EC Number   |
Cofactor |
Reference |
|---|
   1.1.3.17 | FAD |
- |
654876, 696349, 698905, 711016, 712974, 724108, 724282, 724368, 739787, 740068, 740077, 741453 |
| 1.1.3.17 | FAD |
8alpha substituted flavin covalently linked to N1 of H87 |
654712 |
| 1.1.3.17 | FAD |
Ala21 is part of an alpha-helix which interacts with the diphosphate moiety of the flavin cofactor and might influence the activity and specificity of the enzyme |
724047 |
| 1.1.3.17 | FAD |
covalent binding of FAD to purified proteins ascertained, rates of flavin reduction determined in wild-type and mutant variants |
685213 |
| 1.1.3.17 | FAD |
covalently bound in both mutants (V464A and V464T) |
696243 |
| 1.1.3.17 | FAD |
covalently bound to the enzyme, complete reduction of the enzyme-bound flavin is observed in a stopped-flow spectrophotometer upon anaerobic mixing with betaine aldehyde or choline at pH 8.0, with similar kred values |
672121 |
| 1.1.3.17 | FAD |
covalently bound to the enzyme, spectral analysis of denatured wild-type and mutant enzymes, overview |
654773 |
| 1.1.3.17 | FAD |
dependent on |
655800, 674159 |
| 1.1.3.17 | FAD |
dependent on, covalently bound to the enzyme |
671605, 677058 |
| 1.1.3.17 | FAD |
dependent on, covalently bound to the enzyme, involving His466, in an 1:1 stoichiometry, spectrometrical analysis, effects of pH, mutant enzyme H466D shows a 0.29:1 stoichiometry, overview, comparison of midpoint reduction-oxidation potentials of the enzyme-FAD form with mutants H466D and H466A |
672136 |
