Caspase 2

Caspase 2 is an enzyme that proteolytically cleaves other proteins.It belongs to a family of cysteine proteases called caspases that only cleave proteins at an amino acid following a aspartic acid residue. Within this family, caspase 2 is part of the Ich-1 subfamily. It is one of the most conserved caspases in different species of animal. Caspase 2 has a similar amino acid sequence to initiator caspases, including caspase 1, caspase 4, caspase 5 and caspase 9. It is produced as a zymogen, which contains a long pro-domain that is similar to that of caspase 9 and contains a protein interaction domain known as a CARD domain. Pro-caspase-2 contains two subunits, p19 and p12. It has been shown to associate with several proteins involved in apoptosis using its CARD domain, including RIP-associated Ich-1/Ced-3-homologue protein with a death domain (RAIDD), apoptosis repressor with caspase recruitment domain (ARC) and death effector filament-forming Ced-4 like apoptosis protein (DEFCAP). [cite journal |author=Zhivotovsky B, Orrenius S |title=Caspase-2 function in response to DNA damage |journal=Biochem. Biophys. Res. Commun. |volume=331 |issue=3 |pages=859–67 |year=2005 |pmid=15865942 |doi=10.1016/j.bbrc.2005.03.191]

References

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