EC Number   |
Posttranslational Modification |
Reference |
|---|
    1.13.11.11 | acetylation |
weaning exacerbates the deacetylation of tryptophan 2,3-dioxygenase. Weaning alters the tryptophan 2,3-dioxygenase activity by affecting the acetylation state of the enzyme in piglets livers |
765327 |
| 1.13.11.11 | ubiquitination |
in low tryptophan, the lack of tryptophan binding in the exosites destabilizes the tetramer into inactive monomers and dimers and unmasks a four-amino acid degron that triggers polyubiquitination of tryptophan 2,3-dioxygenase by SKP1-CUL1-F-box complexes, resulting in proteasome-mediated degradation of the enzyme and rapid interruption of tryptophan catabolism |
765688 |
| 1.13.11.11 | ubiquitination |
the enzyme can be recognized and ubiquitinated by two E3 ubiquitin ligases, gp78/AMFR and CHIP, and subsequently degraded via ubiquitin-dependent proteasomal degradation pathway. 15 ubiquitination K-sites are identified. Trp-binding to an exosite impedes its proteolytic degradation |
764108 |
