Calpain-2
| 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, Bode W (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. 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.
External links
- Calpain-2 at the US National Library of Medicine Medical Subject Headings (MeSH)
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