EC Number |
Posttranslational Modification |
Reference |
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3.4.22.63 | proteolytic modification |
autoprocessing, the wild-type 55000 Da GST fusion protein is cleaved to the 43000 Da active form |
647719 |
3.4.22.63 | proteolytic modification |
caspase-10 is activated at the DISC, downstream of death-receptor signaling. Caspases-8 and -10 are recruited to the DISC as intact monomers and recruitment of the caspases to the DISC subsequently leads to their dimerization and activation through induced proximity, mechanism, overview |
717282 |
3.4.22.63 | proteolytic modification |
caspase-10/c and caspase-10/d are splice isoforms. Caspase-10/c is a truncated protein that is essentially a prodomain-only form of the caspase. Caspase-10/d is a hybrid of caspase-10/a (Mch4) and caspase-10/b (FLICE2), as it is identical to FLICE2 except for the small p12 catalytic subunit, which is identical to Mch4 |
647713 |
3.4.22.63 | proteolytic modification |
Mch4 is derived from a single chain proenzym, granzyme B cleaves proMch4 at a IXXD-A processing sequence to produce mature Mch4 |
647431 |
3.4.22.63 | proteolytic modification |
procaspase-10 is activated to caspase-10, mechanism of activation and the role of the inter-subunit cleavage, overview. Caspase-10 follows the proximity-induced dimerization model for apical caspases |
717252 |
3.4.22.63 | proteolytic modification |
procaspase-10 is activated to caspase-10. Activation of caspase-10 is induced in apoptosis |
718261 |
3.4.22.63 | proteolytic modification |
proMch4 can autoprocess after Asp-219 and Asp-372 to generate the two subunits of the mature enzyme : P17, the large subunit and p12, the small subunit |
647447 |
3.4.22.63 | proteolytic modification |
the enzyme is activated by proteoltic cleavage |
732763 |