EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.22.60 | proteolytic modification |
- |
647657 |
| 3.4.22.60 | proteolytic modification |
activation site is IQAD (P4,P3,P2,P1) |
647429 |
| 3.4.22.60 | proteolytic modification |
both Mch4 and the serine protease granzyme B cleave proMch3 at a conserved IXXD-S sequence to produce the large and small subunits of the active protease. Mch3 is a target of mature protease in apoptotic cells |
647431 |
| 3.4.22.60 | proteolytic modification |
caspase-7 possesses two cleavage sites after Asp23 and Asp198 |
695998 |
| 3.4.22.60 | proteolytic modification |
cleavage of procaspase-7 of 35 kDa to the active forms of 31 and 20 kDa, TNF-induced caspase-7 activation takes place exclusively within TNF receptosomes |
717539 |
| 3.4.22.60 | proteolytic modification |
CPP32 can efficiently cleave proMch3alpha |
647658 |
| 3.4.22.60 | proteolytic modification |
enzyme is synthesized as an inactive 30000-35000 Da precursor and is thought to be cleaved during apoptosis to generate active fragments of 20000 Da and 10000 Da |
647663 |
| 3.4.22.60 | proteolytic modification |
Mch3alpha is made of two subunits derived from a precursor ProMch3alpha. Asp23 and Asp198 are the most likely processing sites. Bacterially expressed Mch3 has intrinsic autocatalytic and autoactivation activity |
647658 |
| 3.4.22.60 | proteolytic modification |
procaspase-7 is activated by caspase-1 cleavage to caspase-7 |
-, 700916 |
| 3.4.22.60 | proteolytic modification |
procaspase-7 is activated by processing to the mature caspase-7 |
700210 |
