EC Number   |
Cofactor  |
Reference |
|---|
   1.14.15.8 | adrenodoxin |
- |
693956 |
| 1.14.15.8 | adrenodoxin |
dependent on |
725584 |
| 1.14.15.8 | cytochrome P450 |
- |
724061, 725584 |
| 1.14.15.8 | cytochrome P450meg |
it is possible to resolve the hydroxylase system into three proteins: a strictly NADPH-dependent FMN-containing flavoprotein (megaredoxin reductase), an iron-sulfur protein (megaredoxin), and cytochrome P-450 (P-450meg). The activity of the 15beta-hydroxylase system is fully reconstituted upon combination of these three proteins and addition of NADPH. Megaredoxin has an apparent sulfur to iron ratio of 0.98 and shows g-signals at 1.90, 1.93, and 2.06 when analyzed by electron paramagnetic resonance spectroscopy |
698682 |
| 1.14.15.8 | Ferredoxin |
- |
724061 |
| 1.14.15.8 | heme |
- |
696142, 725584 |
| 1.14.15.8 | heme |
deoxycorticosterone binds in the heme pocket near the iron ligand |
695980 |
| 1.14.15.8 | heme |
presence of dehydroabietic acid does not induce a high-spin shift of the enzyme |
744706 |
| 1.14.15.8 | heme |
steroids beta-estradiol, estrone, pregnenolone and 17alpha-hydroxypregnenolone, do not shift the heme iron into the high-spin form |
744148 |
| 1.14.15.8 | heme |
the heme content of cytochrome P-450meg is 0.94 nmol of heme per nmol of cytochrome P-450 |
698682 |
