EC Number   |
Cofactor |
Reference |
|---|
    1.5.8.4 | FAD |
- |
392527, 741817, 742499 |
| 1.5.8.4 | tetrahydrofolate |
- |
741817, 742499 |
| 1.5.8.4 | Tetrahydropteroylpentaglutamate |
- |
392496, 392500, 392516, 392520, 392526 |
| 1.5.8.4 | more |
1-methoxy-5-methylphenazinium methylsulfate can act as electron acceptor |
657277 |
| 1.5.8.4 | more |
2,6-dichlorophenolindophenol can act as electron acceptor |
657277 |
| 1.5.8.4 | FAD |
A280/A450 ratios of the highly pure protein fractions are between 14-16 and 20-25 for wild-type and mutant H109R, respectively. The redox potential for the reduction of FAD is -93 mV |
742499 |
| 1.5.8.4 | FAD |
absolutely required, covalently bound to the apoenzyme via a histidinyl(N3)-(8alpha)FAD linkage, cofactor-free apoenzyme shows 70% reduced activity compared to the holoenzyme |
657277 |
| 1.5.8.4 | FAD |
covalent attachment of FAD to the apoenzyme proceeds in vitro spontaneously and does not require a mitochondrial protein factor |
392526 |
| 1.5.8.4 | FAD |
covalently bound |
392496, 392497, 392498, 392499, 392500, 392501, 392520, 392524, 392525, 392526 |
| 1.5.8.4 | FAD |
FAD is covalently bound via an autocatalytic reaction |
687135 |
