EC Number   |
Posttranslational Modification |
Reference |
|---|
    6.3.1.2 | adenylylation |
enzyme activity is regulated by adenylylation-deadenylylation |
661971 |
| 6.3.1.2 | adenylylation |
regulation via adenylation, the enzyme is substrate for Escherichia coli adenylyl transferase, adenylylation state of Mycobacterium bovis enzyme is higher than with the enzyme of pathogenic Mycobacterium tuberculosis |
662218 |
| 6.3.1.2 | adenylylation |
regulation via adenylation, the enzyme is substrate for Escherichia coli adenylyl transferase, but only low adenylylation states are accessible |
-, 662218 |
| 6.3.1.2 | adenylylation |
the enzyme is regulated by adenylylation/deadenylylation. High levels of deadenyllylated biosynthetically active glutamine synthetase are observed in cultures growing with limiting amounts of nitrogen while synthesis of the enzyme is repressed and that present is adenylylated in cultures with excess nitrogen |
391443 |
| 6.3.1.2 | more |
GlnA1 is subject to posttranslational modification, while GlnA2 is not |
692709 |
| 6.3.1.2 | nitrosylation |
isozyme MtGS2a activity is inhibited by thiol residue nitrosylation |
728509 |
| 6.3.1.2 | phosphoprotein |
- |
676918 |
| 6.3.1.2 | phosphoprotein |
phosphorylation in root nodules |
675138 |
| 6.3.1.2 | proteolytic modification |
deduced protein contains a target peptide and is predicted to be driven to the plastid |
714625 |
| 6.3.1.2 | proteolytic modification |
the first 49 amino acids of the N-terminus are predicted to be the transit peptide, the sorting signal for targeting nucleus-encoded proteins to the plastids, which is cleaved during the import. The protein can only assemble to its active form when this sorting signal is removed |
746127 |
