Calpain-2
Calpain-2 | |||||||||
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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 | ||||||||
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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. (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.; Elce, J.S. (2002). "Origins of the difference in Ca2+ requirement for activation of μ- and m-calpain". Biochem. J. 367: 263–269. doi:10.1042/bj20020485. PMID 12014988.
External links
- Calpain-2 at the US National Library of Medicine Medical Subject Headings (MeSH)
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