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Information on EC 3.2.1.48 - sucrose alpha-glucosidase and Organism(s) Mus musculus and UniProt Accession B5THE3

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IUBMB Comments
This enzyme is isolated from intestinal mucosa as a single polypeptide chain that also displays activity towards isomaltose (EC 3.2.1.10 oligo-1,6-glucosidase).
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This record set is specific for:
Mus musculus
UNIPROT: B5THE3
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The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
hide
isomaltose
+
h2O
=
2
D-glucose
+
=
2
Synonyms
sucrase-isomaltase, isomaltase, intestinal sucrase, sucrase isomaltase, sucrose hydrolase, sucrase/isomaltase, sucrase-isomaltase enzyme complex, sucrose alpha-glucosidase, sucrose alpha-glucohydrolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
sucrase-isomaltase
-
glucosidase, sucrose alpha-
-
-
-
-
intestinal sucrase
-
-
-
-
sucrase
-
-
-
-
sucrase isomaltase
-
-
sucrase-invertase
-
-
-
-
sucrase-isomaltase
sucrose alpha-glucohydrolase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of O-glycosyl bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
sucrose-alpha-D-glucohydrolase
This enzyme is isolated from intestinal mucosa as a single polypeptide chain that also displays activity towards isomaltose (EC 3.2.1.10 oligo-1,6-glucosidase).
CAS REGISTRY NUMBER
COMMENTARY hide
37288-39-4
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
maltose + H2O
alpha-D-glucose + D-glucose
show the reaction diagram
-
-
-
?
isomaltose + H2O
2 D-glucose
show the reaction diagram
-
-
-
-
?
maltose + H2O
2 glucose
show the reaction diagram
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
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
maltose + H2O
2 glucose
show the reaction diagram
-
-
-
?
sucrose + H2O
alpha-D-glucose + D-fructose
show the reaction diagram
-
-
-
-
?
sucrose + H2O
D-glucose + D-fructose
show the reaction diagram
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(+)-catechin
noncompetitive
(-)-epigallocatechin gallate
noncompetitive
caffeic acid
noncompetitive
chlorogenic acid
noncompetitive
gallic acid
noncompetitive
gallic acid
-
inhibition of brush border sucrase by polyphenols in mouse intestine. Inhibition by gallic acid is a pure V effect at pH 5.0, which changes to mixed type at pH 7.2, and pure K effect at pH 8.5
Tannic acid
-
inhibition of brush border sucrase by polyphenols in mouse intestine. Sucrase inhibition by tannic acid is a pure K effect at acidic pH and uncompetitive type in the alkaline pH range
additional information
-
inhibition of mice sucrase by polyphenols is pH-dependent, and is associated with conformational modifications of the enzyme. At pH 4.8, the polyphenols inhibit sucrase activity by 85-96%, which is reduced to 51 and 64%, respectively, at pH 7.2. However, at pH 8.5, 60 and 76% inhibition of enzyme activity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20.2 - 138
sucrose
additional information
additional information
-
Km values in presence of inhibitors, at pH 7.2, both gallic acid and tannic acid show mixed-type enzyme inhibition, Km is enhanced by 77-114% and Vmax by 55-60%, overview
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
17.5
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
the fully glycosylated mature form of sucrase isomaltase is decreased in core2 1,6-N-acetylglucosaminyltransferase-2 knock-out mice but not in core2 N-acetylglucosaminyltransferase-3 nulls. Expression of sucrase isomaltase and dipeptidyl peptidase-IV is dramatically reduced in core2 1,6-N-acetylglucosaminyltransferase-1-3 triple knock-out mice. Goblet cells in the upper part of the crypt show impaired maturation in the core2 O-glycan-deficient mice
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
B5THE3_MOUSE
1818
1
209100
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
210000
-
x * 210000, about
220000
-
-
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 210000, about
dimer
-
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
pH 5.9, inactivation, soluble enzyme activity is stable to heat treatment, membrane associated enzyme was heat-labile under these conditions
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from brush border 155fold by isolation from the microvillus membranes by papain, gel filtration and anion exchange chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Drosophila S2 cells
recombinant expression in a baculovirus-Sf9 insect cell system
mouse SI mRNA synthesized from mouse SI cDNA, pMSI-A1 cloned into pBluescript KS, cDNA cloned from mouse intestinal RNA with anchored polymerase chain reaction method
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Quezada-Calvillo, R.; Markowitz, A.J.; Traber, P.G.; Underdown, B.J.
Murine intestinal disaccharidases: identification of structural variants of sucrase-isomaltose complex
Am. J. Physiol.
265
1142-1149
1993
Mus musculus
-
Manually annotated by BRENDA team
Honma, K.; Mochizuki, K.; Goda, T.
Carbohydrate/fat ratio in the diet alters histone acetylation on the sucrase-isomaltase gene and its expression in mouse small intestine
Biochem. Biophys. Res. Commun.
357
1124-1129
2007
Mus musculus
Manually annotated by BRENDA team
Gupta, S.; Mahmood, S.; Khan, R.H.; Mahmood, A.
Inhibition of brush border sucrase by polyphenols in mouse intestine
Biosci. Rep.
30
111-117
2010
Mus musculus
Manually annotated by BRENDA team
Lee, S.H.; Yu, S.Y.; Nakayama, J.; Khoo, K.H.; Stone, E.L.; Fukuda, M.N.; Marth, J.D.; Fukuda, M.
Core2 O-glycan structure is essential for the cell surface expression of sucrase isomaltase and dipeptidyl peptidase-IV during intestinal cell differentiation
J. Biol. Chem.
285
37683-37692
2010
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Simsek, M.; Quezada-Calvillo, R.; Ferruzzi, M.G.; Nichols, B.L.; Hamaker, B.R.
Dietary phenolic compounds selectively inhibit the individual subunits of maltase-glucoamylase and sucrase-isomaltase with the potential of modulating glucose release
J. Agric. Food Chem.
63
3873-3879
2015
Mus musculus (B5THE3), Mus musculus, Homo sapiens (P14410), Homo sapiens
Manually annotated by BRENDA team