Caspase-3, Active

Caspase-3 belongs to the peptidase C14A enzyme family and is known to play an important role in the apoptotic cascade. Caspase-3 exists in both an active form and an inactive pro-enzyme form. Active Caspase-3 cleaves and activates other caspases and is a primary regulator of apoptotic-associated proteolysis. The active enzyme is formed by cleavage of the inactive 32kDa pro-enzyme into the p17 and p12 subunits. These subunits then noncovalently heterodimerize, which precedes the formation of the final antiparallel homodimer consisting of two p17-p12 heterodimers. The active site is localized to the p17 subunit giving the final enzyme two catalytic sites.

Swiss-Prot Accession Number: P42574