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Information on EC 3.2.1.48 - sucrose alpha-glucosidase
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EC Tree
3.2.1.48 sucrose alpha-glucosidaseIUBMB 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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Word Map
- 3.2.1.48
- border
-
brush
- lactase
- enterocytes
- disaccharidase
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caco-2
- mucosal
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crypt
- jejunal
- starch
- maltase-glucoamylase
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brush-border
- glucoamylase
- maltose
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lactase-phlorizin
- ileum
- trehalase
- microvillus
- acarbose
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basolateral
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postprandial
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dipeptidyl
- villin
-
suckling
-
dipeptidylpeptidase
- malabsorption
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goblet
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3.2.1.20
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enterocyte-like
- isomaltose
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3.4.11.2
-
intestine-specific
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carbohydrase
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small-intestinal
- aminopeptidase-n
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postconfluent
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crypt-villus
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paneth
- 1-deoxynojirimycin
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bloating
- dextrin
- agriculture
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
sucrase-isomaltase, isomaltase, intestinal sucrase, sucrase isomaltase, sucrose hydrolase, sucrase/isomaltase, sucrase-isomaltase enzyme complex, sucrose alpha-glucosidase, sucrose alpha-glucohydrolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glucosidase, sucrose alpha-
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intestinal sucrase
sucrase
sucrase isomaltase
sucrase-invertase
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sucrase-isomaltase
sucrose alpha-glucohydrolase
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sucrose hydrolase
additional information
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the enzyme belongs to the subfamily 4 of the glycoside hydrolase family 13, GH-13
intestinal sucrase
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sucrase
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sucrase-isomaltase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
isomaltose + h2O = 2 D-glucose
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isomaltose + h2O = 2 D-glucose
The enzyme complex consists of two noncovalently linked subunits. The active site of the sucrase subunit cleaves alpha,beta-(1-2)glycosidic bonds and contains only two subsites and, thus can bind only two monomeric parts of a substrate with positive affinity. The isomaltase cleaves alpha-(1-6) and alpha-(1-1) glycoside bonds
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isomaltose + h2O = 2 D-glucose
the protein with strong homology to a rabbit sucrase-isomaltase is a cAMP-dependent epithelial chloride channel
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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PATHWAY SOURCE
PATHWAYS
BRENDA
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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).
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CAS REGISTRY NUMBER
COMMENTARY
37288-39-4
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1,6-di-O-alpha-D-glucopyranosyl-D-fructofuranose + H2O
alpha-D-glucose + D-fructose
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99% cleavage compared to 1,6-di-O-alpha-D-glucopyranosyl-D-fructofuranose
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-
?
1-O-alpha-D-glucopyranosyl-D-glucitol + H2O
alpha-D-glucose + D-glucitol
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68% cleavage compared to 1-O-alpha-D-glucopyranosyl-D-glucitol
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-
?
1-O-alpha-D-glucopyranosyl-D-mannitol + H2O
alpha-D-glucose + D-mannitol
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25% cleavage compared to 1-O-alpha-D-glucopyranosyl-D-mannitol
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?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
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?
4-nitrophenyl-alpha-D-glucoside + H2O
4-nitrophenol + alpha-D-glucose
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?
6-bromo-2-naphthyl-alpha-D-glucoside + H2O
6-bromonaphthol + alpha-D-glucose
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?
6-O-alpha-D-glucopyranosyl-D-glucitol + H2O
alpha-D-glucose + D-glucitol
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35% cleavage compared to 6-O-alpha-D-glucopyranosyl-D-glucitol
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?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-fructofuranose + H2O
alpha-D-glucose + D-fructose
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97% cleavage compared to alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-fructofuranose
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?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-fructopyranose + H2O
alpha-D-glucose + D-fructose
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92% cleavage compared to alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-fructopyranose
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?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-glucopyranose + H2O
alpha-D-glucose
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?
alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-glucopyranosyl-(1-6)-D-fructofuranose + H2O
alpha-D-glucose + D-fructose
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100% cleavage compared to alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-D-glucopyranosyl-(1-6)-D-fructofuranose
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?
alpha-D-glucopyranosyl-(1-6)-beta-fructofuranosyl-alpha-D-glucopyranoside + H2O
alpha-D-glucose + beta-D-fructose
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29% cleavage compared to alpha-D-glucopyranosyl-(1-6)-beta-fructofuranosyl-alpha-D-glucopyranoside
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?
maltose + H2O
?
comparable catalytic efficiencies for panose and maltose
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?
maltose + L-ascorbic acid
L-ascorbic acid alpha-D-glucoside
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enzyme form L-ascorbic acid alpha-glucoside by splitting maltose among the disaccharides
r
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + alpha-D-glucopyranose
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?
panose + H2O
?
comparable catalytic efficiencies for panose and maltose
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?
sucrose + glucan
?
SUH active site structure analysis, overview
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?
p-nitrophenyl-alpha-glucoside + H2O
p-nitrophenol + D-glucose
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?
sucrose + H2O
alpha-D-glucose + D-fructose
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the enzyme is involved in osmoregulation in the gut and hemolymph of pea aphids in response to the diet, analysis of honeydew sugar composition
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?
sucrose + H2O
alpha-D-glucose + D-fructose
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the absolute enzyme exhibits a flat negative trough, indicating the presence of alpha-helices and beta-sheet structures in the enzyme
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?
sucrose + H2O
alpha-D-glucose + D-fructose
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substrate binding site and structure, overview
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?
additional information
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enzyme mutation can cause the congenital sucrase-isomaltase deficiency phenotype II, overview
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?
additional information
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rhesus monkey rotavirus impairs expression and activity of the brush border-associated enzyme in Caco-2 cells, the inhibition is not due to virus-induced, Ca2+-dependent disassembly of the F-actin cytoskeleton, but to a mechanism involving cAMP protein kinase A, PKA, EC 2.7.11.11, signalling and hyperphosphorylation of cytokeratin 18, the effect is antagonized by PKA blockers, e.g. H-89
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?
additional information
?
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the enzyme expression is transactivated by transcription factors hepatocyte nuclear factors 1alpha and 1beta, HNF-1alpha and HNF-1beta, molecular mechanism and responsible amino acids of HNFs, overview
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?
additional information
?
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the enzyme expression is transactivated by transcription factors hepatocyte nuclear factors 1alpha and 1beta, HNF-1alpha and HNF-1beta, molecular mechanism and responsible amino acids of HNFs, overview
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?
additional information
?
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hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products
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?
additional information
?
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hydrolyze the mixture of linear alpha-1,4- and branched alpha-1,6-oligosaccharide substrates that typically make up terminal starch digestion products
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?
additional information
?
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human maltase-glucoamylase and sucrase-isomaltase are composed of duplicated catalytic domains, N- and C-terminal, which display overlapping substrate specificities. The N-terminal catalytic domain of human MGAM has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides
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?
additional information
?
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human maltase-glucoamylase and sucrase-isomaltase are composed of duplicated catalytic domains, N- and C-terminal, which display overlapping substrate specificities. The N-terminal catalytic domain of human MGAM has a preference for short linear alpha-1,4-oligosaccharides, whereas N-terminal SI has a broader specificity for both alpha-1,4- and alpha-1,6-oligosaccharides
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?
additional information
?
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the enzyme performs hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action (EC 3.2.1.48), and hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose (EC 3.2.1.10), reaction mechanism
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?
additional information
?
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the enzyme performs hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action (EC 3.2.1.48), and hydrolysis of (1->6)-alpha-D-glucosidic linkages in some oligosaccharides produced from starch and glycogen by alpha-amylase, and in isomaltose (EC 3.2.1.10), reaction mechanism
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?
additional information
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pullulan is likely degraded extracellularly by an amylopullulanase and further hydrolyzed by the PF0132 protein after intracellular transport
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?
additional information
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pullulan is likely degraded extracellularly by an amylopullulanase and further hydrolyzed by the PF0132 protein after intracellular transport
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?
additional information
?
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Additional substrates are mixtures of isomers containing mannitol and glucitol, e.g. alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-1)-D-mannitol and alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-1)-D-glucitol in a ratio 2:3, alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-alpha-D-gluco-pyranosyl-(1-1)-D-mannitol and alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-6)-alpha-D-gluco-pyranosyl-(1-1)-D-glucitol in a ratio 2:3, 1,6-di-O-alpha-D-glucopyranosyl-D-mannitol and 1,6-di-O-alpha-D-glucopyranosyl-D-glucitol, alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-1)-D-mannitol and alpha-D-glucopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-1)-D-glucitol. The end products are glucose, mannose and glucitol in accordance with the composition of the initial substrate.
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?
additional information
?
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the enzyme activity influences the development of size and digestive capacity of the jejunum and small intestine
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?
additional information
?
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the enzyme is involved in regulating the secretion of cellobiase through co-aggregation
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?
additional information
?
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not: alpha-D-glucopyranosyl-(1-4)-D-glucopyranose, alpha-D-glucopyranosyl-(1-6)-D-glucopyranose, alpha-D-glucopyranosyl alpha-D-glucopyranoside, alpha-D-galactopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-2)-beta-D-fructofuranoside, alpha-D-galactopyranosyl-(1-6)-alpha-D-galactopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-2)-beta-D-fructofuranoside
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?
additional information
?
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not: alpha-D-glucopyranosyl-(1-4)-D-glucopyranose, alpha-D-glucopyranosyl-(1-6)-D-glucopyranose, alpha-D-glucopyranosyl alpha-D-glucopyranoside, alpha-D-galactopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-2)-beta-D-fructofuranoside, alpha-D-galactopyranosyl-(1-6)-alpha-D-galactopyranosyl-(1-6)-alpha-D-glucopyranosyl-(1-2)-beta-D-fructofuranoside
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?
additional information
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the enzyme is identified as NpAS, i.e. Neisseria polysaccharea amylosucrase, homolog, involved in regulation of the utilization of plant sucrose in phytopathogenic bacteria. But the enzyme is exclusively a hydrolase and not a glucosyltransferase and is termed sucrose hydrolase, SUH, overview
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
maltose + H2O