EC Number   |
Natural Substrates |
|---|
   1.7.2.3 | trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+ |
- |
| 1.7.2.3 | trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H+ |
- |
| 1.7.2.3 | trimethylamine-N-oxide + electron donor |
- |
| 1.7.2.3 | trimethylamine-N-oxide + electron donor |
anaerobic respiration |
| 1.7.2.3 | trimethylamine-N-oxide + enzyme-MoIV |
anaerobic respiration |
| 1.7.2.3 | trimethylamine-N-oxide + electron donor |
cytochrome 554,557 may be the physiological electron donor |
| 1.7.2.3 | trimethylamine-N-oxide + electron donor |
cytochrome c-556 may be the physiological electron donor |
| 1.7.2.3 | trimethylamine N-oxide + NADH |
enzyme is highly specific for trimethylamine oxide as alternative terminal electron acceptor |
| 1.7.2.3 | more |
enzyme is probably required for acquisition of molybdenum cofactor and translocation of the trimethylamine reductase TorA, EC 1.6.6.9, monomeric and dimeric enzyme forms bind to Tor A, the dimeric form binds more efficiently |
| 1.7.2.3 | trimethylamine N-oxide + (ferrocytochrome c)-subunit + H+ |
reaction mechanism |
