Cysteinyl aspartate-specific protease Caspases are classed as initiator caspases such as 2, 8, 9 and 10, effector caspases, such as 3, 6 and 7 or inflammatory caspases, such as 1, 4 and 5. They have cysteine residues in their active sites (within a QACXG motif), and catalyse proteolysis at specific aspartate residues. Active caspases are tetramers of two large and two small subunits. They are formed from the cleavage of two procaspase proteins.
any of a group of proteases that mediate apoptosis
intracellular cysteine protease that cleaves protein substrates when activated during apoptosis.
An enzyme that breaks down cell protiens during apoptosis.
A type of protein that is involved in apoptosis. Caspases are characterized by their unusual ability to cleave proteins at specific sites. Active caspases can often activate other caspases, leading to a cascade of protein degradation.
A member of a family of related proteases that take part in initiating and carrying out the cell death response.
Caspases are a group of cysteine proteases, enzymes with a crucial cysteine residue that can cleave other proteins after an aspartic acid residue, a specificity which is unusual among proteases. The name "caspase" derives from this characteristic molecular function: cysteine-aspartic-acid-proteases. Caspases are essential in cells for apoptosis, one of the main types of programmed cell death in development and most other stages of adult life, and have been termed "executioner" proteins for their roles in the cell.