3.2.1.48: sucrose alpha-glucosidase
This is an abbreviated version!
For detailed information about sucrose alpha-glucosidase, go to the full flat file.
Word Map on EC 3.2.1.48
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3.2.1.48
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border
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brush
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lactase
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enterocytes
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disaccharidase
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caco-2
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mucosal
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crypt
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jejunal
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starch
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maltase-glucoamylase
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brush-border
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glucoamylase
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maltose
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lactase-phlorizin
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ileum
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trehalase
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microvillus
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acarbose
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basolateral
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postprandial
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dipeptidyl
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villin
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suckling
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dipeptidylpeptidase
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malabsorption
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goblet
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3.2.1.20
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enterocyte-like
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isomaltose
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3.4.11.2
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intestine-specific
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carbohydrase
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small-intestinal
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aminopeptidase-n
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postconfluent
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crypt-villus
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paneth
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1-deoxynojirimycin
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bloating
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dextrin
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agriculture
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medicine
- 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
-
postprandial
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dipeptidyl
- villin
-
suckling
-
dipeptidylpeptidase
- malabsorption
-
goblet
-
3.2.1.20
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enterocyte-like
- isomaltose
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3.4.11.2
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intestine-specific
-
carbohydrase
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small-intestinal
- aminopeptidase-n
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postconfluent
-
crypt-villus
-
paneth
- 1-deoxynojirimycin
-
bloating
- dextrin
- agriculture
- medicine
Reaction
Synonyms
alpha-glucosidase, glucosidase, sucrose alpha-, intestinal sucrase, isomaltase, More, PF0132, pro-SI, SI, sucrase, sucrase isomaltase, sucrase-invertase, sucrase-isomaltase, sucrase-isomaltase enzyme complex, sucrase/isomaltase, sucrose alpha-glucohydrolase, sucrose hydrolase, SUH
ECTree
3.2.1.48 sucrose alpha-glucosidaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.2.1.48 - sucrose alpha-glucosidase
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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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
-
-
?
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
?
-
-
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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?
