EC Number   |
Posttranslational Modification |
Reference |
|---|
   2.4.1.16 | glycoprotein |
- |
488638 |
| 2.4.1.16 | glycoprotein |
purified chitin synthase complex can be stained with Calcofluor White suggesting that it is either glycosylated, or still associated with chitin fibrils |
704022 |
| 2.4.1.16 | phosphoprotein |
phosphorylation site mapping, Chs2 contains twelve phosphorylation sites, all in the N-terminal domain, phosphorylation of the N-terminal domain is important for Chs2 stability, these sites might play an important role in the cell cycle-dependent degradation of the enzyme, and thus in cell division |
-, 685019 |
| 2.4.1.16 | proteolytic modification |
- |
488656, 488663 |
| 2.4.1.16 | proteolytic modification |
activated by acid proteases, slightly activated by trypsin, inhibited by neutral proteases |
488656 |
| 2.4.1.16 | proteolytic modification |
activated by all proteases |
488656 |
| 2.4.1.16 | proteolytic modification |
activated by trypsin |
488664 |
| 2.4.1.16 | proteolytic modification |
activity can be increased 6fold by digestion of the enzyme preparation with trypsin |
488647 |
| 2.4.1.16 | proteolytic modification |
activity increases up to 20times by digestion with trypsin |
488638 |
| 2.4.1.16 | proteolytic modification |
affinity-purified enzyme requires protease treatment to give rise to enzyme activity |
706474 |
