EC Number   |
Cofactor |
Reference |
|---|
  1.1.5.12 | FAD |
- |
727253, 740028 |
| 1.1.5.12 | FAD |
1 mol of FAD per mol of enzyme |
740643 |
| 1.1.5.12 | FAD |
the enzyme contains a flavin adenine dinucleotide (FAD)-containing dehydrogenase domain. Compared to the intact enzyme, the FAD-containing dehydrogenase domain shows increased catalytic efficiency with cytochrome c as the electron acceptor, but it completely loses the ability to use coenzyme Q10. The FAD containing dehydrogenase domain is no longer associated with the cell membrane, and it can not support the utilization of D-lactate as a carbon source |
763205 |
| 1.1.5.12 | FAD |
the enzyme contains one FAD molecule |
763205 |
| 1.1.5.12 | FAD |
the ratio of Fe-S D-iLDH to FAD is 0.92. Compared to the intact enzyme, the FAD-containing dehydrogenase domain shows increased catalytic efficiency with cytochrome c as the electron acceptor, but it completely lost the ability to use coenzyme Q10. The isolated FAD-containing dehydrogenase domain is no longer associated with the cell membrane, and it can not support the utilization of D-lactate as a carbon source |
761384 |
| 1.1.5.12 | FAD |
visible absorption spectrum of the purified enzyme shows a broad peak at around 450 nm and a shoulder at around 480 nm |
740029 |
| 1.1.5.12 | Fe-S center |
protein is predicted to bind three [4Fe-4S] clusters and a [3Fe-4S] cluster overall |
761384 |
| 1.1.5.12 | Fe-S center |
the enzyme contains an Fe-S oxidoreductase domain. The Fe-S oxidoreductase domain functions as an electron transfer component to facilitate the utilization of quinone as an electron acceptor by the enzyme (Fe-S D-iLDH), and it helps the enzyme associate with the cell membrane |
763205 |
| 1.1.5.12 | Fe-S cluster |
the enzyme contains an Fe-S oxidoreductase domain that functions as an electron transfer component to facilitate the utilization of quinone as an electron acceptor. It helps the enzyme to associate with the cell membrane |
763205 |
