ABSTRACT
The mechanism by which caspases cleave substrates is a multistep process that involves several distinct steps. First, the caspase must be converted from the inactive precursor protein (the procaspase) to the active form, which then binds a protein substrate and catalyzes the subsequent cleavage of a peptide bond. This highly coordinated process results in the activation of caspases when required, yet keeps the proteins inactive to prevent aberrant cell death.
