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Metacaspase 2 of Trypanosoma brucei is a calcium‐dependent cysteine peptidase active without processing
Author(s) -
Moss Catherine X.,
Westrop Gareth D.,
Juliano Luiz,
Coombs Graham H.,
Mottram Jeremy C.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.11.009
Subject(s) - trypanosoma brucei , cysteine , biochemistry , proteolysis , cysteine protease , chemistry , enzyme , biology , microbiology and biotechnology , gene
Metacaspases are cysteine peptidases that are distantly related to the caspases, for which proteolytic processing is central to their activation. Here, we show that recombinant metacaspase 2 (MCA2) from Trypanosoma brucei has arginine/lysine‐specific, Ca 2+ ‐dependent proteolytic activity. Autocatalytic processing of MCA2 occurred after Lys55 and Lys268; however, this was shown not to be required for the enzyme to be proteolytically active. The necessity of Ca 2+ , but not processing, for MCA2 enzymatic activity clearly distinguishes MCA2 from the caspases and would be consistent with different physiological roles.