EC Number   |
Cofactor |
Reference |
|---|
   1.8.3.2 | FAD |
- |
393064, 393065, 657645, 659578, 691085, 724056, 724998, 742490, 743627, 743883, 764692 |
| 1.8.3.2 | FAD |
at a diminutive FAD binding domain, the isoalloxazine ring of the flavin prosthetic group is bound at the mouth of a 4-helix bundle in each subunit with a 5th small helix adjacent to the adenine moiety of FAD. A proximal redox-active disulfide is located adjacent to the C4a position of the isoalloxazine ring |
741890 |
| 1.8.3.2 | FAD |
bound to the enzyme |
659861 |
| 1.8.3.2 | FAD |
contains FAD |
393066 |
| 1.8.3.2 | FAD |
dependent on |
393061, 393063, 658104, 659585, 659861, 659862, 659912 |
| 1.8.3.2 | FAD |
dependent on, N-terminal cysteine pair contributes to the correct arrangement of the FAD-binding fold |
658616 |
| 1.8.3.2 | FAD |
dependent on, noncovalently bound to the enzyme, Cys62 and Cys65 are involved in redox cycling of the FAD moiety essential for enzyme activity |
660455 |
| 1.8.3.2 | FAD |
dependent on, quantitative analysis of formation or decay of RSS*R radical, and the flavin quinone, semiquinone, and hydroquinone, overview |
704513 |
| 1.8.3.2 | FAD |
dependent on. The three disulfides of the enzyme are not essential for FAD binding |
704550 |
| 1.8.3.2 | FAD |
dithionite and photochemical reductions of Erv2p show full reduction of the flavin cofactor after the addition of 4 electrons with a midpoint potential of -200 mV at pH 7.5. No charge-transfer complex between a proximal thiolate and the oxidized flavin |
690893 |
