[HTML][HTML] A sequential two-step mechanism for the production of the mature p17: p12 form of caspase-3 in vitro
Z Han, EA Hendrickson, TA Bremner… - Journal of Biological …, 1997 - ASBMB
The apoptotic cysteine protease, caspase-3, is expressed in cells as an inactive 32-kDa
precursor from which 17 kDa (p17) and 12 kDa (p12) subunits of the mature caspase-3 are
proteolytically generated during apoptosis. Two amino acid sequences, ESMD↓ S (amino
acids 25–29) and IETD↓ S (amino acids 172–176), in the precursor have been defined as
the cleavage sites for the production of the p17 and p12 subunits. Using a cell-free assay
system, we demonstrate that the caspase-3 precursor appears to be cleaved first at the …
precursor from which 17 kDa (p17) and 12 kDa (p12) subunits of the mature caspase-3 are
proteolytically generated during apoptosis. Two amino acid sequences, ESMD↓ S (amino
acids 25–29) and IETD↓ S (amino acids 172–176), in the precursor have been defined as
the cleavage sites for the production of the p17 and p12 subunits. Using a cell-free assay
system, we demonstrate that the caspase-3 precursor appears to be cleaved first at the …
