EC Number   |
Posttranslational Modification |
Reference |
|---|
    3.1.3.8 | glycoprotein |
- |
-, 649584, 649616, 651384, 653451, 653518, 678749, 682689, 708831, 710482 |
| 3.1.3.8 | glycoprotein |
28.8% glycosylation |
-, 677788 |
| 3.1.3.8 | glycoprotein |
31% carbohydrate |
650588 |
| 3.1.3.8 | glycoprotein |
36% glycosylation |
114250 |
| 3.1.3.8 | glycoprotein |
after treatment with EndoH, protein gives one band of 50 kDa in SDS-PAGE |
729467 |
| 3.1.3.8 | glycoprotein |
analysis of second virial coefficients of the heavily glycosylated phytase and its enzymatically deglycosylated counterpart. The native forms of phytase and deglycosylated phytase are equally repulsive at the studied pH 8. When thermally denatured, the second virial coefficient of deglycosylated phytase decreases whereas it remaines unchanged for phytase. The expanding effect of the glycans on the denatured protein conformation relies on steric hindrance that limits the range of torsion angles available to the polypeptide |
707750 |
| 3.1.3.8 | glycoprotein |
contains 30.5% total carbohydrate |
652593 |
| 3.1.3.8 | glycoprotein |
enzyme AppAS contains three potential sites of N-glycosylation, recombinant nontagged enzyme from Pichia pastoris strain GS115(his4) is glycosylated, deglycosylation of rAppAP is carried out using Endo H deglycosylase |
751936 |
| 3.1.3.8 | glycoprotein |
glycosylation of six potential N-glycosylation sites |
-, 752009 |
| 3.1.3.8 | glycoprotein |
in silico analysis reveals 4 potential N-glycosylation sites, Asp165,Asp200, Asp275 and Asp346, and 3 potential O-glycosylation sites, Thr185, Thr274, and Thr321, in the enzyme |
750839 |
