Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
42396 | - |
1 * 42396, calculated, 1 * 50000, SDS-PAGE | Mycobacterium sp. |
50000 | - |
gel filtration | Mycobacterium sp. |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium sp. | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 ferricyanide + NADH | - |
Mycobacterium sp. | 2 ferrocyanide + NAD+ + H+ | - |
? | |
2 ferricytochrome c + NADH | - |
Mycobacterium sp. | 2 ferrocytochrome c + NAD+ + H+ | - |
? | |
ferricytochrome c + NADH | - |
Mycobacterium sp. | ferrocytochrome c + NAD+ + H+ | - |
r |
Subunits | Comment | Organism |
---|---|---|
monomer | 1 * 42396, calculated, 1 * 50000, SDS-PAGE | Mycobacterium sp. |
More | enzyme interacts functionally with its redox partner, the Fe3S4 protein ferredoxin, and with the Fe2S2 protein adrenodoxin. Ferredoxin requires its specific NADH:ferredoxin reductase from the P450 system for efficient catalytic function | Mycobacterium sp. |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
4.5 | - |
ferricytochrome c | pH 8.5, 30°C | Mycobacterium sp. | |
60.2 | - |
ferricyanide | pH 8.5, 30°C | Mycobacterium sp. |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | spectral maxima at 273, 378 and 452 nm, 0.75 mol of FAD per mol of protein | Mycobacterium sp. |