EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.5.1.40 | additional information | - |
additional information | analysis of the F420 redox moiety (FO)-dependent NADP+/NADPH redox process by stopped-flow spectrophotometry, steady state kinetics, overview | Archaea |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.5.1.40 | reduced coenzyme F420 + NADP+ | Archaea | - |
oxidized coenzyme F420 + NADPH + H+ | - |
r |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.5.1.40 | Archaea | - |
methanogenic | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.5.1.40 | additional information | F420 and the F420 redox moiety, FO, are phenolic 5-deazaflavin cofactors that complement nicotinamide and flavin redox coenzymes in biochemical oxidoreductases and photocatalytic systems. Specifically, these 5-deazaflavins lack the single electron reactivity with O2 of riboflavin-derived coenzymes (FMN and FAD), and, in general, have a more negative redox potential than NAD(P)+. A convenient synthesis of FO is achieved by improving the redox stability of synthetic intermediates containing a polar, electron-rich aminophenol fragment, Fno enzyme activity is restored with FO in the absence of F420, method optimization, overview | Archaea | ? | - |
? | |
1.5.1.40 | reduced coenzyme F420 + NADP+ | - |
Archaea | oxidized coenzyme F420 + NADPH + H+ | - |
r |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.5.1.40 | F420-dependent NADP+ oxidoreductase | - |
Archaea |
1.5.1.40 | Fno | - |
Archaea |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.5.1.40 | physiological function | F420-dependent NADP+ oxidoreductase (Fno) is critical to the conversion of CO2 to CH4 by methanogenic archaea, while the F420 redox moiety, FO, functions as a light-harvesting agent in DNA repair | Archaea |