| Entry |
|
| Name |
calpain-2;
calcium-activated neutral protease II;
m-calpain;
milli-calpain
|
| Class |
Hydrolases;
Acting on peptide bonds (peptidases);
Cysteine endopeptidases
 |
| Reaction(IUBMB) |
Broad endopeptidase specificity
|
| Comment |
Type example of peptidase family C2. Requires Ca2+ at millimolar concentrations for activity. Cytosolic in animal cells. The active enzyme molecule is a heterodimer in which the large subunit contains the peptidase unit, and the small subunit is also a component of EC 3.4.22.52, calpain-1.
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| Orthology |
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| Genes |
HSA: | | PTR: | | PPS: | | GGO: | | PON: | | MCC: | | MMU: | | RNO: | | CFA: | | AML: | | FCA: | | BTA: | | SSC: | | ECB: | | MDO: | | OAA: | | GGA: | | MGP: | | TGU: | | ACS: | | XLA: | | XTR: | | DRE: | | TRU: | | » show all
 |
| Reference |
|
| Authors |
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. |
| Title |
The crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium. |
| Journal |
Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 588-92. |
| Organism |
|
| Reference |
|
| Authors |
Dutt P, Spriggs CN, Davies PL, Jia Z, Elce JS. |
| Title |
Origins of the difference in Ca2+ requirement for activation of mu- and m-calpain. |
| Journal |
Biochem. J. 367 (2002) 263-9. |
| Organism |
Rattus norvegicus [GN: rno] |
| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: CAS: 702693-80-9 |