EC Number   |
Cofactor |
Reference |
|---|
    1.5.5.2 | FAD |
proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor, redox active prosthetic group |
743834 |
| 1.5.5.2 | FAD |
TcPRODH is a FAD-dependent protein, key residues involved in cofactor (FAD) binding are Arg431 and Glu559 |
743635 |
| 1.5.5.2 | FMN |
- |
739932 |
| 1.5.5.2 | FMN |
proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor, redox active prosthetic group |
743834 |
| 1.5.5.2 | more |
the recombinant holo form of MBP-tagged TtProDH, as produced in Escherichia coli TOP10 cells, contains about three times more FMN than FAD. The crystal structure of TtProDH variant DELTAABC, which lacks helices alphaA, alphaB and alphaC, shows no electron density for an AMP moiety of the cofactor. ProDH adopts a distorted (betalpha)8 TIM-barrel fold and is the only known TIM-barrel enzyme that contains an FAD cofactor. One cofactor molecule per enzyme subunit |
743834 |
| 1.5.5.2 | phenazine methosulfate |
- |
742487 |
| 1.5.5.2 | [4Fe-4S]-center |
- |
739932 |
