EC Number   |
Posttranslational Modification |
Reference |
|---|
   2.4.1.B62 | proteolytic modification |
in presence of dithiothreitol or 2-mercaptoethanol, toxin A undergoes autocatalytic cleavage to an N-terminal catalytic domain of 60 kDa and a C-terminal part of 250 kDa. N-ethylmaleimide or iodoacetamide block this cleavage |
727860 |
| 2.4.1.B62 | proteolytic modification |
in presence of dithiothreitol or 2-mercaptoethanol, toxin B undergoes autocatalytic cleavage with release of the catalytic domain and a fragment of 210 kDa. Myo-inositol hexakisphosphate also facilitates cleavage and has a synergistic effect with dithiothreitol. Co-treatment of toxin B with N-ethylmaleimide blocks the processing induced by myo-inositol hexakisphosphate |
727860 |
| 2.4.1.B62 | proteolytic modification |
maturation of the host cell endosome causes a conformational change in the pore-forming domain of TcsL, causing it to form a pore in the endosomal membrane. The autoprocessing domain is activated by host inositol hexakisphosphate and cleaves the glucosyltransferase domain (GTD), presumably to permit access to substrates residing at the plasma membrane |
-, 759813 |
| 2.4.1.B62 | proteolytic modification |
the toxin requires InsP6-dependent autocleavage for activation |
760217 |
| 2.4.1.B62 | proteolytic modification |
toxin A undergoes autocatalytic processing. The glucosyltransferase activity of the TcdA(1-1832) protein is activated by autoproteolysis. The presence of the autoprotease domain, residues 543-800, is restricting the activity of the glucosyl transferase domain |
-, 727939 |
