EC Number   |
Cofactor |
Reference |
|---|
   1.7.1.6 | FAD |
- |
394310, 723925 |
| 1.7.1.6 | FAD |
about 60% of the activity in presence of FMN. FAD binds to the apo-form and the bound FAD is stably retained in the enzyme molecule without degradation to FMN. The isoalloxazine ring of FAD localizes at the same site and plays the same role as that of FMN in the enzyme |
725732 |
| 1.7.1.6 | FAD |
added FAD stimulates reaction |
657603 |
| 1.7.1.6 | FAD |
increases activity |
394295, 394302, 394303, 394306, 394307, 394308 |
| 1.7.1.6 | FAD |
one mol of enzyme contains 2 mol of FAD |
394296 |
| 1.7.1.6 | FAD |
prosthetic group |
394309 |
| 1.7.1.6 | flavin |
prosthetic group seems to be flavin |
394295 |
| 1.7.1.6 | flavin |
typical flavoprotein absorption spectrum |
394296 |
| 1.7.1.6 | FMN |
- |
673224, 674607, 696845, 696902, 697473, 697495, 698629, 698751, 700040, 724045, 724120, 724384, 724864, 725732, 726423, 743853, 763991, 765737 |
| 1.7.1.6 | FMN |
a flavin-dependent azoreductase, FMN is anchored by a series of sequence-independent hydrogen bonds to a structural motif referred to as the FMN binding cradle. One molecule of flavin is bound within each active site and is required for activity |
742211 |
