EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.11.1.5 | E290C | formation of a covalent complex with cytochrome c mutant K79C, kinetic studies. Residual activity of complex is due to unreacted enzyme that copurifies with the complex. In the complex, the Pelletier-Kraut site is blocked which results in zero catalytic activity | Saccharomyces cerevisiae |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.11.1.5 | 0.002 | - |
ferrocytochrome c | recombinant wild-type, pH 7.5, 25°C, 100 mM phosphate buffer | Saccharomyces cerevisiae | |
1.11.1.5 | 0.011 | - |
ferrocytochrome c | covalent complex of mutant E290C, pH 7.5, 25°C, 100 mM phosphate buffer. Activity is due to unreacted enzyme copurifying with the complex | Saccharomyces cerevisiae | |
1.11.1.5 | 0.047 | - |
ferrocytochrome c | recombinant wild-type, pH 7.5, 25°C, 10 mM phosphate buffer | Saccharomyces cerevisiae | |
1.11.1.5 | 0.13 | - |
ferrocytochrome c | covalent complex of mutant E290C, pH 7.5, 25°C, 10 mM phosphate buffer. Activity is due to unreacted enzyme copurifying with the complex | Saccharomyces cerevisiae |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.11.1.5 | Saccharomyces cerevisiae | - |
- |
- |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.11.1.5 | 2 ferrocytochrome c + H2O2 + 2 H+ = 2 ferricytochrome c + 2 H2O | only ferrocytochrome c bound at the Pelletier-Kraut site of enzyme is oxidized during turnover | Saccharomyces cerevisiae |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.11.1.5 | ferrocytochrome c + H2O2 | - |
Saccharomyces cerevisiae | ferricytochrome c + 2 H2O | - |
? |