EC Number   |
Cofactor |
Reference |
|---|
   1.10.5.1 | FAD |
- |
658023, 658434, 671708, 671921, 698051, 711432, 711470, 711729, 712829, 725669 |
| 1.10.5.1 | FAD |
1 molecule per subunit, binds to the active site of each subunit |
725071 |
| 1.10.5.1 | FAD |
contains 1 FAD per monomer firmly bound to the enzyme through multiple interactions |
657888 |
| 1.10.5.1 | FAD |
dependent on |
724751 |
| 1.10.5.1 | FAD |
dstabilisation of the cofactor FAD by mutation N18E shows that 2-[125I]-iodo-5-methoxycarbonylamino-N-acetyltryptamine binding is closely linked to the conformational integrity of quinone oxidoreductase 2 |
695860 |
| 1.10.5.1 | FAD |
flavin redox switch, structural changes, overview |
725512 |
| 1.10.5.1 | FAD |
flavoenzyme, binding structure, overview. 2 molecules per enzyme dimer, quantification, overview |
725158 |
| 1.10.5.1 | FAD |
mediates hydride transfer, very tightly bound to the enzyme. Activity of the purified enzyme is not further increased by added FAD |
660397 |
| 1.10.5.1 | FAD |
one prosthetic group per subunit |
394377 |
| 1.10.5.1 | FAD |
the enzyme contains FAD as the sole bound flavin. The prosthetic group can be removed by treatment with acid in ammonium sulfate, and the resolved enzyme may be reactivated by FAD or by higher concentrations FMN |
659111 |
