EC Number   |
Cofactor |
Reference |
|---|
  1.5.1.38 | 2-thio-FMN |
binds to the cofactor site of the apoenzyme with an affinity similar to that for FMN binding. The holoenzyme reconstituted with 2-thioFMN is catalytically active in using either FMN or 2-thioFMN as a substrate |
392300 |
| 1.5.1.38 | FMN |
contains a tightly bound FMN cofactor |
392297 |
| 1.5.1.38 | FMN |
the apoenzyme binds one FMN per enzyme monomer with a dissociation constant of 0.2 mM at 23°C. The reconstituted holoenzyme is catalytically as active as the native enzyme. FMN binding results in 87% and 92% of quenching of protein and flavin fluorescence, respectively, indicating a conformational difference between the apoprotein and the holoenzyme. Neither riboflavin nor FAD shows any appreciable binding to the cofactor site of the apoenzyme but both flavins are active substrates for the FMN-containing holoenzyme |
392300 |
| 1.5.1.38 | FMN |
the enzyme is specific for FMN as cofactor. FMN is recognized and tightly bound by a network of 16 hydrogen bonds, while steric considerations prevent the binding of FAD. A flexible loop containing a Lys and an Arg could account for the NADPH specificity |
392299 |
| 1.5.1.38 | more |
the enzyme does not contain any bound flavin cofactor |
438770 |
| 1.5.1.38 | NADH |
kcat/KM for NADPH is 335fold higher compared to kcat/KM for NADH |
438770 |
| 1.5.1.38 | NADP+ |
- |
741865, 741896, 741937 |
| 1.5.1.38 | NADPH |
- |
741865, 741896, 741937, 764152 |
| 1.5.1.38 | NADPH |
kcat/KM for NADPH is 335fold higher compared kcat/KM for NADH |
438770 |
| 1.5.1.38 | NADPH |
the affinity of the NADPH-specific reductase for NADPH is 1000 times greater than for NADH |
392179 |
