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Information on EC 3.2.1.10 - oligo-1,6-glucosidase and Organism(s) Homo sapiens

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IUBMB 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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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
disaccharidase, oligo-1,6-glucosidase, sucrase-isomaltase complex, limit-dextrinase, intestinal sucrase/isomaltase, sea lion isomaltase, amy112, exo-oligo-1,6-glucosidase, oligo-1,4-1,6-alpha-glucosidase, alpha-glucosidase 2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomaltase
oligo-1,6-glucosidase
Oligosaccharide alpha-1,6-glucosidase
-
-
-
-
sucrase
-
-
sucrase isomaltase
-
-
sucrase-isomaltase
sucrase-isomaltase complex
-
-
additional information
the enzyme belongs to the family 31 of glycoside hydrolases
REACTION
REACTION DIAGRAM
COMMENTARY hide
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
show the reaction diagram
enzyme from intestinal mucosa also catalyzes the reaction of sucrase alpha-glucosidase, EC 3.2.1.48
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
PATHWAY SOURCE
PATHWAYS
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9032-15-9
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
show the reaction diagram
-
-
-
?
alpha-limit dextrin + H2O
?
show the reaction diagram
-
-
-
-
?
isomaltosaccharides + H2O
D-glucose
show the reaction diagram
-
n = 2, isomaltose
-
?
isomaltose + H2O
2 D-glucose
show the reaction diagram
maltodextrin + H2O
?
show the reaction diagram
-
corn maltodextrin
-
-
?
maltopentose + H2O
?
show the reaction diagram
-
-
-
-
?
maltose + H2O
2 D-glucose
show the reaction diagram
maltose + H2O
D-glucose + D-glucose
show the reaction diagram
-
-
-
-
?
maltotetraose + H2O
?
show the reaction diagram
-
-
-
-
?
maltotriose + H2O
?
show the reaction diagram
-
-
-
-
?
oligosaccharide + H2O
monosaccharide
show the reaction diagram
-
role in absorption of sucrose, isomaltose, maltose
-
?
palatinose + H2O
D-glucose + fructose
show the reaction diagram
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
isomaltose + H2O
2 D-glucose
show the reaction diagram
-
-
-
?
oligosaccharide + H2O
monosaccharide
show the reaction diagram
-
role in absorption of sucrose, isomaltose, maltose
-
?
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
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(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
-
-
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
blintol
selenium analogue of salacinol
D-glucose
de-O-sulfonated kotalanol
de-O-sulfonated ponkoranol
-
-
de-O-sulfonated salacinol
-
-
diethanolamine
-
about 80% inhibition of isomaltase activity by 50 mM
hepatocyte nuclear factor-1alpha
-
gene expression of HNF-1alpha exhibits a positive correlation with that of sucrase-isomaltase regulated by glucose
-
kotalanol
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
-
salacinol
triethanolamine
-
about 80% inhibition of isomaltase activity by 50 mM
Tris
-
complete inhibition of isomaltase activity by 50 mM
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 hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.3
4-nitrophenyl alpha-D-glucopyranoside
in 100 mM MES buffer, pH 6.5, at 37°C
8.9 - 11.1
isomaltose
3.6
maltopentose
-
IP-SI, immunoprecipitated human sucrase-isomaltase complex
6.83 - 7.1
maltose
3.79
maltotetrose
-
IP-SI, immunoprecipitated human sucrase-isomaltase complex
5.55
maltotriose
-
IP-SI, immunoprecipitated human sucrase-isomaltase complex
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
17
4-nitrophenyl alpha-D-glucopyranoside
in 100 mM MES buffer, pH 6.5, at 37°C
97
isomaltose
in 100 mM MES buffer, pH 6.5, at 37°C
137
maltose
in 100 mM MES buffer, pH 6.5, at 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13
4-nitrophenyl alpha-D-glucopyranoside
in 100 mM MES buffer, pH 6.5, at 37°C
9
isomaltose
in 100 mM MES buffer, pH 6.5, at 37°C
19
maltose
in 100 mM MES buffer, pH 6.5, at 37°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000007 - 0.000035
3'-O-methylponkoranol
0.014
acarbose
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 - 0.000302
de-O-sulfonated ponkoranol
0.0006
kotalanol
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
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 hide
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
0.3
de-O-sulfonated salacinol
Homo sapiens
-
pH and temperature not specified in the publication
1.3
salacinol
Homo sapiens
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.3
-
mutant SIQ/P, 37°C
2.3
-
purified enzyme, isomaltose as substrate
2.6
-
mutant SIQ/P, 20°C
2.8
-
wild-type enzyme, 20°C
3.1
-
wild-type enzyme, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
primary and metastatic
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
sucrase-isomaltase (SI) catalyzes the final step of carbohydrate digestion by breaking disaccharides and oligosaccharides to absorbable monosaccharides
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
enzyme structure-function analysis, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SUIS_HUMAN
1827
1
209453
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100000
SDS-PAGE
130000
-
SDS-PAGE
148000
-
isomaltase in adult jejunum, SDS-PAGE
150000
-
isomaltase in adult colon, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
-
proteolytic modification
-
pro-sucrase-isomaltase precursor, complex glycosylated sucrase-isomaltase precursor, high-mannose sucrase-isomaltase precursor
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
additional information
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
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
nickel-Sepharose resin column chromatography
recombinant N-terminally His-tagged enzyme from Drosophila melanogaster S2 cells by copper affinity chromatography and ion exchange chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
5'-flanking region of the gene
-
expressed in Drosophila melanogaster S2 cells
gene SI, sequence comparisons, recominant expression of wild-type and mutant enzymes in COS-1 cells
recombinant expression of N-terminally His-tagged enzyme in Drosophila melanogaster S2 cells
transient expression of wild-type and mutant enzyme Q1098P in COS-1 cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Asp, N.G.; Dahlqvist, A.
Separation of human small-intestinal sucrase from isomaltase
FEBS Lett.
35
303-305
1973
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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, Macaca mulatta, Mus musculus, Pan troglodytes, Suncus murinus (O62653), Oryctolagus cuniculus (P07768), Homo sapiens (P14410), Rattus norvegicus (P23739)
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team