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Information on EC 3.2.1.10 - oligo-1,6-glucosidase and Organism(s) Rattus norvegicus and UniProt Accession P23739

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EC Tree
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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Rattus norvegicus
UNIPROT: P23739
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The taxonomic range for the selected organisms is: Rattus norvegicus
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
oligo-1,6-glucosidase
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sucrase-isomaltase
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dextrin 6-alpha-D-glucanohydrolase
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Oligosaccharide alpha-1,6-glucosidase
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-
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sucrase-isomaltase
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-
REACTION
REACTION DIAGRAM
COMMENTARY hide
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
enzyme from intestinal mucosa also catalyzes the reaction of sucrase alpha-glucosidase, EC 3.2.1.48
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
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-
-
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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
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-methylumbelliferyl beta-D-glucoside + H2O
4-methylumbelliferol + beta-D-glucose
show the reaction diagram
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-
-
-
?
isomaltosaccharides + H2O
D-glucose
show the reaction diagram
isomaltose + H2O
2 D-glucose
show the reaction diagram
maltose + H2O
2 D-glucose
show the reaction diagram
-
-
-
?
sucrose + H2O
D-fructose + D-glucose
show the reaction diagram
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-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(2S,3S,4S,5S)-2-(hydroxymethyl)-5-[3-(4-methylphenyl)propyl]pyrrolidine-3,4-diol
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(2S,3S,4S,5S)-2-(hydroxymethyl)-5-[4-(4-methoxyphenyl)butyl]pyrrolidine-3,4-diol
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(2S,3S,4S,5S)-2-[4-(3,5-difluorophenyl)butyl]-5-(hydroxymethyl)pyrrolidine-3,4-diol
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good inhibition activities against intestinal isomaltase and sucrase
1,2,3-tri-O-galloyl-beta-D-glucose
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about 20% inhibition at 1 mM
1-O-Galloyl-beta-D-glucose
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about 15% inhibition at 1 mM, 34.4% inhibition at 5 mM
1-O-methyl-2,3-di-O-galloyl-beta-D-glucose
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about 10% inhibition at 1 mM
casuarictin
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ellagtannin, from flower buds of Syzygium aromaticum, about 16% inhibition at 1 mM
eugeniin
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ellagtannin, from flower buds of Syzygium aromaticum, about 18% inhibition at 1 mM
gallic acid
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8% inhibition at 5mM
penta-O-galloyl-beta-D-glucose
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about 40% inhibition at 1-5 mM
additional information
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structure-activity relationship study of inhibitors, inhibitory effect of the inhibitors on the different enzyme activities, such as maltase, sucrase and isomaltase activity, overview, an increasing number of galloyl units in the molecule leads to an increase in inhibitory potency
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00063
(2S,3S,4S,5S)-2-(hydroxymethyl)-5-[3-(4-methylphenyl)propyl]pyrrolidine-3,4-diol
Rattus norvegicus
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pH 6.8, 37°C
0.0018
(2S,3S,4S,5S)-2-(hydroxymethyl)-5-[4-(4-methoxyphenyl)butyl]pyrrolidine-3,4-diol
Rattus norvegicus
-
pH 6.8, 37°C
0.00022
(2S,3S,4S,5S)-2-[4-(3,5-difluorophenyl)butyl]-5-(hydroxymethyl)pyrrolidine-3,4-diol
Rattus norvegicus
-
pH 6.8, 37°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GH31 module subject to phylogenetic analysis
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
SUIS_RAT
1841
1
210350
Swiss-Prot
Secretory Pathway (Reliability: 1)
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
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proteolytic modification
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification of the enzyme complex from rat intestinal acetone powder, by solubilization with Triton X-100, gel filtration, dialysis, ion exchange chromatography, and preparative PAGE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning the region including the C-terminus of isomaltase and the N-terminus of sucrase subunit
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hauri, H.P.; Quaroni, A.; Isselbacher, K.J.
Biogenesis of intestinal plasma membrane: posttranslational route and cleavage of sucrase-isomaltase
Proc. Natl. Acad. Sci. USA
76
5183-5186
1979
Rattus norvegicus
Manually annotated by BRENDA team
Broyart, J.P.; Hugot, J.P.; Perret, C.; Porteu, A.
Molecular cloning and characterization of a rat intestinal sucrase-isomaltase cDNA. Regulation of sucrase-isomaltase gene expression by sucrose feeding
Biochim. Biophys. Acta
1087
61-67
1990
Rattus norvegicus
Manually annotated by BRENDA team
Toda, M.; Kawabata, J.; Kasai, T.
Inhibitory effects of ellagi- and gallotannins on rat intestinal alpha-glucosidase complexes
Biosci. Biotechnol. Biochem.
65
542-547
2001
Rattus norvegicus
Manually annotated by BRENDA team
Suzuki, T.; Mochizuki, K.; Goda, T.
Histone H3 modifications and Cdx-2 binding to the sucrase-isomaltase (SI) gene is involved in induction of the gene in the transition from the crypt to villus in the small intestine of rats
Biochem. Biophys. Res. Commun.
369
788-793
2008
Rattus norvegicus
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)
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Manually annotated by BRENDA team
Yorita, S.; Mochizuki, K.; Goda, T.
Induction of histone acetylation on the sucrase-isomaltase gene in the postnatal rat jejunum
Biosci. Biotechnol. Biochem.
73
933-935
2009
Rattus norvegicus, Rattus norvegicus Sprague-Dawley
Manually annotated by BRENDA team
Natori, Y.; Sakuma, T.; Yoshimura, Y.; Kinami, K.; Hirokami, Y.; Sato, K.; Adachi, I.; Kato, A.; Takahata, H.
Synthesis and biological evaluation of alpha-1-C-4'-arylbutyl-L-arabinoiminofuranoses, a new class of alpha-glucosidase inhibitors
Bioorg. Med. Chem. Lett.
24
3298-3301
2014
Rattus norvegicus
Manually annotated by BRENDA team