EC Number   |
Cofactor |
Reference |
|---|
   1.14.14.20 | FAD |
- |
701875 |
| 1.14.14.20 | FAD |
activity of the oxygenase component His6PheA1 of phenol hydroxylase is strictly dependent on FAD |
701875 |
| 1.14.14.20 | FAD |
PheA2 uses FAD both as a substrate and as a prosthetic group, strictly dependent on, neither FMN nor riboflavin can replace FAD in this reaction. PheA2 is a a homodimer, with each subunit containing a highly fluorescent FAD prosthetic group |
659279 |
| 1.14.14.20 | FADH2 |
- |
701875, 736132, 736171 |
| 1.14.14.20 | FADH2 |
FAD is again reduced at the expense of NADH and NADPH |
736121 |
| 1.14.14.20 | FADH2 |
FAD is bound to PheA2, binding structure analysis, overview |
659279 |
| 1.14.14.20 | FADH2 |
PheA2 is a single domain homodimeric protein with each FAD-containing subunit being organized around a six-stranded beta-sheet and a capping alpha-helix. The tightly bound FAD prosthetic group binds near the dimer interface, and the re face of the FAD isoalloxazine ring is fully exposed to solvent, binding structure, overview |
736400 |
| 1.14.14.20 | FMN |
- |
659279, 701875 |
| 1.14.14.20 | more |
reactive exogenous FAD substrate binds in the NADH cleft after release of NAD product. PheA2 is able to bind one FAD cofactor and one FAD substrate. PheA2 contains a dual binding cleft for NADH and FAD substrate, which alternate during catalysis. No activity with FMN, riboflavin, and NADPH |
736400 |
| 1.14.14.20 | more |
the flavoprotein monooxygenase uses electrons of NAD(P)H to activate and cleave a molecule of oxygen through the formation of an intermediate flavin hydroperoxide and enable the incorporation of an oxygen atom into the substrate |
701875 |
