EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|---|
1.18.1.3 | 42396 | - |
1 * 42396, calculated, 1 * 50000, SDS-PAGE | Mycobacterium sp. |
1.18.1.3 | 50000 | - |
gel filtration | Mycobacterium sp. |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.18.1.3 | Mycobacterium sp. | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.18.1.3 | 2 ferricyanide + NADH | - |
Mycobacterium sp. | 2 ferrocyanide + NAD+ + H+ | - |
? | |
1.18.1.3 | 2 ferricytochrome c + NADH | - |
Mycobacterium sp. | 2 ferrocytochrome c + NAD+ + H+ | - |
? | |
1.18.1.3 | ferricytochrome c + NADH | - |
Mycobacterium sp. | ferrocytochrome c + NAD+ + H+ | - |
r |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.18.1.3 | monomer | 1 * 42396, calculated, 1 * 50000, SDS-PAGE | Mycobacterium sp. |
1.18.1.3 | 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. |
EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.18.1.3 | 4.5 | - |
ferricytochrome c | pH 8.5, 30°C | Mycobacterium sp. | |
1.18.1.3 | 60.2 | - |
ferricyanide | pH 8.5, 30°C | Mycobacterium sp. |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.18.1.3 | FAD | spectral maxima at 273, 378 and 452 nm, 0.75 mol of FAD per mol of protein | Mycobacterium sp. |