EC Number   |
Posttranslational Modification |
Reference |
|---|
    3.1.1.1 | glycoprotein |
- |
668446, 696128, 700370 |
| 3.1.1.1 | glycoprotein |
63000 Da, SDS-PAGE of glycosylated protein, 58000 Da, SDS-PAGE of non-glycosylated protein |
677732 |
| 3.1.1.1 | glycoprotein |
crystallization data, high-mannose N-linked glycosylation at N79 |
681399 |
| 3.1.1.1 | glycoprotein |
most CES isozymes are glycoproteins, and the carbohydrate chain is required for the enzyme activity |
694289 |
| 3.1.1.1 | glycoprotein |
N-glycosylated residue is Asn275 |
651131 |
| 3.1.1.1 | glycoprotein |
N-glycosylated residue is Asn79 |
651131 |
| 3.1.1.1 | glycoprotein |
N-glycosylated residues are Asn261, Asn272, and Asn550 |
651131 |
| 3.1.1.1 | glycoprotein |
N-glycosylated residues are Asn79 and Asn489 |
651131 |
| 3.1.1.1 | glycoprotein |
N-glycosylated residues are Asn79, Asn107, and Asn489 |
651131 |
| 3.1.1.1 | glycoprotein |
N-glycosylation of hCES2 is relevant for thermostability of the enzyme and also for its in vivo folding or secretion, but is not crucial for enzyme activity. Carboxylesterase 2 (hCES2) is a glycoprotein. Partial or non-glycosylated forms of a secreted form of hCES2 are obtained by three approaches: (i) enzymatic deglycosylation with peptide N-glycosidase F, (ii) incubation with the inhibitor tunicamycin, (iii) site-directed mutagenesis of each or both N-glycosylation sites. Deglycosylated protein does not show a detectable decrease in enzyme activity. The glycans are involved, to some extent, in protein folding in vivo, but removal of glycans does not abrogate the activity of secreted hCES2. Deglycosylation of purified recombinant His10-tagged hCES2 shows a decreased level of detection using the glycoprotein detection method with the deglycosylated bands only being faintly detected probably due to nonspecific binding or to O-glycosylation |
749792 |
