Background
Caspase-3 is a critical executioner of apoptosis, as it is either partially or totally responsible for the proteolytic cleavage of many key proteins, such as the nuclear enzyme poly polymerase. Activation of caspase-3 requires proteolytic processing of its inactive zymogen into activated p17 and p12 fragments. Cleavage of caspase-3 requires the aspartic acid residue at the P1 position.
References
[1] Fernandes-Alnemri, T. et al. (1994) J Biol Chem 269, 30761-4.
[2] Nicholson, D.W. et al. (1995) Nature 376, 37-43.
