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Literature summary extracted from
- Inactivation of cytochrome c oxidase by mutant SOD1s in mouse motoneuronal NSC-34 cells is independent from copper availability but is because of nitric oxide (2010), J. Neurochem., 112, 183-192.
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 7.1.1.9 | medicine | the copper-enzyme cytochrome c oxidase has been indicated as a primary molecular target of mutant copper, zinc superoxide dismutase in familial amyotrophic lateral sclerosis | Mus musculus |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 7.1.1.9 | mitochondrion | - |
Mus musculus | 5739 | - |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.1.1.9 | copper | - |
Mus musculus |  |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.1.1.9 | ferrocytochrome c + O2 + H+ | Mus musculus | - |
ferricytochrome c + H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 7.1.1.9 | Mus musculus | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 7.1.1.9 | mitochondria are prepared | Mus musculus |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 7.1.1.9 | NSC-34 cell | - |
Mus musculus | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 7.1.1.9 | ferrocytochrome c + O2 + H+ | - |
Mus musculus | ferricytochrome c + H2O | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 7.1.1.9 | oligomer | - |
Mus musculus |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 7.1.1.9 | complex IV of the mitochondrial electron transport chain | - |
Mus musculus |
| 7.1.1.9 | cytochrome c oxidase | - |
Mus musculus |
| 7.1.1.9 | CytOX | - |
Mus musculus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 7.1.1.9 | 25 | - |
activity assay | Mus musculus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 7.1.1.9 | 7.4 | - |
activity assay | Mus musculus |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 7.1.1.9 | heme a | - |
Mus musculus | |
| 7.1.1.9 | Heme a3 | - |
Mus musculus | |
Expression
| EC Number | Organism | Comment | Expression |
|---|---|---|---|
| 7.1.1.9 | Mus musculus | mutated human superoxide dismutase, SOD1, decreases the Cytox activity, but not the protein content of the Cytox subunit II | down |
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Release 2023.1 (January 2023)
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