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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Identification and characterization of CPP32/Mch2 homolog 1, a novel cysteine protease similar to CPP32.

We have identified and characterized a novel cysteine protease named CMH-1 that is a new member of the interleukin 1 beta converting enzyme (ICE) family of proteases with substrate specificity for Asp-X. CMH-1 has the highest similarity to CPP32 (52% amino acid identity) and MCH2 (31% identical). CMH-1 shares conserved amino acid residues that form the core structure of ICE as well as those residues involved in catalysis and in the P1 aspartate binding. Overexpression of CMH-1 in COS cells resulted in the processing of CMH-1 and the induction of apoptosis of transfected cells. Coexpression of CMH-1 with poly(ADP-ribose) polymerase (PARP) also resulted in a specific cleavage of PARP. Purified recombinant CMH-1 cleaved PARP but not interleukin 1 beta precursor in vitro.[1]

References

  1. Identification and characterization of CPP32/Mch2 homolog 1, a novel cysteine protease similar to CPP32. Lippke, J.A., Gu, Y., Sarnecki, C., Caron, P.R., Su, M.S. J. Biol. Chem. (1996) [Pubmed]
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