EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.14.5 | glycoprotein |
- |
649200, 649229, 663815, 679973, 697489, 697519, 703784 |
| 3.4.14.5 | glycoprotein |
11% glycosylation |
653298 |
| 3.4.14.5 | glycoprotein |
9 N-glycosylation sites, glycosylation is no prerequisite for enzyme activity, dimerization or binding of adenosine deaminase, structural analysis |
653810 |
| 3.4.14.5 | glycoprotein |
at Asn85, Asn150, and Asn229, glycosylation reduces the activity, and is not necessary for thermal stability |
653913 |
| 3.4.14.5 | glycoprotein |
glycosylation can be estimated to account for 24% of the molecular mass of the whole glycosylated protein |
731664 |
| 3.4.14.5 | glycoprotein |
glycosylation is a prerquisite for tetramer formation |
650930 |
| 3.4.14.5 | glycoprotein |
heavily glycosylated, differing in the pattern dependent on the enzyme origin |
651079 |
| 3.4.14.5 | glycoprotein |
heterologous glycosylation, several isozymes |
649281 |
| 3.4.14.5 | glycoprotein |
N-glycosylation at Asn279 is important for adenosine deaminase binding |
653593 |
| 3.4.14.5 | glycoprotein |
N-glycosylation sites are N85, N92, N150, N219, N229, N281, N321, N520, N685, glycosylation is not important for catalytic activity, homodimer formation and adenosine deaminase binding |
653811 |
