EC Number   |
Cofactor |
Reference |
|---|
   1.17.3.2 | FAD |
- |
715158, 715273, 745064, 745473 |
| 1.17.3.2 | FAD |
a molybdenum-iron-flavoenzyme |
706259 |
| 1.17.3.2 | FAD |
bovine liver: 1 FAD per subunit (2 per molecule) |
644653 |
| 1.17.3.2 | FAD |
contains FAD, molybdenum and iron in the ratio 1 : 4 : 4 |
393008, 644645 |
| 1.17.3.2 | FAD |
flavoprotein |
392993, 393001, 393008, 644555, 644564, 644565, 644580, 644582, 644619, 644620, 644621, 644622, 644623, 644624, 644625, 644627, 644628, 644629, 644632, 644633, 644635, 644638, 644639, 644640, 644641, 644642, 644643, 644644, 644645, 644646, 644647, 644648, 644649, 644650, 644651, 644653, 644654, 644655, 644657, 644658 |
| 1.17.3.2 | FAD |
one FAD per enzyme molecule |
744875 |
| 1.17.3.2 | FAD |
required for reoxidation of the enzyme, contains two non-identical [2Fe-2S] centers |
689276 |
| 1.17.3.2 | FAD |
role of Asp428 in the FAD reactivity, overview |
715273 |
| 1.17.3.2 | FAD |
the FAD cofactor is open to solvent in XO, but much less accessible in XDH, binding site structure, overview |
703626 |
| 1.17.3.2 | FAD |
the Mo(VI) ion at the active site is reduced to Mo(IV), which then transfers two electrons, via the 2Fe-2S clusters, to the FAD cofactor |
714785 |
