EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.2.1.108 | glycoprotein |
- |
700144 |
| 3.2.1.108 | glycoprotein |
existence of two forms of brush border membrane-associated LPH, as N-glycosylated molecule and N- and O-glycosylated molecule |
679123 |
| 3.2.1.108 | glycoprotein |
membrane anchored type I glycoprotein |
756114 |
| 3.2.1.108 | glycoprotein |
processing of enzyme to a complex glycosylated protein increases in presence of pro-region |
656110 |
| 3.2.1.108 | 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 |
749964 |
| 3.2.1.108 | glycoprotein |
two forms of brush border membrane-associated LPH are known, an N-glycosylated, and an N- and O-glycosylated molecule |
679123 |
| 3.2.1.108 | proteolytic modification |
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 |
679123 |
| 3.2.1.108 | proteolytic modification |
oral doses of insulin-like growth factor I increase the processing efficiency of pro-enzyme but do not affect enzyme activity |
656599 |
| 3.2.1.108 | proteolytic modification |
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 |
656110 |
