EC Number   |
Cofactor |
Reference |
|---|
   1.1.3.4 | FAD |
defined as flavoprotein oxidase, two very tightly bound FAD molecules per dimer, kinetic behavior |
389803 |
| 1.1.3.4 | FAD |
dependent on, the FAD cofactor is not covalently but tightly bound to the enzyme domain, that consists of a five-stranded beta-sheet sandwiched between a three-stranded beta-sheet and three alpha-helices |
743597 |
| 1.1.3.4 | FAD |
dimerization is only possible with the proper incorporation of the cofactor in the FAD-binding pocket |
726896 |
| 1.1.3.4 | FAD |
dissociation of FAD from the holoenzyme is responsible for the thermal inaction of the enzyme |
656139 |
| 1.1.3.4 | FAD |
each monomer has one co-enzyme molecule of FAD, which acts as an electron receptor during catalysis |
743857 |
| 1.1.3.4 | FAD |
each subunit of dimeric GOD contains one tightly bound FAD as cofactor |
710908 |
| 1.1.3.4 | FAD |
electron transfer between FAD centers and metal electrodes after chemical modification of enzyme |
389817 |
| 1.1.3.4 | FAD |
enzyme pen-GOx contains one mol of tightly but not covalently bound FAD cofactor at the active site of each subunit. The FAD-binding domain of GOx is formed by a beta-sheet lid. The lid prevents the release of FAD from the dimer. Loosening of tertiary structure leads to opening of this lid, causing FAD loss anddissociation of the dimer. Loss of FAD from GOx is concurrent with tertiary structure loss. FAD, especially isoalloxazine, is important for the catalytic activity for beta-D-glucose. The binding of FAD cofactor also plays a key role on the catalytic activity of flavoproteins for the correct folding, assembly and protein stability. The three-dimensional structure of the glucose oxidase is stabilized by FAD, which can act as a redox carrier in catalysis |
743111 |
| 1.1.3.4 | FAD |
flavin-dependent oxidase with covalently linked FAD which is located at the bottom of a funnel-shaped pocket that forms the active site |
696297 |
| 1.1.3.4 | FAD |
flavoenzyme |
676974 |
