3.2.1.108: lactase
This is an abbreviated version!
For detailed information about lactase, go to the full flat file.
Word Map on EC 3.2.1.108
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3.2.1.108
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sucrase
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milk
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maltase
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intolerance
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disaccharidase
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brush
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border
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mucosal
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jejunal
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gastrointestinal
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malabsorption
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breath
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children
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dairy
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wean
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villus
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diarrhea
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enterocytes
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infant
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bowel
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ileum
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hypolactasia
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suckling
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crypt
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duodenal
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aminopeptidase
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piglets
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trehalase
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brush-border
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non-persistence
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sucrase-isomaltase
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maldigestion
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adult-type
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yogurt
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glucoamylase
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3.2.1.23
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isomaltase
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lactulose
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bloating
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small-intestinal
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microvillus
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coeliac
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flatulence
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archaeological
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maltase-glucoamylase
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medicine
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crypt-villus
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pharmacology
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food industry
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cellobiase
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carbohydrases
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formula-fed
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pastor
- 3.2.1.108
- sucrase
- milk
- maltase
- intolerance
- disaccharidase
-
brush
- border
- mucosal
- jejunal
- gastrointestinal
- malabsorption
- breath
- children
-
dairy
-
wean
- villus
-
diarrhea
- enterocytes
- infant
- bowel
- ileum
- hypolactasia
-
suckling
-
crypt
- duodenal
- aminopeptidase
-
piglets
- trehalase
-
brush-border
-
non-persistence
- sucrase-isomaltase
-
maldigestion
-
adult-type
-
yogurt
- glucoamylase
-
3.2.1.23
- isomaltase
- lactulose
-
bloating
-
small-intestinal
- microvillus
-
coeliac
-
flatulence
-
archaeological
- maltase-glucoamylase
- medicine
-
crypt-villus
- pharmacology
- food industry
- cellobiase
-
carbohydrases
-
formula-fed
-
pastor
Reaction
Synonyms
intestinal lactase, lactase, lactase phlorizin hydrolase, lactase phlorizin-hydrolase, lactase-phlorizin hydrolase, lactase-phlorizin hydrolase LPH, lactase-phlorozin hydrolase, lactase/phlorizin hydrolase, LCT, LPH
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Posttranslational Modification
Posttranslational Modification on EC 3.2.1.108 - lactase
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glycoprotein
proteolytic modification
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processing of enzyme to a complex glycosylated protein increases in presence of pro-region
glycoprotein
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existence of two forms of brush border membrane-associated LPH, as N-glycosylated molecule and N- and O-glycosylated molecule
glycoprotein
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two forms of brush border membrane-associated LPH are known, an N-glycosylated, and an N- and O-glycosylated molecule
glycoprotein
the polypeptide stretch in domain II between L735-R868 harbors a unique N-glycosylation site that is responsible for lactase phlorizin-hydrolase retention in the endoplasmic reticulum via association with calnexin and facilitates proper folding of domains I and III before ER exit of lactase phlorizin-hydrolase. A similar N-glycosylation site in domain IV shows comparable effects on the trafficking of lactase phlorizin-hydrolase-derived molecules
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pro-enzyme is cleaved in trans-Golgi network between Arg734 and Leu735, pro-region of enzyme is an intramolecular chaperone, analysis of processing and folding
proteolytic modification
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human LPH is synthesized as a precursor pro-LPH molecule, pro-LPH undergoes proteolytic cleavage to yield mature LPH by a trypsin-like protease that occurs intracellularly
proteolytic modification
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oral doses of insulin-like growth factor I increase the processing efficiency of pro-enzyme but do not affect enzyme activity