EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.1.1.11 | glycoprotein |
- |
-, 674093, 695057, 714956, 729080, 729774, 730283 |
| 3.1.1.11 | glycoprotein |
Asn-linked N-acetylglucosamine-stub form enzyme, isozyme Ani-PME2 has two glycosylation sites. Uncorrelated rotations are observed about the glycosidic bonds of a partially de-methyl-esterified decasaccharide model substrate. Removal of N-linked high mannose glycans from Ani-PME is performed by MBP-tagged EndoHf or His-tagged PNGaseF, deglycosylated enzyme structure analysis, overview |
751060 |
| 3.1.1.11 | glycoprotein |
carbohydrate detection, overview |
679294 |
| 3.1.1.11 | glycoprotein |
enzyme PME contains one N-glycosylation site, deglycosylation of Sl-pectinases is performed using endoglycosidase H (Endo H), peptide-N-glycosidase F (PNGase F) and O-glycosidase at 37°C |
750786 |
| 3.1.1.11 | glycoprotein |
N-linked glycoprotein, consists of 22 hexoses including 16 mannose, 4 N-acetylglucosamine and 2 glalactose residues |
651557 |
| 3.1.1.11 | glycoprotein |
native protein has about 10% carbohydrates, recombinant protein appears to be hyperglycosylated |
674101 |
| 3.1.1.11 | glycoprotein |
PME1 contains two potential N-linked glycosylation sites, specified by the sequence Asn-X-Ser/Thr in the N-terminal Pro region |
682430 |
| 3.1.1.11 | glycoprotein |
possible glycosylation concluded from the relatively high mass of the kiwi enzyme compared with other plant PMEs |
674087 |
| 3.1.1.11 | glycoprotein |
the enzyme contains three putative O-glycosylation sites and one N-glycosylation site |
-, 751146 |
| 3.1.1.11 | glycoprotein |
the enzyme forms exhibits two principal glycoisoforms |
729867 |
