EC Number |
Cofactor |
Reference |
---|
1.1.3.2 | FMN |
- |
440395, 744203, 744444, 745455 |
1.1.3.2 | FMN |
flavin reduction is a direct measure of alpha-C-H bond breakage |
746330 |
1.1.3.2 | FMN |
FMN is positioned deep down in the funnel-shaped substrate-binding site, behind (or underneath) the substrate when it is bound. Residues Tyr40, Pro93, Gln144, Tyr146, Thr172, Lys241, Asp296, Arg300 and Arg320 are involved in binding |
743949 |
1.1.3.2 | FMN |
removal of FMN and reconstitution of the apoprotein with 12 FMN derivatives with various substituents at the flavin 6- and 8-positions show an increase in the reduction rate constant with increasing redox potential, except that, with lactate, a limiting rate constant is obtained with flavins of high potential |
746332 |
1.1.3.2 | FMN |
The standard redox potentials of enzyme-FMN/enzyme-FMNH and enzyme-FMNH/enzyme-FMNH2 are -95 mV and -161 mV, respectively, at pH 7.0, 25°C in 0.01 M imidazol buffer |
744451 |