Caspase
Capases
Capsases belong to a subfamily of proteases known as endopeptidases which cleave target proteins at specific aspartic acids. They hydrolze petide bonds C-terminally in aspartate residues.[1] The caspases have cysteine at their active site and are named due to the 'C' for cysteine and the 'asp' for aspartic acid. Caspases are synthesised in the cell as procaspases [2].
Capases and Apoptosis
Capases are responsible for the programmed death of a cell. In their inactive state capases are present as zymogens, precapases or blocked by specific capases inhibitors. When apoptosis is triggered the capases activate each other forming a cascade. The signal becomes amplified along the cascade and leads to the death of the cell.