Calpain-2
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| Calpain-2 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.22.53 | ||||||||
| CAS number | 702693-80-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Calpain-2 (EC 3.4.22.53, calcium-activated neutral protease II, m-calpain, milli-calpain) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction
- Broad endopeptidase specificity
This enzyme belongs to the peptidase family C2.
See also
References
- ↑ Strobl, S., Fernandez-Catalan, C., Braun, M., Huber, R., Masumoto, H., Nakagawa, K., Irie, A., Sorimachi, H., Bourenkow, G., Bartunik, H., Suzuki, K. and Bode, W. (2000). "The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium". Proc. Natl. Acad. Sci. USA 97: 588–592. doi:10.1073/pnas.97.2.588. PMC 15374. PMID 10639123.
- ↑ Dutt, P., Spriggs, C.N., Davies, P.L., Jia, Z. and Elce, J.S. (2002). "Origins of the difference in Ca2+ requirement for activation of μ- and m-calpain". Biochem. J. 367: 263–269. PMID 12014988.
External links
- Calpain-2 at the US National Library of Medicine Medical Subject Headings (MeSH)
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