EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.22.65 | glycoprotein |
- |
647682 |
| 3.4.22.65 | glycoprotein |
analysis of the glycosylation pattern and comparison to other allergens, mannosylation appears to be a dominant feature among allergens, overview. The main dominant sugars on these allergens are 1-2, 1-3 and 1-6 mannose, the sugar part of the enzyme is recognized by lectins from Datura stramonium lectin, Arachis hypogaea, and Sambucus nigra. Sodium periodate deglycosylation of natural and recombinant enzyme Der p 1 resulting in a significant decrease in the uptake of both Der p 1 preparations into dendritic cells. The recombinant enzyme shows a higher degree of mannans compared to the native enzyme |
732689 |
| 3.4.22.65 | glycoprotein |
different levels of glycosylation or isozymes |
717698 |
| 3.4.22.65 | glycoprotein |
GlcNAc is contained at the non-reducing terminus of the sugar chains of native Der f1 but not of lysylendopeptidase-treated reDEr f1 E(-1)K. Lysylendopeptidase-treated reDEr f1 E(-1)K reacts with Lens culinaris agglutinin but native Der f1 does not , suggesting that fucose is connected with GlcNAc, bound to an asparagine residue, but not of native Der f1 |
647684 |
| 3.4.22.65 | glycoprotein |
N-glycosylation is essential for secretion in insect Sf9 cells but not in Pichia pastoris |
647688 |
| 3.4.22.65 | glycoprotein |
N-glycosylation of the prosequences decelerated the maturation. Systems using Pro-Der p 1 without the prodomain glycosylation are useful for the efficient preparation of a recombinant mature allergen |
665201 |
| 3.4.22.65 | glycoprotein |
the wild-type recombinant enzyme is more highly glycosylated than the native enzyme |
647683 |
| 3.4.22.65 | proteolytic modification |
contribution of the N-terminal region of the Der p 1 prosequence including the N-glycosylation site, Asn(-65), on effective inhibition of proteolytic activity in pro-Der p 1 |
647682 |
| 3.4.22.65 | proteolytic modification |
the Der p 1 enzyme propeptide of 80 amino acids plays an essential role in zymogen folding as an intramolecular chaperone and in the inhibition of its own enzymatic activity |
731348 |
| 3.4.22.65 | proteolytic modification |
the Der p 1 propiece is a potent competitive inhibitor of Der p 1. The Der p 1 propiece behaves as a substrate and is fully degraded during this interaction. The rapid inactivation of Der p 1 prodomain is a mechanism that may contribute to the potency of this allergen |
677434 |
