilies from the alpha-amylase family defined by the fifth conserved sequence region
Cell. Mol. Life Sci.
59
1945-1959
2002
Bacillus cereus, Weizmannia coagulans, Bacillus flavocaldarius, Bacillus sp. (in: Bacteria), Parageobacillus thermoglucosidasius, Erwinia rhapontici, Bacillus subtilis (Q9F4G4), Bacillus sp. (in: Bacteria) F5
brenda
Frandsen, T.P.; Palcic, M.M.; Svensson, B.
Substrate recognition by three family 13 yeast alpha-glucosidases. Evaluation of deoxygenated and conformationally biased isomaltosides
Eur. J. Biochem.
269
728-734
2002
Saccharomyces cerevisiae
brenda
Finn, A.L.; Kuzhikandathil, E.V.; Oxford, G.S.; Itoh-Lindstrom, Y.
Sucrase-isomaltase is an adenosine 3',5'-cyclic monophosphate-dependent epithelial chloride channel
Gastroenterology
120
117-125
2001
Necturus sp.
brenda
Yamaguchi, K.; Morimoto, N.; Wang, Y.; Watanabe, K.; Unno, T.; Ito, H.; Matsui, H.
Cloning and expression of an oligo-1,6-glucosidase gene from Arthrobacter globiformis I42 and biochemical characterization of the recombinant enzyme
J. Appl. Glycosci.
51
37-40
2004
Arthrobacter globiformis, Arthrobacter globiformis I42
-
brenda
Noguchi, A.; Yano, M.; Ohshima, Y.; Hemmi, H.; Inohara-ochiai, M.; Okada, M.; Min, K.s.; Nakayama, T.; Nishino, T.
Deciphering the molecular basis of the broad substrate specificity of alpha-glucosidase from Bacillus sp. SAM1606
J. Biochem.
134
543-550
2003
Bacillus sp. (in: Bacteria), Bacillus sp. (in: Bacteria) SAM1606
brenda
Proepsting, M.J.; Jacob, R.; Naim, H.Y.
A glutamine to proline exchange at amino acid residue 1098 in sucrase causes a temperature-sensitive arrest of sucrase-isomaltase in the endoplasmic reticulum and cis-Golgi
J. Biol. Chem.
278
16310-16314
2003
Homo sapiens
brenda
Gu, N.; Adachi, T.; Takeda, J.; Aoki, N.; Tsujimoto, G.; Ishihara, A.; Tsuda, K.; Yasuda, K.
Sucrase-isomaltase gene expression is inhibited by mutant hepatocyte nuclear factor (HNF)-1alpha and mutant HNF-1beta in Caco-2 cells
J. Nutr. Sci. Vitaminol.
52
105-112
2006
Homo sapiens
brenda
Bosse, T.; Fialkovich, J.J.; Piaseckyj, C.M.; Beuling, E.; Broekman, H.; Grand, R.J.; Montgomery, R.K.; Krasinski, S.D.
Gata4 and Hnf1alpha are partially required for the expression of specific intestinal genes during development
Am. J. Physiol. Gastrointest. Liver Physiol.
292
G1302-G1314
2007
Mus musculus
brenda
Gu, N.; Adachi, T.; Matsunaga, T.; Tsujimoto, G.; Ishihara, A.; Yasuda, K.; Tsuda, K.
HNF-1alpha participates in glucose regulation of sucrase-isomaltase gene expression in epithelial intestinal cells
Biochem. Biophys. Res. Commun.
353
617-622
2007
Homo sapiens
brenda
Suzuki, T.; Mochizuki, K.; Goda, T.
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
Biochem. Biophys. Res. Commun.
369
788-793
2008
Rattus norvegicus
brenda
Naumoff, D.G.
Structure and evolution of the mammalian maltase-glucoamylase and sucrase-isomaltase genes
Mol. Biol.
41
962-973
2007
Bos taurus, Canis lupus familiaris, Homo sapiens (P14410), Macaca mulatta, Mus musculus, Oryctolagus cuniculus (P07768), Pan troglodytes, Rattus norvegicus (P23739), Suncus murinus (O62653)
-
brenda
Yamamoto, K.; Miyake, H.; Kusunoki, M.; Osaki, S.
Crystallization and preliminary X-ray analysis of isomaltase from Saccharomyces cerevisiae
Acta Crystallogr. Sect. F
64
1024-1026
2008
Saccharomyces cerevisiae
brenda
Pokusaeva, K.; OConnell-Motherway, M.; Zomer, A.; Fitzgerald, G.F.; van Sinderen, D.
Characterization of two novel alpha-glucosidases from Bifidobacterium breve UCC2003
Appl. Environ. Microbiol.
75
1135-1143
2009
Bifidobacterium breve (C0JP82), Bifidobacterium breve (C0JP83), Bifidobacterium breve UCC2003 (C0JP82), Bifidobacterium breve UCC2003 (C0JP83), Bifidobacterium breve UCC2003
brenda
Minami, Y.; Kuriyama, C.; Ikeda, K.; Kato, A.; Takebayashi, K.; Adachi, I.; Fleet, G.W.; Kettawan, A.; Okamoto, T.; Asano, N.
Effect of five-membered sugar mimics on mammalian glycogen-degrading enzymes and various glucosidases
Bioorg. Med. Chem.
16
2734-2740
2008
Rattus sp.
brenda
Yorita, S.; Mochizuki, K.; Goda, T.
Induction of histone acetylation on the sucrase-isomaltase gene in the postnatal rat jejunum
Biosci. Biotechnol. Biochem.
73
933-935
2009
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
brenda
Quezada-Calvillo, R.; Sim, L.; Ao, Z.; Hamaker, B.R.; Quaroni, A.; Brayer, G.D.; Sterchi, E.E.; Robayo-Torres, C.C.; Rose, D.R.; Nichols, B.L.
Luminal starch substrate "brake" on maltase-glucoamylase activity is located within the glucoamylase subunit
J. Nutr.
138
685-692
2008
Homo sapiens
brenda
Wetzel, G.; Heine, M.; Rohwedder, A.; Naim, H.Y.
Impact of glycosylation and detergent-resistant membranes on the function of intestinal sucrase-isomaltase
Biol. Chem.
390
545-549
2009
Homo sapiens
brenda
Sim, L.; Willemsma, C.; Mohan, S.; Naim, H.Y.; Pinto, B.M.; Rose, D.R.
Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains
J. Biol. Chem.
285
17763-17770
2010
Homo sapiens (P14410)
brenda
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
Bioorg. Med. Chem.
19
3929-3934
2011
Homo sapiens (P14410)
brenda
Eskandari, R.; Jones, K.; Rose, D.R.; Pinto, B.M.
Selectivity of 3-O-methylponkoranol for inhibition of N- and C-terminal maltase glucoamylase and sucrase isomaltase, potential therapeutics for digestive disorders or their sequelae
Bioorg. Med. Chem. Lett.
21
6491-6494
2011
Homo sapiens
brenda
Yamamoto, K.; Miyake, H.; Kusunoki, M.; Osaki, S.
Crystal structures of isomaltase from Saccharomyces cerevisiae and in complex with its competitive inhibitor maltose
FEBS J.
277
4205-4214
2010
Saccharomyces cerevisiae (P53051), Saccharomyces cerevisiae
brenda
Teste, M.A.; Francois, J.M.; Parrou, J.L.
Characterization of a new multigene family encoding isomaltases in the yeast Saccharomyces cerevisiae, the IMA family
J. Biol. Chem.
285
26815-26824
2010
Saccharomyces cerevisiae
brenda
Choi, K.H.; Hwang, S.; Cha, J.
Identification and characterization of MalA in the maltose/maltodextrin operon of Sulfolobus acidocaldarius DSM639
J. Bacteriol.
195
1789-1799
2013
Sulfolobus acidocaldarius (Q4J9M3), Sulfolobus acidocaldarius DSM 639 (Q4J9M3)
brenda
Natori, Y.; Sakuma, T.; Yoshimura, Y.; Kinami, K.; Hirokami, Y.; Sato, K.; Adachi, I.; Kato, A.; Takahata, H.
Synthesis and biological evaluation of alpha-1-C-4'-arylbutyl-L-arabinoiminofuranoses, a new class of alpha-glucosidase inhibitors
Bioorg. Med. Chem. Lett.
24
3298-3301
2014
Rattus norvegicus
brenda
Deng, X.; Petitjean, M.; Teste, M.; Kooli, W.; Tranier, S.; Francois, J.; Parrou, J.
Similarities and differences in the biochemical and enzymological properties of the four isomaltases from Saccharomyces cerevisiae
FEBS Open Bio
4
200-212
2014
Saccharomyces cerevisiae (P0CW40), Saccharomyces cerevisiae (P40884), Saccharomyces cerevisiae (P53051), Saccharomyces cerevisiae (Q08295)
brenda
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
Hum. Mol. Genet.
22
2273-2282
2013
Homo sapiens (P14410)
brenda
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.
57
704-712
2013
Mus musculus
brenda
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.
101
973-982
2017
Alkalihalophilus pseudofirmus, Alkalihalophilus pseudofirmus 703
brenda
Delgado, S.; Florez, A.B.; Guadamuro, L.; Mayo, B.
Genetic and biochemical characterization of an oligo-alpha-1,6-glucosidase from Lactobacillus plantarum
Int. J. Food Microbiol.
246
32-39
2017
Lactiplantibacillus plantarum subsp. plantarum (D7VFY4), Lactiplantibacillus plantarum subsp. plantarum ATCC 149917 (D7VFY4), Lactiplantibacillus plantarum subsp. plantarum LL441 (D7VFY4)
brenda
Gericke, B.; Schecker, N.; Amiri, M.; Naim, H.Y.
Structure-function analysis of human sucrase-isomaltase identifies key residues required for catalytic activity
J. Biol. Chem.
292
11070-11078
2017
Homo sapiens (P14410)
brenda
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