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Literature summary for 7.2.2.10 extracted from
- Two types of proton-modulated calcium binding in the sarcoplasmic reticulum Ca2+-ATPase. II. Characterization of their calcium bindings (1994), J. Biol. Chem., 269, 30822-30827.
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Oryctolagus cuniculus | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| skeletal muscle | - |
Oryctolagus cuniculus | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O + Ca2+/out | existence of two different conformations of chemically equivalent Ca2+-ATPase: E1, the high affinity state for Ca2+ and E2, the low affinity state for Ca2+ | Oryctolagus cuniculus | ADP + phosphate + Ca2+/in | - |
? |  |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
different types of proton participation in E1 to E2 transition and in calcium binding | Oryctolagus cuniculus |
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Release 2023.1 (January 2023)
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