Any feedback?
Literature summary extracted from
- Involvement of calpains in Ca2+-induced disruption of excitation-contraction coupling in mammalian skeletal muscle fibers (2009), Am. J. Physiol. Cell Physiol., 296, C1115-C1122.
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.22.52 | leupeptin | - |
Homo sapiens |  |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.22.52 | Ca2+ | mu-calpain is autolytically activated at micromolar Ca2+, mice muscle fibers that are partially excitation-contraction uncoupled by exposure to 0.005 mM Ca2+ for 3 min (no ATP) show the presence of autolytic activation of a proportion of the human mu-calpain present | Homo sapiens | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.22.52 | Homo sapiens | - |
- |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.4.22.52 | erythrocyte | - |
Homo sapiens | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.22.52 | titin + H2O | - |
Homo sapiens | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.22.52 | mu-calpain | - |
Homo sapiens |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.4.22.52 | physiological function | mu-calpain is responsible for Ca2+-induced disruption of excitation-contraction coupling | Homo sapiens |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
