EC Number |
Cofactor |
Reference |
---|
1.5.99.15 | flavin |
iron-sulfur flavoprotein |
727782 |
1.5.99.15 | FMN |
bioinformatic analysis reveals the presence of one FMN-binding site. The purified protein shows an absorbance peaks at 380 and 460 nm, characteristic of oxidized FMN |
727782 |
1.5.99.15 | Ferredoxin |
ferredoxin may serve as an electron donor |
742781 |
1.5.99.15 | FMN |
the enzyme contains one flavin mononucleotide (FMN)-binding site |
742781 |
1.5.99.15 | more |
NAD(P)H is incapable of directly reducing the flavin cofactor, but dithionite eliminates the FMN peaks, indicating successful electron transfer to MJ0208. An electron transfer system of NADPH, spinach NADPH-ferredoxin oxidoreductase, and ferredoxin can also reduce the FMN peaks. Dithiothreitol-reduced MJ0208 can transfer electrons to dihydromethanopterin |
742781 |
1.5.99.15 | more |
NAD(P)H is incapable of directly reducing the flavin cofactor, but dithionite eliminates the FMN peaks, indicating successful electron transfer to MM1854. An electron transfer system of NADPH, spinach NADPH-ferredoxin oxidoreductase, and ferredoxin can also reduce the FMN peaks. Dithiothreitol-reduced MM1854 can transfer electrons to dihydromethanopterin |
742781 |
1.5.99.15 | [4Fe-4S]-center |
the enzyme contains two iron-sulfur cluster sites |
742781 |
1.5.99.15 | FMN |
- |
742870 |
1.5.99.15 | FMN |
within a homotrimer, each monomer-monomer interface exhibits an active site with two adjacently bound flavin mononucleotide (FMN) ligands, one deeply buried and tightly bound and one more peripheral. Computational docking suggests that the peripheral site binds either the observed FMN (the electron donor for the overall reaction) or the pterin, H2MPT (the electron acceptor for the overall reaction), in configurations ideal for electron transfer to and from the tightly bound FMN. Analysis of the FMN binding structure in the active site, and kinetics, overview |
742870 |
1.5.99.15 | more |
determination of FMN is the cofactor of DmrB, overview |
742870 |