Calpain-2 (EC 3.4.22.53 , calcium-activated neutral protease II , m-calpain , milli-calpain ) is an intracellular heterodimeric calcium-activated cysteine protease.[ 1] [ 2] This enzyme catalyses the following chemical reaction
Broad endopeptidase specificity
This enzyme belongs to the peptidase family C2. It is one of 15 proteins in the calpain family.[ 3]
^ Strobl S, Fernandez-Catalan C, Braun M, Huber R, Masumoto H, Nakagawa K, et al. (January 2000). "The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium" . Proceedings of the National Academy of Sciences of the United States of America . 97 (2): 588–92. Bibcode :2000PNAS...97..588S . doi :10.1073/pnas.97.2.588 . PMC 15374 . PMID 10639123 .
^ Dutt P, Spriggs CN, Davies PL, Jia Z, Elce JS (October 2002). "Origins of the difference in Ca2+ requirement for activation of mu- and m-calpain" . The Biochemical Journal . 367 (Pt 1): 263–9. doi :10.1042/bj20020485 . PMC 1222847 . PMID 12014988 .
^ Ono Y, Sorimachi H (January 2012). "Calpains: an elaborate proteolytic system" . Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics . 1824 (1): 224–36. doi :10.1016/j.bbapap.2011.08.005 . PMID 21864727 .