Information on EC 3.2.1.10 - oligo-1,6-glucosidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY
3.2.1.10
-
RECOMMENDED NAME
GeneOntology No.
oligo-1,6-glucosidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by EC 3.2.1.1 (alpha-amylase), and in isomaltose
show the reaction diagram
-
-
-
-
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by EC 3.2.1.1 (alpha-amylase), and in isomaltose
show the reaction diagram
enzyme from intestinal mucosa also catalyzes the reaction of sucrase alpha-glucosidase, EC 3.2.1.48
-
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by EC 3.2.1.1 (alpha-amylase), and in isomaltose
show the reaction diagram
enzyme from intestinal mucosa also catalyzes the reaction of sucrase alpha-glucosidase, EC 3.2.1.48
-
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by EC 3.2.1.1 (alpha-amylase), and in isomaltose
show the reaction diagram
enzyme from intestinal mucosa also catalyzes the reaction of sucrase alpha-glucosidase, EC 3.2.1.48
-
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by EC 3.2.1.1 (alpha-amylase), and in isomaltose
show the reaction diagram
enzyme from intestinal mucosa also catalyzes the reaction of sucrase alpha-glucosidase, EC 3.2.1.48
-
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by EC 3.2.1.1 (alpha-amylase), and in isomaltose
show the reaction diagram
enzyme from intestinal mucosa also catalyzes the reaction of sucrase alpha-glucosidase, EC 3.2.1.48
-
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by EC 3.2.1.1 (alpha-amylase), and in isomaltose
show the reaction diagram
enzyme from intestinal mucosa also catalyzes the reaction of sucrase alpha-glucosidase, EC 3.2.1.48
-
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by EC 3.2.1.1 (alpha-amylase), and in isomaltose
show the reaction diagram
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
-
Hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by EC 3.2.1.1 (alpha-amylase), and in isomaltose
show the reaction diagram
stereochemistry, molecular substrate recognition mechanism, catayltic mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Galactose metabolism
-
-
Metabolic pathways
-
-
Starch and sucrose metabolism
-
-
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.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Oligosaccharide alpha-1,6-glucosidase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9032-15-9
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Arthrobacter globiformis I42
strain I42
-
-
Manually annotated by BRENDA team
GenPept accession number CAA37583.1
-
-
Manually annotated by BRENDA team
strain ATCC 7064
-
-
Manually annotated by BRENDA team
Bacillus cereus NY-14
NY-14
-
-
Manually annotated by BRENDA team
GenPept accession number BAA11354.1
-
-
Manually annotated by BRENDA team
GenPept accession number BAB18518.1
-
-
Manually annotated by BRENDA team
strain F5, GenPept accession number BAA00534.1
-
-
Manually annotated by BRENDA team
strain SAM1606
-
-
Manually annotated by BRENDA team
Bacillus sp. SAM1606
strain SAM1606
-
-
Manually annotated by BRENDA team
GenPept accession number AAG23399.1
SwissProt
Manually annotated by BRENDA team
Bacillus thermoamyloliquefaciens KP1071
-
-
-
Manually annotated by BRENDA team
strain DSM 20083, gene aglA
SwissProt
Manually annotated by BRENDA team
strain UCC2003
UniProt
Manually annotated by BRENDA team
Alaskan fur seal
-
-
Manually annotated by BRENDA team
GenPept accession number AAK28737.1
-
-
Manually annotated by BRENDA team
formerly Bacillus thermoglucosidius; KP 1006
-
-
Manually annotated by BRENDA team
GenPept accession number BAA01368.1
-
-
Manually annotated by BRENDA team
Geobacillus thermoglucosidasius KP 1006
KP 1006
-
-
Manually annotated by BRENDA team
Geobacillus thermoglucosidasius KP1006
strain KP1006
-
-
Manually annotated by BRENDA team
GH31 module subject to phylogenetic analysis
UniProt
Manually annotated by BRENDA team
barley
-
-
Manually annotated by BRENDA team
Necturus sp.
-
-
-
Manually annotated by BRENDA team
GH31 module subject to phylogenetic analysis
SwissProt
Manually annotated by BRENDA team
enzyme complex of sucrase and isomaltase integrated into the intestinal alpha-glucosidase function with the complex of maltase-glucoamylase
-
-
Manually annotated by BRENDA team
GH31 module subject to phylogenetic analysis
SwissProt
Manually annotated by BRENDA team
Sprague-Dawley
-
-
Manually annotated by BRENDA team
Sprague-Dawley, male
-
-
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
Sprague-Dawley
-
-
Manually annotated by BRENDA team
isoform Ima1
UniProt
Manually annotated by BRENDA team
isoform Ima2
UniProt
Manually annotated by BRENDA team
isoform Ima3
UniProt
Manually annotated by BRENDA team
isoform Ima5
UniProt
Manually annotated by BRENDA team
several strains, 5 genes IMA1 to IMA5, i.e. YGR287c, YIL172c, YJL216c, YJL221c and YOL157c. Gene IMA1/YGR287c encodes the major isomaltase
-
-
Manually annotated by BRENDA team
GH31 module subject to phylogenetic analysis
SwissProt
Manually annotated by BRENDA team
house musk shrew, contains 2 enzyme forms: a sucrase-free isomaltase and a sucrase-isomaltase
-
-
Manually annotated by BRENDA team
enzyme SI, bifunctional enzyme with sucrase and isomaltase activity
-
-
Manually annotated by BRENDA team
Thermoanaerobium sp.
Tok6-B1
-
-
Manually annotated by BRENDA team
Thermoanaerobium sp. Tok6-B1
Tok6-B1
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
additional information
P53051
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
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,6-di-O-alpha-D-glucitol + H2O
D-glucitol
show the reaction diagram
-
-
-
-
?
1,6-di-O-alpha-D-glucopyranosyl-D-fructofuranose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
-
?
1,6-di-O-alpha-D-mannitol + H2O
D-mannitol
show the reaction diagram
-
-
-
-
?
1-O-alpha-D-glucopyranosyl-D-fructopyranose + H2O
D-fructose
show the reaction diagram
-
-
-
-
?
1-O-alpha-D-glucopyranosyl-D-glucitol + H2O
D-glucose + D-glucitol
show the reaction diagram
-
-
-
-
?
1-O-alpha-D-glucopyranosyl-D-mannitol + H2O
D-glucose + D-mannitol
show the reaction diagram
-
-
-
-
?
2'-deoxy-methyl-alpha-isomaltoside + H2O
?
show the reaction diagram
-
-
-
-
?
2-deoxy-methyl-alpha-isomaltoside + H2O
?
show the reaction diagram
-
-
-
-
?
3'-deoxy-methyl-alpha-isomaltoside + H2O
?
show the reaction diagram
-
-
-
-
?
3-deoxy-methyl-alpha-isomaltoside + H2O
?
show the reaction diagram
-
-
-
-
?
4'-deoxy-methyl-alpha-isomaltoside + H2O
?
show the reaction diagram
-
-
-
-
?
4-deoxy-methyl-alpha-isomaltoside + H2O
?
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl alpha-D-glucoside + H2O
4-methylumbelliferol + alpha-D-glucose
show the reaction diagram
Q9AF93
-
-
-
?
4-methylumbelliferyl beta-D-glucoside + H2O
4-methylumbelliferol + beta-D-glucose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl 1-O-alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
show the reaction diagram
Bacillus sp., Bacillus sp. SAM1606
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside
4-nitrophenol + alpha-D-glucopyranose
show the reaction diagram
-
-
-
-
-
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
show the reaction diagram
Q9AF93
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
show the reaction diagram
P14410
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
show the reaction diagram
P0CW40, P40884, P53051, Q08295
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
show the reaction diagram
Geobacillus thermoglucosidasius KP1006
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
show the reaction diagram
Arthrobacter globiformis I42
-
-
-
-
?
4-O-alpha-D-glucopyranosyl-D-glucopyranose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
6'-deoxy-methyl-alpha-isomaltoside + H2O
?
show the reaction diagram
-
-
-
-
?
6(R)-ethyl-alpha-isomaltoside + H2O
?
show the reaction diagram
-
-
-
-
?
6(S)-ethyl-alpha-isomaltoside + H2O
?
show the reaction diagram
-
-
-
-
?
6-O-alpha-D-glucopyranosyl-D-fructofuranose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
-
?
6-O-alpha-D-glucopyranosyl-D-glucitol + H2O
D-glucose + D-glucitol
show the reaction diagram
-
-
-
-
?
6-O-alpha-D-glucopyranosyl-D-glucopyranose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-1)-D-glucitol + H2O
D-glucose + D-glucitol
show the reaction diagram
-
-
-
-
?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-1)-D-mannitol + H2O
D-glucose + D-mannitol
show the reaction diagram
-
-
-
-
?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-1)-D-mannitol + H2O
D-glucose + D-mannitol
show the reaction diagram
-
-
-
-
?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-glucitol + H2O
D-glucose + D-glucitol
show the reaction diagram
-
-
-
-
?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-D-fructofuranose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
-
?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-fructofuranose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
-
?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-glucitol + H2O
D-glucose + D-glucitol
show the reaction diagram
-
-
-
-
?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-glucopyranose + H2O
D-glucose
show the reaction diagram
-
-
-
-
?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-D-fructofuranose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
-
?
alpha-D-glucopyranosyl-(1-6)-beta-fructofuranosyl-alpha-D-glucopyranoside + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
-
?
alpha-limit dextrin + H2O
?
show the reaction diagram
-
-
-
-
?
alpha-limit dextrins + H2O
D-glucose
show the reaction diagram
-
-
-
?
alpha-limit dextrins + H2O
D-glucose
show the reaction diagram
-
-
-
?
alpha-limit dextrins + H2O
D-glucose
show the reaction diagram
-
-
-
?
alpha-limit dextrins + H2O
D-glucose
show the reaction diagram
-
-
-
?
amylose + H2O
?
show the reaction diagram
-
n = 18, low activity of wild-type sucrase-isomaltase, very low activity of mutant isomaltase
-
-
?
glycogen + H2O
?
show the reaction diagram
-
substrate from oyster, low activity of wild-type sucrase-isomaltase, very low activity of mutant isomaltase
-
-
?
isomaltosaccharides + H2O
D-glucose
show the reaction diagram
-
-
-
?
isomaltosaccharides + H2O
D-glucose
show the reaction diagram
-
-
-
?
isomaltosaccharides + H2O
D-glucose
show the reaction diagram
-
n = 2-6
-
-
-
isomaltosaccharides + H2O
D-glucose
show the reaction diagram
-
n = 2-6
-
?
isomaltosaccharides + H2O
D-glucose
show the reaction diagram
-
n = 2-6
-
?
isomaltosaccharides + H2O
D-glucose
show the reaction diagram
-
n = 3-5
-
-
-
isomaltosaccharides + H2O
D-glucose
show the reaction diagram
Thermoanaerobium sp.
-
n = 2-3
-
?
isomaltosaccharides + H2O
D-glucose
show the reaction diagram
-
n = 2, isomaltose
-
?
isomaltosaccharides + H2O
D-glucose
show the reaction diagram
-
n = 2, isomaltose
-
?
isomaltosaccharides + H2O
D-glucose
show the reaction diagram
-
n = 2, isomaltose
-
?
isomaltosaccharides + H2O
D-glucose
show the reaction diagram
-
n = 2, isomaltose
-
?
isomaltosaccharides + H2O
D-glucose
show the reaction diagram
-
n = 2, isomaltose
-
?
isomaltosaccharides + H2O
D-glucose
show the reaction diagram
-
n = 2, isomaltose
-
?
isomaltosaccharides + H2O
D-glucose
show the reaction diagram
Geobacillus thermoglucosidasius KP 1006
-
-
-
?
isomaltosaccharides + H2O
D-glucose
show the reaction diagram
Bacillus cereus NY-14
-
-
-
?
isomaltose + H2O
D-glucose
show the reaction diagram
-
-
-
?
isomaltose + H2O
D-glucose
show the reaction diagram
-
-
-
?
isomaltose + H2O
D-glucose
show the reaction diagram
-
-
-
?
isomaltose + H2O
D-glucose
show the reaction diagram
-
-
-
?
isomaltose + H2O
D-glucose
show the reaction diagram
-
-
-
?
isomaltose + H2O
D-glucose
show the reaction diagram
-
-
-
-
-
isomaltose + H2O
D-glucose
show the reaction diagram
-
-
-
?
isomaltose + H2O
D-glucose
show the reaction diagram
Thermoanaerobium sp.
-
-
-
?
isomaltose + H2O
D-glucose
show the reaction diagram
-
-
-
-
-
isomaltose + H2O
D-glucose
show the reaction diagram
-
-
-
?
isomaltose + H2O
D-glucose
show the reaction diagram
-
-
-
?
isomaltose + H2O
D-glucose
show the reaction diagram
-
-
-
?
isomaltose + H2O
D-glucose
show the reaction diagram
P14410
-
-
-
?
isomaltose + H2O
D-glucose
show the reaction diagram
-
best substrate for the mutant isomaltase
-
-
?
isomaltose + H2O
D-glucose
show the reaction diagram
Geobacillus thermoglucosidasius KP 1006
-
-
-
?
isomaltose + H2O
D-glucose
show the reaction diagram
Geobacillus thermoglucosidasius KP 1006
-
-
-
-
-
isomaltose + H2O
D-glucose
show the reaction diagram
Thermoanaerobium sp. Tok6-B1
-
-
-
?
isomaltose + H2O
D-glucose
show the reaction diagram
Bacillus cereus NY-14
-
-
-
?
isomaltose + H2O
?
show the reaction diagram
-
-
-
-
?
isomaltose + H2O
?
show the reaction diagram
-
-
-
-
?
isomaltose + H2O
?
show the reaction diagram
Q9AF93
-
-
-
?
isomaltose + H2O
?
show the reaction diagram
Bacillus sp. SAM1606
-
-
-
-
?
isomaltose + H2O
?
show the reaction diagram
Arthrobacter globiformis I42
-
-
-
-
?
isomaltose + H2O
alpha-D-glucose + D-glucose
show the reaction diagram
C0JP82, C0JP83
-
-
-
?
isomaltose + H2O
alpha-D-glucose + D-glucose
show the reaction diagram
C0JP82, C0JP83
-
-
-
?
isomaltose + H2O
alpha-D-glucose
show the reaction diagram
Q4J9M3
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
2 D-glucose
show the reaction diagram
P0CW40, P40884, P53051, Q08295
-
-
-
?
isomaltotriose + H2O
3 alpha-D-glucose
show the reaction diagram
C0JP82, C0JP83
-
-
-
?
isomaltotriose + H2O
3 alpha-D-glucose
show the reaction diagram
C0JP82, C0JP83
-
-
-
?
isomaltriose + H2O
?
show the reaction diagram
Q9AF93
-
-
-
?
isomaltriose + H2O
?
show the reaction diagram
P0CW40, P40884, P53051, Q08295
-
-
-
?
kojibiose + H2O
D-glucose
show the reaction diagram
-
weak activity
-
?
maltodextrin + H2O
?
show the reaction diagram
-
corn maltodextrin
-
-
?
maltoheptaose + H2O
?
show the reaction diagram
-
low activity of mutant isomaltase
-
-
?
maltohexaose + H2O
?
show the reaction diagram
-
low activity of mutant isomaltase
-
-
?
maltopentaose + H2O
?
show the reaction diagram
-
-
-
-
?
maltopentose + H2O
?
show the reaction diagram
-
-
-
-
?
maltose + H2O
D-glucose
show the reaction diagram
-
-
-
?
maltose + H2O
D-glucose
show the reaction diagram
-
-
-
?
maltose + H2O
D-glucose
show the reaction diagram
-
-
-
?
maltose + H2O
D-glucose
show the reaction diagram
-
-
-
?
maltose + H2O
D-glucose
show the reaction diagram
-
-
-
?
maltose + H2O
D-glucose
show the reaction diagram
-
-
-
?
maltose + H2O
D-glucose
show the reaction diagram
P14410
-
-
-
?
maltose + H2O
D-glucose
show the reaction diagram
-
best substrate of the wild-type sucrase-isomaltase
-
-
?
maltose + H2O
D-glucose + D-glucose
show the reaction diagram
-
-
-
-
?
maltotetraose + H2O
?
show the reaction diagram
-
-
-
-
?
maltotetraose + H2O
?
show the reaction diagram
-
low activity of mutant isomaltase
-
-
?
maltotriitol + H2O
D-glucose + maltitol
show the reaction diagram
-
-
-
?
maltotriose + H2O
?
show the reaction diagram
-
-
-
-
?
maltotriose + H2O
?
show the reaction diagram
-
low activity of mutant isomaltase
-
-
?
maltotriose + H2O
D-glucose
show the reaction diagram
-
-
-
?
maltulose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
C0JP82, C0JP83
-
-
-
?
maltulose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
C0JP82, C0JP83
-
-
-
?
methyl alpha-D-glucopyranoside + H2O
methanol + alpha-D-glucopyranose
show the reaction diagram
P0CW40, P40884, P53051, Q08295
-
-
-
?
nigerose + H2O
2 D-glucose
show the reaction diagram
Thermoanaerobium sp.
-
weak activity
-
?
nigerose + H2O
2 D-glucose
show the reaction diagram
Geobacillus thermoglucosidasius, Geobacillus thermoglucosidasius KP 1006
-
weak activity
-
?
nigerose + H2O
2 D-glucose
show the reaction diagram
Thermoanaerobium sp. Tok6-B1
-
weak activity
-
?
nigerose + H2O
alpha-D-glucose + D-glucose
show the reaction diagram
C0JP82, C0JP83
-
-
-
?
nigerose + H2O
alpha-D-glucose + D-glucose
show the reaction diagram
C0JP82, C0JP83
-
-
-
?
oligosaccharide + H2O
monosaccharide
show the reaction diagram
-
role in digestion of carbohydrates
-
?
oligosaccharide + H2O
monosaccharide
show the reaction diagram
-
role in starch degradation
-
?
oligosaccharide + H2O
monosaccharide
show the reaction diagram
-
role in absorption of sucrose, isomaltose, maltose
-
?
oligosaccharide + H2O
monosaccharide
show the reaction diagram
-
direct function in maltose and isomaltose metabolism
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
show the reaction diagram
Thermoanaerobium sp.
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
show the reaction diagram
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
show the reaction diagram
Bacillus flavocaldarius, Bacillus thermoamyloliquefaciens KP1071
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
show the reaction diagram
Geobacillus thermoglucosidasius KP 1006
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
show the reaction diagram
Geobacillus thermoglucosidasius KP 1006
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
show the reaction diagram
Geobacillus thermoglucosidasius KP 1006
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
D-glucose + p-nitrophenol
show the reaction diagram
Geobacillus thermoglucosidasius KP 1006
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
show the reaction diagram
-
-
-
-
?
palatinose + H2O
D-glucose + fructose
show the reaction diagram
-
-
-
?
palatinose + H2O
D-glucose + fructose
show the reaction diagram
-
-
-
?
palatinose + H2O
D-glucose + fructose
show the reaction diagram
-
-
-
?
palatinose + H2O
D-glucose + fructose
show the reaction diagram
-
-
-
?
palatinose + H2O
D-glucose + fructose
show the reaction diagram
-
-
-
?
palatinose + H2O
D-glucose + fructose
show the reaction diagram
-
-
-
?
palatinose + H2O
D-glucose + fructose
show the reaction diagram
Thermoanaerobium sp., Thermoanaerobium sp. Tok6-B1
-
weak aktivity
-
?
palatinose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
C0JP82, C0JP83
-
-
-
?
palatinose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
C0JP82, C0JP83
-
-
-
?
palatinose + H2O
D-glucose + D-fructose
show the reaction diagram
P0CW40, P40884, P53051, Q08295
-
-
-
?
panitol
glucitol + maltitol
show the reaction diagram
-
-
-
?
panose + H2O
D-glucose + maltose
show the reaction diagram
-
-
-
?
panose + H2O
D-glucose + maltose
show the reaction diagram
-
-
-
?
panose + H2O
D-glucose + maltose
show the reaction diagram
-
-
-
?
panose + H2O
D-glucose + maltose
show the reaction diagram
Thermoanaerobium sp.
-
-
-
?
panose + H2O
D-glucose + maltose
show the reaction diagram
-
-
-
?
panose + H2O
D-glucose + maltose
show the reaction diagram
-
-
-
?
panose + H2O
D-glucose + maltose
show the reaction diagram
Geobacillus thermoglucosidasius KP 1006
-
-
-
?
panose + H2O
D-glucose + maltose
show the reaction diagram
Thermoanaerobium sp. Tok6-B1
-
-
-
?
panose + H2O
alpha-D-glucose
show the reaction diagram
Q4J9M3
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
alpha-D-glucose + maltose
show the reaction diagram
C0JP82, C0JP83
preference for the cleavage of the alpha-1,6 linkage
-
-
?
phenyl-alpha-D-glucopyranoside + H2O
D-glucose + phenol
show the reaction diagram
-
-
-
-
-
phenyl-alpha-D-glucopyranoside + H2O
D-glucose + phenol
show the reaction diagram
-
-
-
?
pullulan + H2O
?
show the reaction diagram
-
low activity
-
-
?
pullulan + H2O
D-glucose + maltose
show the reaction diagram
-
-
-
?
soluble starch + H2O
?
show the reaction diagram
-
low activity of wild-type sucrase-isomaltase, very low activity of mutant isomaltase
-
-
?
sucrose + H2O
D-fructose + D-glucose
show the reaction diagram
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
P0CW40, P40884, P53051, Q08295
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
small activity
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
wild-type sucrase-isomaltase, no activity with the mutant isomaltase
-
-
?
trehalose + H2O
?
show the reaction diagram
-
-
-
-
?
trehalose + H2O
?
show the reaction diagram
Q9AF93
low activity
-
-
?
trehalose + H2O
?
show the reaction diagram
Bacillus sp. SAM1606
-
-
-
-
?
trehalose + H2O
2 alpha-D-glucose
show the reaction diagram
C0JP82, C0JP83
-
-
-
?
trehalulose + H2O
alpha-D-glucose + beta-D-fructose
show the reaction diagram
C0JP82, C0JP83
-
-
-
?
turanose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
turanose + H2O
alpha-D-glucose + beta-D-fructose
show the reaction diagram
C0JP82, C0JP83
-
-
-
?
methyl-alpha-isomaltoside + H2O
?
show the reaction diagram
-
-
-
-
?
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 maltase activity
-
-
-
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
?
-
-
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
?
-
Q9F4G4
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
?
-
-
the enzyme might be involved in degradation for utilization of dextran in the bacterium
-
-
-
additional information
?
-
Necturus sp.
-
enzyme can also function as a cAMP-dependent chloride channel
-
-
-
additional information
?
-
-
enzyme is highly specific for alpha-1,6-linkages
-
-
-
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 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
?
-
Q9AF93
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
?
-
P14410
N-terminal sucrase-isomaltase has a broad specificity for both alpha-1,4- and alpha-1,6-oligosaccharides
-
-
-
additional information
?
-
-
substrate specificities of isozymes IMA1 to IMA5, overview
-
-
-
additional information
?
-
P53051
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 enzyme is active with maltose, maltotriose, and sucrose, only the N-terminal catalytic domain acts as alpha-1,6-glucosidase
-
-
-
additional information
?
-
P0CW40, P40884, P53051, Q08295
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
?
-
P0CW40, P40884, P53051, Q08295
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
?
-
Geobacillus thermoglucosidasius KP1006
-
N-terminal domain alpha/beta motifs are probably recognized by the endogenous GroEL protein, leading to binding and stabilization
-
-
-
additional information
?
-
Bacillus sp. 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, enzyme is highly specific for alpha-1,6-linkages
-
-
-
additional information
?
-
Geobacillus thermoglucosidasius KP 1006
-
no maltase activity
-
-
-
additional information
?
-
Thermoanaerobium sp. Tok6-B1
-
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
?
-
Arthrobacter globiformis I42
-
the enzyme might be involved in degradation for utilization of dextran in the bacterium
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
oligosaccharide + H2O
monosaccharide
show the reaction diagram
-
role in digestion of carbohydrates
-
?
oligosaccharide + H2O
monosaccharide
show the reaction diagram
-
role in starch degradation
-
?
oligosaccharide + H2O
monosaccharide
show the reaction diagram
-
role in absorption of sucrose, isomaltose, maltose
-
?
oligosaccharide + H2O
monosaccharide
show the reaction diagram
-
direct function in maltose and isomaltose metabolism
-
?
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
?
-
-
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
?
-
Q9F4G4
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
?
-
-
the enzyme might be involved in degradation for utilization of dextran in the bacterium
-
-
-
additional information
?
-
Bacillus sp. 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
?
-
Arthrobacter globiformis I42
-
the enzyme might be involved in degradation for utilization of dextran in the bacterium
-
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Thermoanaerobium sp.
-
stabilization of activity by 1 mM at pH 5.6, 76C
Mg2+
Thermoanaerobium sp.
-
stabilization of activity by 1 mM at pH 5.6, 76C
Mn2+
Thermoanaerobium sp.
-
stabilization of activity by 1 mM at pH 5.6, 76C
INHIBITORS
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
1,2,3-tri-O-galloyl-beta-D-glucose
-
about 20% inhibition at 1 mM
1,4-anhydro-4-thio-D-arabinitol
-
-
1,4-dideoxy-1,4-((S)-[(2S,3S)-2,4-dihydroxy-3-butyl]episulfoniumylidene)-D-arabinitol
-
-
1,4-dideoxy-1,4-(hydroxyethyliminiumyl)-D-arabinitol
-
-
1,4-dideoxy-1,4-imino-D-arabinitol
-
-
1,4-dideoxy-1,4-imino-L-arabinitol
-
-
1,4-dideoxy-1,4-[(S)-[(2S,3S)-2,4-dihydroxy-3-(sulfooxy)butyl]episulfoniumylidene]-D-arabinitol
-
-
1,4-dideoxy-1,4-[(S)-[(2S,3S)-2,4-dihydroxy-3-butyl]episulfoniumylidene]-D-arabinitol
-
-
1,4-imino-1,2,4-trideoxy-D-arabinitol
-
-
1-O-Galloyl-beta-D-glucose
-
about 15% inhibition at 1 mM, 34.4% inhibition at 5 mM
1-O-methyl-2,3-di-O-galloyl-beta-D-glucose
-
about 10% inhibition at 1 mM
1-O-methyl-alpha-D-glucose
Thermoanaerobium sp.
-
42% inhibition by 62 mM
1-O-methyl-beta-D-glucose
Thermoanaerobium sp.
-
52% inhibition by 62 mM
2,5-dideoxy-2,5-imino-D-glucitol
-
-
2,5-dideoxy-2,5-imino-D-mannitol
-
-
2,5-dideoxy-2,5-imino-L-mannitol
-
-
2-Amino-2-ethyl-1,3-propanediol
-
80% inhibition of isomaltase activity by 50 mM
2-amino-2-methyl-1,3-propanediol
-
almost complete inhibition of isomaltase activity by 50 mM
3'-O-methylponkoranol
-
inhibits the different subunits to different extents, with extraordinary selectivity for C-terminal subunit of the enzyme
4-nitrophenyl alpha-D-glucopyranoside
P0CW40, P40884, P53051, Q08295
-
acarbose
-
-
Ba2+
-
72% inhibition by 2 mM BaCl2
blintol
-
selenium analogue of salacinol
Ca2+
-
29% inhibition by 2 mM CaCl2
casuarictin
-
ellagtannin, from flower buds of Syzygium aromaticum, about 16% inhibition at 1 mM
Cd2+
-
complete inhibition
Chymotrypsin
-
almost 25% of palatinase activity after incubation with 0.1 mg/ml for 30 min
-
Co2+
-
complete inhibition
Co2+
-
96% inhibition by 2 mM in 20 mM borate buffer, pH 7.5 with p-nitrophenyl-alpha-D-glucopyranoside as substrate
conduritol-B-epoxide
-
complete inactivation by 0.024 mM
conduritol-B-epoxide
-
-
Cu2+
-
96% inhibition by 2 mM CuCl2
Cu2+
-
95% inhibition by 2 mM in 20 mM borate buffer, pH 7.5 with p-nitrophenyl-alpha-D-glucopyranoside as substrate
Cu2+
-
complete inhibition by 1 mM CuCl2
D-glucose
Thermoanaerobium sp.
-
product inhibition, inhibition of 70.1% of activity by 110 mM
D-glucose
-
52% inhibition by 10 mM, competitive
D-glucose
-
sucrase-isomaltase gene expression is negatively regulated by glucose
de-O-sulfonated kotalanol
-
isolated from Salacia reticulata
de-O-sulfonated kotalanol
-
-
de-O-sulfonated ponkoranol
-
-
de-O-sulfonated salacinol
-
-
diethanolamine
-
about 80% inhibition of isomaltase activity by 50 mM
DnaJ
-
the coexpression of the Hsp70 team chaperone protein leads to reduced activity
-
DnaK
-
the coexpression of the Hsp70 team chaperone protein leads to reduced activity
-
EDTA
Thermoanaerobium sp.
-
rapid loss of activity at 1 mM, pH 5.6, 76C
EDTA
-
no inhibition by 2 mM at pH 7.5
EDTA
-
no inhibition by 2 mM at pH 7.5
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
Fe2+
-
complete inhibition by 2 mM in 20 mM borate buffer, pH 7.5 with p-nitrophenyl-alpha-D-glucopyranoside as substrate
Fe2+
-
90% inhibition by 1 mM FeCl2
Fe3+
-
86% inhibition by 2 mM FeCl3
gallic acid
-
8% inhibition at 5mM
glucono-delta-lactone
-
57% inhibition by 10 mM, competitive
glucono-delta-lactone
-
-
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
-
Hg2+
-
99% inhibition by 2 mM HgCl2
Hg2+
-
complete inhibition by 2 mM in 20 mM borate buffer, pH 7.5 with p-nitrophenyl-alpha-D-glucopyranoside as substrate
Hg2+
-
complete inhibition by 1 mM HgCl2
isofagomine
-
stereoisomer of (-)-1-azafagomine, racemic, competitive
isomaltose
P0CW40, P40884, P53051, Q08295
-
KCl
-
40% inhibition by 1 M
kotalanol
-
isolated from Salacia reticulata
kotalanol
-
-
maltose
P53051
competitive inhibitor
maltose
P0CW40, P40884, P53051, Q08295
competitive; competitive; mixed
methyl alpha-D-glucopyranoside
P0CW40, P40884, P53051, Q08295
-
Mg2+
-
42% inhibition by 2 mM MgCl2
miglitol
-
-
Mn2+
-
92% inhibition by 2 mM MbCl2
Mn2+
-
40% inhibition by 2 mM in 20 mM borate buffer, pH 7.5 with p-nitrophenyl-alpha-D-glucopyranoside as substrate
Monoethanolamine
-
about 70% inhibition of isomaltase activity by 50 mM
mutant hepatocyte nuclear factor-1alpha
-
in the wild HNF-1alpha cells SI gene expression and enzyme activity is not significantly diminished
-
mutant hepatocyte nuclear factor-1beta
-
in the wild HNF-1beta cells SI gene expression and enzyme activity is not significantly diminished
-
N-ethylmaleimide
Thermoanaerobium sp.
-
70% inactivation by 3.3 mM at room temperature after 10 min
NaCl
-
50% inhibition by 500 mM
Ni2+
-
94% inhibition by 2 mM NiCl2
p-chloromercuribenzoate
-
no inhibition by 2 mM with p-nitrophenyl-alpha-D-glucopyranoside as substrate
p-chloromercuribenzoate
-
complete inhibition by 0.1 mM
p-nitrophenol
-
complete inhibition by 2 mM
p-nitrophenol
-
-
palatinose
P0CW40, P40884, P53051, Q08295
-
Papain
-
proteolytic inactivation at 35C, pH 6.8
-
Pb2+
-
complete inhibition
Pb2+
-
90% inhibition by 2 mM in 20 mM borate buffer, pH 7.5 with p-nitrophenyl-alpha-D-glucopyranoside as substrate
Pb2+
-
complete inhibition by 1 mM PbCl2
penta-O-galloyl-beta-D-glucose
-
about 40% inhibition at 1-5 mM
Phenol
-
in combination with Tris most potent inhibitor
phenyl alpha-D-glucoside
-
58% inhibition by 10 mM
phenyl alpha-D-glucoside
-
-
Phenyl alpha-maltoside
-
92% inhibition by 10 mM, noncompetitive
pronase E
-
proteolytic inactivation at 35C, pH 6.8
-
salacinol
-
isolated from Salacia reticulata
salacinol
-
-
SDS
Thermoanaerobium sp.
-
96% inhibition by 3.5 mM under standard conditions
Sn2+
-
complete inhibition
subtilisin BPN'
-
proteolytic inactivation at 35C, pH 6.8
-
triethanolamine
-
about 80% inhibition of isomaltase activity by 50 mM
Tris
-
complete inhibition of isomaltase activity by 50 mM
Tris
-
89% inhibition by 5 mM, competitive
Tris
-
93% inhibition by 5 mM
Trypsin
-
almost 25% of palatinase activity after incubation with 0.1 mg/ml for 30 min
-
Trypsin
-
proteolytic inactivation at 35C, pH 6.8
-
Urea
Thermoanaerobium sp.
-
26% inhibition by 4 mM under standard conditions
Urea
Bacillus thermoamyloliquefaciens KP1071
-
50% inactivation after treatment with 8.7 M for 5 h at 25C or 2.4 M at 60C and pH 6.8
Urea
-
50% inactivation after treatment with 9.2 M for 5 h at 25C or 2.7 M at 60C and pH 6.8
Urea
-
50% inactivation after treatment with 4.6 M for 5 h at 25C and pH 6.8
Urea
-
50% inactivation after treatment with 1.42 M at 25C or 0.74 M at 35C for 5 h
Zn2+
Thermoanaerobium sp.
-
rapid inactivation by 1 mM possibly through interaction with free thiol groups of the enzyme
Zn2+
-
complete inhibition
Zn2+
-
96% inhibition by 2 mM in 20 mM borate buffer, pH 7.5 with p-nitrophenyl-alpha-D-glucopyranoside as substrate
Zn2+
-
99% inhibition by 1 mM ZnCl2
monoiodoacetate
-
77% inhibition by 1 mM
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
-
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
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
Thermoanaerobium sp.
-
2.3fold increase of activity by 1 mM
dithiothreitol
Thermoanaerobium sp.
-
-
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.012
4-nitrophenyl alpha-D-glucopyranoside
-
recombinant mutant D199N, pH 7.0, 35C
0.015
4-nitrophenyl alpha-D-glucopyranoside
-
recombinant mutant E255Q, pH 7.0, 35C
0.35
4-nitrophenyl alpha-D-glucopyranoside
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
0.48
4-nitrophenyl alpha-D-glucopyranoside
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
0.58
4-nitrophenyl alpha-D-glucopyranoside
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
0.8
4-nitrophenyl alpha-D-glucopyranoside
-
recombinant wild-type enzyme, pH 7.0, 35C
0.89
4-nitrophenyl alpha-D-glucopyranoside
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
0.99
4-nitrophenyl alpha-D-glucopyranoside
-
recombinant mutant H103N, pH 7.0, 35C
1.05
4-nitrophenyl alpha-D-glucopyranoside
Q9AF93
pH 6.5, 30C
1.3
4-nitrophenyl alpha-D-glucopyranoside
-
pH 6.8, 30C
1.3
4-nitrophenyl alpha-D-glucopyranoside
-
in 100 mM MES buffer, pH 6.5, at 37C
1.76
4-nitrophenyl alpha-D-glucopyranoside
-
-
13.3
4-nitrophenyl alpha-D-glucopyranoside
-
recombinant mutant H328N, pH 7.0, 35C
11
isomaltohexaose
-
-
15
isomaltohexaose
-
-
4.6
isomaltopentaose
-
-
13
isomaltopentaose
-
-
21
isomaltopentaose
-
-
0.45
isomaltose
-
-
2.5
isomaltose
-
33 mM sodium maleate buffer, pH 6.8
3
isomaltose
-
-
3.33
isomaltose
-
-
5.3
isomaltose
-
wild-type enzyme, pH 7.2, 35C
6.2
isomaltose
-
-
6.9
isomaltose
-
pH 6.8, 30C
8.3
isomaltose
C0JP82, C0JP83
-
9
isomaltose
C0JP82, C0JP83
-
11.1
isomaltose
-
in 100 mM MES buffer, pH 6.5, at 37C
12.8
isomaltose
-
wild-type sucrase-isomaltase
13
isomaltose
-
mutant N342T, pH 7.2, 35C
13
isomaltose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
13.6
isomaltose
-
mutant isomaltase
14
isomaltose
-
mutant P273G, pH 7.2, 35C
17
isomaltose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C; pH 7.0, 30C
20
isomaltose
-
mutant P273G/N342T, pH 7.2, 35C
24.1
isomaltose
-
-
37
isomaltose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
2.8
isomaltotetraose
-
-
7.4
isomaltotetraose
-
-
13
isomaltotetraose
-
-
1.7
isomaltotriose
-
-
3
isomaltotriose
-
-
4.4
isomaltotriose
-
-
5.5
isomaltotriose
C0JP82, C0JP83
-
11
isomaltotriose
-
-
16.7
isomaltotriose
C0JP82, C0JP83
-
72
isomaltriose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
83
isomaltriose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
128
isomaltriose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
3.6
maltopentose
-
IP-SI, immunoprecipitated human sucrase-isomaltase complex
0.13
maltose
-
-
2.4
maltose
-
33 mM sodium maleate buffer, pH 6.8
6.83
maltose
-
IP-SI, immunoprecipitated human sucrase-isomaltase complex
7
maltose
-
wild-type sucrase-isomaltase
7.1
maltose
-
in 100 mM MES buffer, pH 6.5, at 37C
13.3
maltose
-
-
62.8
maltose
-
mutant isomaltase
3.79
maltotetrose
-
IP-SI, immunoprecipitated human sucrase-isomaltase complex
4
maltotriitol
-
-
1.9
maltotriose
-
-
5.55
maltotriose
-
IP-SI, immunoprecipitated human sucrase-isomaltase complex
15
methyl alpha-D-glucopyranoside
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
27
methyl alpha-D-glucopyranoside
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
0.17
p-nitrophenyl alpha-D-glucopyranoside
-
-
0.21
p-nitrophenyl-alpha-D-glucopyranoside
-
-
0.24
p-nitrophenyl-alpha-D-glucopyranoside
-
-
0.51
p-nitrophenyl-alpha-D-glucopyranoside
Thermoanaerobium sp.
-
-
0.81
p-nitrophenyl-alpha-D-glucopyranoside
-
-
3.5
palatinose
-
33 mM sodium maleate buffer, pH 6.8
7
palatinose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
7.1
palatinose
C0JP82, C0JP83
-
11
palatinose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
12
palatinose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
18
palatinose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
27.2
palatinose
C0JP82, C0JP83
-
1
Panitol
-
-
1
panose
-
-
10.4
panose
C0JP82, C0JP83
-
15
panose
C0JP82, C0JP83
-
2.2
phenyl-alpha-D-glucopyranoside
-
-
10.2
Sucrose
-
-
27.5
Sucrose
-
wild-type sucrase-isomaltase
116
Sucrose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
144
Sucrose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
147
Sucrose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
191
Sucrose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
2
trehalose
-
mutant P273G/N342T, pH 7.2, 35C
14
trehalose
-
mutant P273G, pH 7.2, 35C
31.15
trehalose
C0JP82, C0JP83
-
33.6
trehalose
C0JP82, C0JP83
-
320
trehalose
-
wild-type enzyme, pH 7.2, 35C
22.9
Trehalulose
C0JP82, C0JP83
-
30.2
Trehalulose
C0JP82, C0JP83
-
28
methyl alpha-D-glucopyranoside
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
additional information
additional information
-
kinetics, transition state stabilization energy
-
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)
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.18
4-nitrophenyl alpha-D-glucopyranoside
-
recombinant mutant D199N, pH 7.0, 35C
0.39
4-nitrophenyl alpha-D-glucopyranoside
-
recombinant mutant E255Q, pH 7.0, 35C
3.11
4-nitrophenyl alpha-D-glucopyranoside
-
recombinant mutant H328N, pH 7.0, 35C
7.1
4-nitrophenyl alpha-D-glucopyranoside
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
8.7
4-nitrophenyl alpha-D-glucopyranoside
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
14
4-nitrophenyl alpha-D-glucopyranoside
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C; pH 7.0, 30C
17
4-nitrophenyl alpha-D-glucopyranoside
-
in 100 mM MES buffer, pH 6.5, at 37C
129
4-nitrophenyl alpha-D-glucopyranoside
-
pH 6.8, 30C
352
4-nitrophenyl alpha-D-glucopyranoside
-
recombinant mutant H103N, pH 7.0, 35C
483
4-nitrophenyl alpha-D-glucopyranoside
-
recombinant wild-type enzyme, pH 7.0, 35C
697
4-nitrophenyl alpha-D-glucopyranoside
-
-
15
isomaltose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
30.8
isomaltose
C0JP82, C0JP83
-
33.3
isomaltose
-
pH 6.8, 30C
36.3
isomaltose
C0JP82, C0JP83
-
41
isomaltose
-
-
97
isomaltose
-
in 100 mM MES buffer, pH 6.5, at 37C
97
isomaltose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
101
isomaltose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
103
isomaltose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
12
isomaltotriose
C0JP82, C0JP83
-
12.5
isomaltotriose
C0JP82, C0JP83
-
15
isomaltriose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
18
isomaltriose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
21
isomaltriose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
137
maltose
-
in 100 mM MES buffer, pH 6.5, at 37C
14
methyl alpha-D-glucopyranoside
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
84
methyl alpha-D-glucopyranoside
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
88
methyl alpha-D-glucopyranoside
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
6
palatinose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
12.4
palatinose
C0JP82, C0JP83
-
13
palatinose
C0JP82, C0JP83
-
56
palatinose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
78
palatinose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
104
palatinose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
28.7
panose
C0JP82, C0JP83
-
30
panose
C0JP82, C0JP83
-
3.8
Sucrose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
25
Sucrose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
51
Sucrose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
55
Sucrose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
5.8
trehalose
C0JP82, C0JP83
-
7.3
trehalose
C0JP82, C0JP83
-
35.4
Trehalulose
C0JP82, C0JP83
-
38.7
Trehalulose
C0JP82, C0JP83
-
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 37C
1313
15
4-nitrophenyl alpha-D-glucopyranoside
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
1313
16
4-nitrophenyl alpha-D-glucopyranoside
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
1313
20
4-nitrophenyl alpha-D-glucopyranoside
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
1313
28
4-nitrophenyl alpha-D-glucopyranoside
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
1313
0.41
isomaltose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
449
5.6
isomaltose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
449
5.7
isomaltose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
449
8
isomaltose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
449
9
isomaltose
-
in 100 mM MES buffer, pH 6.5, at 37C
449
0.16
isomaltriose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
123813
0.21
isomaltriose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
123813
0.22
isomaltriose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
123813
19
maltose
-
in 100 mM MES buffer, pH 6.5, at 37C
86
0.9
methyl alpha-D-glucopyranoside
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
7494
3.1
methyl alpha-D-glucopyranoside
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C; pH 7.0, 30C
7494
0.8
palatinose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
4277
4.3
palatinose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
4277
5
palatinose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
4277
9.4
palatinose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
4277
0.02
Sucrose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
55
0.22
Sucrose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
55
0.35
Sucrose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
55
0.38
Sucrose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
55
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00027
(-)-1-azafagomine
-
pH 6.8, 25C
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
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C; pH 7.0, 30C
9.8
4-nitrophenyl alpha-D-glucopyranoside
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
12
4-nitrophenyl alpha-D-glucopyranoside
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
0.014
acarbose
-
-
0.014
acarbose
-
N-terminal cataklytic domain, pH and temperature not specified in the publication
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
0.000103
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
0.0058
isofagomine
-
pH 6.8, 25C
188
isomaltose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
246
isomaltose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C; pH 7.0, 30C
248
isomaltose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
0.0006
kotalanol
-
-
0.0006
kotalanol
-
N-terminal cataklytic domain, pH and temperature not specified in the publication
574
methyl alpha-D-glucopyranoside
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C; pH 7.0, 30C
600
methyl alpha-D-glucopyranoside
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
686
palatinose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C; pH 7.0, 30C
690
palatinose
P0CW40, P40884, P53051, Q08295
pH 7.0, 30C
0.000277
salacinol
-
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
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)
-
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
-
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
-
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
-
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
-
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
-
pH 6.8, 37C
0.0018
(2S,3S,4S,5S)-2-(hydroxymethyl)-5-[4-(4-methoxyphenyl)butyl]pyrrolidine-3,4-diol
-
pH 6.8, 37C
0.00022
(2S,3S,4S,5S)-2-[4-(3,5-difluorophenyl)butyl]-5-(hydroxymethyl)pyrrolidine-3,4-diol
-
pH 6.8, 37C
1
1,4-anhydro-4-thio-D-arabinitol
-
-
0.0057
1,4-dideoxy-1,4-((S)-[(2S,3S)-2,4-dihydroxy-3-(sulfooxy)butyl]episulfoniumylidene)-D-arabinitol
-
-
0.64
1,4-dideoxy-1,4-((S)-[(2S,3S)-2,4-dihydroxy-3-butyl]episulfoniumylidene)-D-arabinitol
-
-
0.07
1,4-dideoxy-1,4-(hydroxyethyliminiumyl)-D-arabinitol
-
-
0.0058
1,4-dideoxy-1,4-imino-D-arabinitol
-
-
0.00008
1,4-dideoxy-1,4-imino-L-arabinitol
-
-
0.73
1,4-imino-1,2,4-trideoxy-D-arabinitol
-
-
0.15
2,5-dideoxy-2,5-imino-D-glucitol
-
-
0.09
2,5-dideoxy-2,5-imino-D-mannitol
-
-
0.00005
2,5-dideoxy-2,5-imino-L-mannitol
-
-
0.3
de-O-sulfonated salacinol
-
pH and temperature not specified in the publication
1.3
salacinol
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.3
-
mutant SIQ/P, 37C
0.4
C0JP82, C0JP83
maltulose; nigerose
0.5
C0JP82, C0JP83
turanose
0.7
C0JP82, C0JP83
nigerose
1.02
-
purified enzyme, palatinose as substrate
1.1
C0JP82, C0JP83
maltulose
1.2
P0CW40, P40884, P53051, Q08295
substrate sucrose, pH 7.0, 30C
1.6
C0JP82, C0JP83
trehalose; turanose
2
C0JP82, C0JP83
trehalose
2.12
-
purified mutant sucrase-free isomaltase, maltase activity
2.3
-
purified enzyme, isomaltose as substrate
2.6
-
mutant SIQ/P, 20C
2.8
-
wild-type enzyme, 20C
3.1
-
wild-type enzyme, 37C
3.2
C0JP82, C0JP83
palatinose
3.9
P0CW40, P40884, P53051, Q08295
substrate 4-nitrophenyl alpha-D-glucopyranoside, pH 7.0, 30C
4.1
C0JP82, C0JP83
palatinose
4.5
-
with isomaltose as substrate
5
P0CW40, P40884, P53051, Q08295
substrate palatinose, pH 7.0, 30C
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
P0CW40, P40884, P53051, Q08295
substrate 4-nitrophenyl alpha-D-glucopyranoside, pH 7.0, 30C
6.07
-
purified recombinant enzyme
7
C0JP82, C0JP83
isomaltotriose
7.2
P0CW40, P40884, P53051, Q08295
substrate isomaltose, pH 7.0, 30C
7.6
P0CW40, P40884, P53051, Q08295
substrate isomaltriose, pH 7.0, 30C
7.7
P0CW40, P40884, P53051, Q08295
substrate 4-nitrophenyl alpha-D-glucopyranoside, pH 7.0, 30C
7.79
-
purified wild-type sucrase-isomaltase, sucrase activity
7.9
P0CW40, P40884, P53051, Q08295
substrate isomaltriose, pH 7.0, 30C
8.08
-
purified wild-type sucrase-isomaltase, isomaltase activity
8.6
C0JP82, C0JP83
isomaltotriose
8.6
P0CW40, P40884, P53051, Q08295
substrate isomaltriose, pH 7.0, 30C
8.74
-
purified recombinant enzyme + coexpressed GroES
9.46
-
purified recombinant enzyme + coexpressed GroES and GroEL
9.48
-
purified recombinant enzyme + coexpressed GroEL
10
C0JP82, C0JP83
trehalulose
10
P0CW40, P40884, P53051, Q08295
substrate 4-nitrophenyl alpha-D-glucopyranoside, pH 7.0, 30C
10.2
P0CW40, P40884, P53051, Q08295
substrate sucrose, pH 7.0, 30C
11
P0CW40, P40884, P53051, Q08295
substrate methyl alpha-D-glucopyranoside, pH 7.0, 30C
11.7
C0JP82, C0JP83
trehalulose
12.3
-
purified mutant sucrase-free isomaltase, isomaltase activity
14.1
C0JP82, C0JP83
isomaltose
14.5
-
purified wild-type sucrase-isomaltase, maltase activity
18.6
P0CW40, P40884, P53051, Q08295
substrate sucrose, pH 7.0, 30C
19.3
C0JP82, C0JP83
panose
19.7
P0CW40, P40884, P53051, Q08295
substrate sucrose, pH 7.0, 30C
20.4
C0JP82, C0JP83
isomaltose
23
C0JP82, C0JP83
panose
34.2
-
purified enzyme, isomaltose as substrate
39
P0CW40, P40884, P53051, Q08295
substrate palatinose, pH 7.0, 30C
52
P0CW40, P40884, P53051, Q08295
substrate methyl alpha-D-glucopyranoside, pH 7.0, 30C; substrate palatinose, pH 7.0, 30C
54
P0CW40, P40884, P53051, Q08295
substrate isomaltose, pH 7.0, 30C
55
P0CW40, P40884, P53051, Q08295
substrate methyl alpha-D-glucopyranoside, pH 7.0, 30C
60
P0CW40, P40884, P53051, Q08295
substrate isomaltose, pH 7.0, 30C
65
P0CW40, P40884, P53051, Q08295
substrate isomaltose, pH 7.0, 30C
74
P0CW40, P40884, P53051, Q08295
substrate palatinose, pH 7.0, 30C
218
-
1120fold purified enzyme
313
-
purified enzyme after expression in Escherichia coli, p-nitrophenyl-alpha-D-glucopyranoside as substrate
additional information
-
-
additional information
-
catalytic efficiency with different substrates, substrate specificity
additional information
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
C0JP82, C0JP83
;
5.9
Bacillus thermoamyloliquefaciens KP1071
-
-
6 - 6.5
-
at 45C, isomaltose as substrate
7
-
p-nitrophenyl-alpha-D-glucopyranoside as substrate
7
-
assay at
7
P53051
assay at
7
P0CW40, P40884, P53051, Q08295
-
7.2
-
assay at
7.6
P0CW40, P40884, P53051, Q08295
-
8
P0CW40, P40884, P53051, Q08295
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.1 - 10.2
-
half-optima at pH 4.8 and 7.3
4.3 - 9.8
Bacillus thermoamyloliquefaciens KP1071
-
half-optima at pH 4.9 and 7.6
4.9 - 9.5
-
half-optima at pH 5.5 and 8.2
5.6 - 7
Thermoanaerobium sp.
-
-
5.7 - 8
-
half-optima at pH 5.75 and 8.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
C0JP82, C0JP83
-
30
P53051
assay at
35
-
assay at
35
-
assay at
36
P0CW40, P40884, P53051, Q08295
-
37
C0JP82, C0JP83
-
43
P0CW40, P40884, P53051, Q08295
-
46
P0CW40, P40884, P53051, Q08295
-
74
Bacillus thermoamyloliquefaciens KP1071
-
half-optima at 58C and 75C
additional information
-
mutant SIQ/P is temperature-sensitive with a permissive temperature for catalysis of 20C, at 37C intracellular degradation of the mutant protein occurs
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
27 - 53
-
half-optima at 27C and 53C, no activity at 60C
47 - 75
-
half-optima at 47C and 75C, no activity at 78C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.9
Q4J9M3
calculated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
expression is repressed shortly after birth
Manually annotated by BRENDA team
-
apical region of normal crypt cells, polyp
Manually annotated by BRENDA team
Q4J9M3
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
Manually annotated by BRENDA team
-
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
-
Manually annotated by BRENDA team
Q4J9M3
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
Manually annotated by BRENDA team
-
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
-
Manually annotated by BRENDA team
Necturus sp.
-
airway
Manually annotated by BRENDA team
Necturus sp.
-
-
Manually annotated by BRENDA team
Necturus sp.
-
-
Manually annotated by BRENDA team
-
expression of the sucrase-isomaltase gene is induced in cells transitioning from the crypt to the villus of jejunum
Manually annotated by BRENDA team
-
jejunal sucrase-isomaltase gene is induced during postnatal development
Manually annotated by BRENDA team
Rattus norvegicus Sprague-Dawley
-
jejunal sucrase-isomaltase gene is induced during postnatal development
-
Manually annotated by BRENDA team
-
germinated
Manually annotated by BRENDA team
-
proximal jejunum and distal ileum
Manually annotated by BRENDA team
Necturus sp.
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
brush-border membrane
Manually annotated by BRENDA team
-
brush-border membrane
Manually annotated by BRENDA team
-
of the small intestinal absorptive cells of the villus and the crypts
Manually annotated by BRENDA team
-
the enzyme is anchored to brush border epithelial cells
Manually annotated by BRENDA team
Geobacillus thermoglucosidasius KP 1006
-
-
-
-
Manually annotated by BRENDA team
Necturus sp.
-
-
Manually annotated by BRENDA team
-
intestinal brush border membrane protein
Manually annotated by BRENDA team
-
microvillus membrane
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30000 - 33000
Thermoanaerobium sp.
-
SDS-PAGE, gel filtration
326242
60000 - 62000
-
SDS-PAGE
326244
60000 - 62000
-
-
326244
60000 - 62000
Bacillus thermoamyloliquefaciens KP1071
-
gel filtration; SDS-PAGE
326244
60000 - 62000
-
-
326244
60000 - 62000
-
SDS-PAGE
326251
60000 - 62000
-
SDS-PAGE
326261
63000
-
Sepharyl S-200 gel filtration
326261
68000
Q9AF93
gel filtration
654304
68220
C0JP82, C0JP83
calculated
690556
68320
C0JP82, C0JP83
calculated
690556
68500
-
gel filtration
393312
70000
C0JP82, C0JP83
SDS-PAGE; SDS-PAGE
690556
100000
-
SDS-PAGE
704667
102000
-
SDS-PAGE
326243
130000
-
SDS-PAGE
136520
140000 - 150000
-
SDS-PAGE, intact pancreatic duct, 2 polypeptide chains, 140000 + 150000
136508
148000
-
isomaltase in adult jejunum, SDS-PAGE
136513
150000
-
isomaltase in ileum, SDS-PAGE
136508
150000
-
isomaltase in adult colon, SDS-PAGE
136513
200000
Necturus sp.
-
-
655668
245000
-
SDS-PAGE
326249
260000
-
SDS-PAGE, pancreas disconnected from duodenum, single polypeptide chain
136508
914000
Q4J9M3
gel filtration
725283
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
Geobacillus thermoglucosidasius KP1006
-
x * 66000
-
dimer
-
1 * 106000, isomaltase subunit of the wild-type enzyme, + 1 * 115000, sucrase subunit of the wild-type enzyme, SDS-PAGE
dodecamer
Q4J9M3
12 * 72000, SDS-PAGE, 12 * 73000, calculated from sequence
dodecamer
-
12 * 72000, SDS-PAGE, 12 * 73000, calculated from sequence
-
monomer
-
1 * 245000, SDS-PAGE
monomer
-
1 * 103000, mutant sucrase-free isomaltase, SDS-PAGE
monomer
Q9AF93
1 * 71000, SDS-PAGE, 1 * 72138, recombinant fusion protein, amino acid sequence calculation
additional information
-
amino acid sequence and tertiary structure analysis
additional information
Q9F4G4
amino acid sequence and tertiary structure analysis
additional information
P53051
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
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
Geobacillus thermoglucosidasius KP 1006
-
-
-
glycoprotein
-
-
proteolytic modification
-
pro-sucrase-isomaltase precursor, complex glycosylated sucrase-isomaltase precursor, high-mannose sucrase-isomaltase precursor
glycoprotein
-
-
proteolytic modification
-
-
glycoprotein
-
enzyme, especially the mutant enzyme, contains probably carbohydrates with terminal L-fucose, determined by lectin affinity, overview
proteolytic modification
-
extracellular proteolysis of single-chain pro-sucrase-isomaltase
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, 25C
-
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
P53051
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.5 - 11.3
-
50% inactivation at pH 3.5 and 11.3 after incubation at 34C for 15 h
326244
4.3 - 10.7
Bacillus thermoamyloliquefaciens KP1071
-
50% inactivation at pH 4.3 and 10.7 after incubation at 34C for 15 h
326244
5 - 9.1
-
50% inactivation at pH 5.0 and 9.1 after incubation at 34C for 15 h
326244, 326246
5.3 - 7.8
-
stable at 37C for 1 h
326249
5.7 - 9
-
stable at 25C for 15 h
326251
6 - 9
-
at 50C, 10 min incubation
326261
6.5 - 7.3
-
50% inactivation at pH 6.5 and 7.3 after incubation at 34C for 15 h
326244, 326246
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 60
Bacillus thermoamyloliquefaciens KP1071
-
stable activity for 10 min at pH 6.8, 50% inactivation after 10 min at 70C
326244
13 - 55
-
heating for 10 min in 33.3 mM phosphate buffer, pH 6.8: no loss of activity from 13 to 40C, 87% of activity at 45C, 56% at 48C, 25% at 50C, no activity at 55C
326251
25 - 55
Bacillus thermoamyloliquefaciens KP1071
-
stable for 15 h at pH 5.5-10.3 at 25C, at pH 6.4-10.1 at 34C, at pH 6.8-8.4 at 55C, no activity after 15 h at pH 2.8 and 11.4 at 25C, at pH 3.1 and 11.1 at 34C, at pH 3.8 and 9.9 at 55C
326244
29.9
P0CW40, P40884, P53051, Q08295
melting temperature, pH 8
729747
30 - 85
-
stable from 30 to 70C, 50% inactivation at 71C after 10 min
326241
33.2
P0CW40, P40884, P53051, Q08295
melting temperature, pH 8
729747
35.7
P0CW40, P40884, P53051, Q08295
melting temperature, pH 8
729747
36.3
P0CW40, P40884, P53051, Q08295
melting temperature, pH 7
729747
36.6
P0CW40, P40884, P53051, Q08295
melting temperature, pH 6
729747
37
P0CW40, P40884, P53051, Q08295
half-life 23.2 min; half-life 26.1 min; half-life 27.4 min; half-life 2.9 min
729747
38.8
P0CW40, P40884, P53051, Q08295
melting temperature, pH 7
729747
40
P0CW40, P40884, P53051, Q08295
half-life 0.8 min; half-life 17.6 min; half-life 18.5 min; half-life 7.6 min
729747
41.6
P0CW40, P40884, P53051, Q08295
melting temperature, pH 8
729747
46.2
P0CW40, P40884, P53051, Q08295
melting temperature, pH 7
729747
46.6
P0CW40, P40884, P53051, Q08295
melting temperature, pH 7
729747
47
P0CW40, P40884, P53051, Q08295
melting temperature, pH 6
729747
50 - 60
-
stable up to 50C, no activity at 60C
326261
53
-
stable at pH 6.8 for 10 min
326246
55.1
P0CW40, P40884, P53051, Q08295
melting temperature, pH 6
729747
55.5
P0CW40, P40884, P53051, Q08295
melting temperature, pH 6
729747
60
-
almost no loss of activity for 5 min at 60C, potassium phosphate buffer, pH 6.0
136512
70
Thermoanaerobium sp.
-
-
326242
70
Bacillus thermoamyloliquefaciens KP1071
-
50% inactivation after 10 min incubation at pH 6.8
326244
76
Thermoanaerobium sp.
-
half-life 20 min at pH 6.5
326242
95
Q4J9M3
half-life: 33.8 h
725283
100
Q4J9M3
half-life: 10.6 h
725283
105
Q4J9M3
half-life: 1.8 h
725283
additional information
-
thermostability rises with proline content
326244
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
N-terminal domain alpha/beta motifs are probably recognized by the endogenous GroEL protein, leading to binding and stabilization
-
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
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ethanol
-
-
Ethanol
-
50% inactivation after 5 h treatment with 32% ethanol at 25C and pH 6.8
Ethanol
-
50% inactivation after 5 h treatment with 49% ethanol at 25C and pH 6.8
Ethanol
Bacillus thermoamyloliquefaciens KP1071
-
50% inactivation after 5 h treatment with 41% ethanol at 25C and pH 6.8
Ethanol
-
fairly stable for 5 h at 4C in 20% ethanol , 50% inactivation after 5 h treatment with 17% ethanol at 25C and pH 6.8
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, purified enzyme, 6 months, no loss of activity
-
4C, stored for at least 6 months without any loss of activity
Q4J9M3
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes from Escherichia coli MV1184
-
-
Bacillus thermoamyloliquefaciens KP1071
-
recombinant enzyme from Escherichia coli
Q9AF93
;
C0JP82, C0JP83
after expression in Escherichia coli
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nickel-Sepharose resin column chromatography
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recombinant N-terminally His-tagged enzyme from Drosophila melanogaster S2 cells by copper affinity chromatography and ion exchange chromatography
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from gall bladder epithelium
Necturus sp.
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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
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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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Thermoanaerobium sp.
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli
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expression in Escherichia coli
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overexpression of wild-type and mutant enzymes in Escherichia coli MV1184
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expression of wild-type and mutant enzymes in Escherichia coli strain W3110
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expression in Escherichia coli
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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
Q9AF93
His-tag; His-tag
C0JP82, C0JP83
expression in Escherichia coli
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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
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5'-flanking region of the gene
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expressed in Drosophila melanogaster S2 cells
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recombinant expression of N-terminally His-tagged enzyme in Drosophila melanogaster S2 cells
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transient expression of wild-type and mutant enzyme Q1098P in COS-1 cells
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DNA and amino acid sequence determination, functional expression in CHO cells and in Xenopus laevis oocytes, in vitro translation
Necturus sp.
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cloning the region including the C-terminus of isomaltase and the N-terminus of sucrase subunit
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genes IMA1 to IMA5, DNA and aminmo acid sequence determination and analysis, transcriptional patterns, overexpression of the 5 genes in Saccharomyces cerevisiae strain JF1811
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expressed in Sulfolobus acidocaldarius. Attempts to obtain soluble enzyme from Escherichia coli strains are unsuccessful
Q4J9M3
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the transcription level of malA is increased 3fold upon the addition of maltose or starch to the medium
Q4J9M3
the transcription level of malA is increased 3fold upon the addition of maltose or starch to the medium
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D199N
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site-directed mutagenesis, active site mutant, highly reduced activity compared to the wild-type enzyme
D329N
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site-directed mutagenesis, active site mutant, catalytically inactive mutant
E255Q
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site-directed mutagenesis, active site mutant, highly reduced activity compared to the wild-type enzyme
H103N
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site-directed mutagenesis, substrate binding mutant, about 50% reduced activity compared to the wild-type enzyme
H328N
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site-directed mutagenesis, substrate binding mutant, highly reduced activity compared to the wild-type enzyme
N342T
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site-directed mutagenesis, reduced activity with isomaltose, altered substrate specificity
P273G
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site-directed mutagenesis, increased activity with trehalose, reduced activity with isomaltose, altered substrate specificity
P273G/N342T
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site-directed mutagenesis, reduced activity with isomaltose, altered substrate specificity
N342T
Bacillus sp. SAM1606
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site-directed mutagenesis, reduced activity with isomaltose, altered substrate specificity
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P273G
Bacillus sp. SAM1606
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site-directed mutagenesis, increased activity with trehalose, reduced activity with isomaltose, altered substrate specificity
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P273G/N342T
Bacillus sp. SAM1606
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site-directed mutagenesis, reduced activity with isomaltose, altered substrate specificity
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Q1098P
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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 20C instead of 37C due to evolved temperature-sensitivity of the mutant
R91T
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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
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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
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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
L240P
P0CW40, P40884, P53051, Q08295
similar to wild-type
D1193N
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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
additional information
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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 20C instead of 37C due to evolved temperature-sensitivity of the mutant
R279Q
P0CW40, P40884, P53051, Q08295
displays substrate specificities and specific activities close to those of isoform Ima2
additional information
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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
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
thermally inactivated enzyme is revived by GroEL
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functional reconstitution of the purified enzyme in a lipid bilayer
Necturus sp.
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
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possibility for use as molecular marker in diagnosis of colon adenocarcinoma
medicine
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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
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the enzyme can serve as therapeutic target for the treatment of digestive disorders or their sequelae
medicine
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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
nutrition
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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