EC Number |
Cofactor |
Reference |
---|
1.5.99.15 | FMN |
- |
742870 |
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 | more |
determination of FMN is the cofactor of DmrB, overview |
742870 |
1.5.99.15 | FMN |
DmrB contains 2 FMN molecules on the active site at the monomer-monomer interface. The FMN-1 molecule shows ionic interactions with residues Ser110 and Asn116 along with some non-bonded contacts. The FMN-2 molecule shows ionic contacts with Lys123 and Gln120 and pi-pi stacking with the Tyr85 residue. FMN stabilizes and preserves the secondary and quaternary structure of DmrB against thermal insult |
764885 |
1.5.99.15 | Ferredoxin |
ferredoxin may serve as an electron donor |
742781 |
1.5.99.15 | flavin |
iron-sulfur flavoprotein |
727782 |
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 | FMN |
the enzyme contains one flavin mononucleotide (FMN)-binding site |
742781 |
1.5.99.15 | [4Fe-4S]-center |
the enzyme contains two iron-sulfur cluster sites |
742781 |