EC Number   |
Cofactor |
Reference |
|---|
   1.11.1.23 | FAD |
FMN and FAD greatly enhance production of fosfomycin. The flavin coenzyme is unlikely an integral part of the epoxidase |
704155 |
| 1.11.1.23 | FAD |
FMN or FAD increase level of fosfomycin production. The effect of FMN is slightly better than that of FAD. The flavin coenzyme is not likely to be an integral part of the epoxidase itself, but it may serve as a surrogate for the putative electron mediator in the in vitro assay |
702205 |
| 1.11.1.23 | FMN |
- |
701900, 727328 |
| 1.11.1.23 | FMN |
a straightforward epoxidase mechanism is proposed that depends on the Lewis acid properties of divalent cations and the redox properties of FMN |
706480 |
| 1.11.1.23 | FMN |
FMN and FAD greatly enhance production of fosfomycin. The flavin coenzyme is unlikely an integral part of the epoxidase |
704155 |
| 1.11.1.23 | FMN |
FMN is an artificial electron mediator for the in vitro HppE activity. It accepts a hydride from NADH and then passes electrons on to reduce the iron center of HppE. Several non-flavin electron mediators can replace FMN |
702208 |
| 1.11.1.23 | FMN |
FMN or FAD increase level of fosfomycin production. The effect of FMN is slightly better than that of FAD. The flavin coenzyme is not likely to be an integral part of the epoxidase itself, but it may serve as a surrogate for the putative electron mediator in the in vitro assay |
702205 |
| 1.11.1.23 | FMN |
if either iron, FMN, or NADH is omitted from the reaction mixture, no product formation is detected. Due to the fact that the reduction of iron requires single electron transfer and NADH is an obligate two-electron donor, FMN is required to mediate the transfer of reducing equivalents from NADH to the active site iron |
702244 |
| 1.11.1.23 | heme |
- |
764973 |
| 1.11.1.23 | NAD(P)H |
- |
727328 |
