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Literature summary for 3.4.22.56 extracted from

  • Fernandes-Alnemri, T.; Armstrong, R.C.; Krebs, J.F.; Srinivasula, S.M.; Wang, L.; Bullrich, F.; Fritz, L.C.; Trapani, J.A.; Tomaselli, K.J.; Litwack, G.; Alnemri, E.S.
    In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains (1996), Proc. Natl. Acad. Sci. USA, 93, 7464-7469.
    View publication on PubMedView publication on EuropePMC
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Activating Compound

Activating Compound Comment Organism Structure
Mch4 activation of CPP32 Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
Asp-Glu-Val-Asp-aldehyde
-
 Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
 full-length proCPP32 has a molecular weight of 32000-33000 Da Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P42574
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification both Mch4 and granzyme B cleave recombinant proCPP32 at a conserved IXXD-S sequence to produce the large and small subunits of the active protease. Granzyme B cleaves at Asp175 to generate the small C-terminal subunit, 12000 Da, and te large N-terminal subunit. Cleavage of the prodomain is an autocatalytic activity of the activated CPP32 Homo sapiens