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
-
medicine
- 3.2.1.48
- border
-
brush
- lactase
- enterocytes
- disaccharidase
-
caco-2
- mucosal
-
crypt
- jejunal
- starch
- maltase-glucoamylase
-
brush-border
- glucoamylase
- maltose
-
lactase-phlorizin
- ileum
- trehalase
- microvillus
- acarbose
-
basolateral
-
postprandial
-
dipeptidyl
- villin
-
suckling
-
dipeptidylpeptidase
- malabsorption
-
goblet
-
3.2.1.20
-
enterocyte-like
- isomaltose
-
3.4.11.2
-
intestine-specific
-
carbohydrase
-
small-intestinal
- aminopeptidase-n
-
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
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Subunits
Subunits on EC 3.2.1.48 - sucrose alpha-glucosidase
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dimer
monomer
additional information
dimer
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1 * 112000 + 1* 100000, hetero-dimer, 2 catalytically active sites for maltase and sucrase
dimer
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1 * 140000 - 160000 + 1 * 140000 -160000 2 large subunits, EC 3.2.1.48 and EC 3.2.1.10, functional dimer, SDS-PAGE
additional information
human maltase-glucoamylase and sucrase-isomaltase are composed of duplicated catalytic domains, N- and C-terminal, which display overlapping substrate specificities
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
additional information
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residues Arg516 and Asp138 are not engaged in salt-bridge formation in the resting enzyme from Xanthomonas campestris pv. campestris in contrast to the enzyme from Xanthomonas axonopodis pv. glycines. In the absence of the salt bridge an opening is created which gives access to subsite 1 from the nonreducing end