Moss, C.X., Westrop, G.D., Juliano, L., Coombs, G.H. and Mottram, J.C. (2007) Metacaspase 2 of Trypanosoma brucei is a calcium-dependent cysteine peptidase active without processing. FEBS Letters, 581(29), pp. 5635-5639. (doi: 10.1016/j.febslet.2007.11.009)
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Abstract
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<sup>2+</sup>-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<sup>2+</sup>, but not processing, for MCA2 enzymatic activity clearly distinguishes MCA2 from the caspases and would be consistent with different physiological roles.
Item Type: | Articles |
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Status: | Published |
Refereed: | Yes |
Glasgow Author(s) Enlighten ID: | Moss, Dr Catherine and Mottram, Professor Jeremy |
Authors: | Moss, C.X., Westrop, G.D., Juliano, L., Coombs, G.H., and Mottram, J.C. |
College/School: | College of Medical Veterinary and Life Sciences > School of Infection & Immunity |
Journal Name: | FEBS Letters |
ISSN: | 0014-5793 |
ISSN (Online): | 1873-3468 |
Published Online: | 13 November 2007 |
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