EC Number   |
Cofactor |
Reference |
|---|
   1.6.2.2 | FAD |
- |
392811, 394194, 394222, 394225, 657648, 657949, 658252, 658832, 659107, 659255, 659784, 685672, 696154, 696575, 699061, 711543, 712469, 712873, 713204, 741542, 741995, 742304, 742312, 742321, 742875, 743151, 743832 |
| 1.6.2.2 | FAD |
1 mol FAD per mol enzyme |
394203, 394218 |
| 1.6.2.2 | FAD |
1 mol FAD per mol of recombinant enzyme |
394199 |
| 1.6.2.2 | FAD |
calculated results suggest that the electron and/or hydride ion transfer reaction from NADH to FAD can be accelerated in the presence of heme(Fe3+) |
688620 |
| 1.6.2.2 | FAD |
cytochrome b5 reductase is composed of one FAD and one NADH binding domain linked by a hinge region |
685857 |
| 1.6.2.2 | FAD |
flavoprotein, the FAD domain has a large cleft in which the FAD prosthetic group is located. The N-terminus of the NADH domain plays a hinge-connecting role between the two domains, the FAD and the NADH domains |
724801 |
| 1.6.2.2 | FAD |
non-covalentely bound prosthetic group |
657675 |
| 1.6.2.2 | FAD |
non-covalently bound in a large cleft between the two major domains |
657460 |
| 1.6.2.2 | FAD |
redox state of FAD during the b5R catalytic cycle and crystal structures comparion of the fully reduced form and the oxidized form, overview |
725721 |
| 1.6.2.2 | FAD |
the FAD cofactor is located in the cleft between the N-terminal FAD-binding domain and the C-terminal NADH-binding domain. The cofactor is located in the cleft between the two domains and interacts primarily with the FAD-binding domain |
764860 |
