EC Number   |
Cofactor |
Reference |
|---|
    1.3.8.7 | 7,8-dichloro-FAD |
artificial cofactor reconstituted into the enzyme. The flavin ring itself affects the pKa value of the ligand via a charge-transfer interaction with the ligand. Interaction between the ligand and the flavin ring also serves to lower the pKa of the ligand, in addition to the hydrogen bonds at C(1)=O of the ligand |
655926 |
| 1.3.8.7 | 8-amino-FAD |
artificial cofactor reconstituted into the enzyme. The flavin ring itself affects the pKa value of the ligand via a charge-transfer interaction with the ligand. Interaction between the ligand and the flavin ring also serves to lower the pKa of the ligand, in addition to the hydrogen bonds at C(1)=O of the ligand |
655926 |
| 1.3.8.7 | 8-chloro-FAD |
artificial cofactor reconstituted into the enzyme. The flavin ring itself affects the pKa value of the ligand via a charge-transfer interaction with the ligand. Interaction between the ligand and the flavin ring also serves to lower the pKa of the ligand, in addition to the hydrogen bonds at C(1)=O of the ligand |
655926 |
| 1.3.8.7 | 8-cyano-FAD |
artificial cofactor reconstituted into the enzyme. The flavin ring itself affects the pKa value of the ligand via a charge-transfer interaction with the ligand. Interaction between the ligand and the flavin ring also serves to lower the pKa of the ligand, in addition to the hydrogen bonds at C(1)=O of the ligand |
655926 |
| 1.3.8.7 | 8-methoxy-FAD |
artificial cofactor reconstituted into the enzyme. The flavin ring itself affects the pKa value of the ligand via a charge-transfer interaction with the ligand. Interaction between the ligand and the flavin ring also serves to lower the pKa of the ligand, in addition to the hydrogen bonds at C(1)=O of the ligand |
655926 |
| 1.3.8.7 | FAD |
- |
391201, 391323, 391362, 654353, 654679, 657278, 675827, 685133, 685352, 743247 |
| 1.3.8.7 | FAD |
1 mol per mol of subunit |
391272, 391318, 391344 |
| 1.3.8.7 | FAD |
binding of FAD and FAD anologues |
391344 |
| 1.3.8.7 | FAD |
FAD can be removed by a treatment of the enzyme with a suspension of charcoal in an acid-ammonium sulfate/potassium bromide mixture |
391353 |
| 1.3.8.7 | FAD |
FAD has an important structural role on the tetramer stability and also in maintaining the volume of the enzyme catalytic pockets. The presence of substrate changes the dynamics of the catalytic pockets and increases FAD affinity |
742255 |
