General Stability | Organism |
---|---|
binding of ferredoxin, FAD, flavodoxin, or riboflavin stabilizes the enzyme | Escherichia coli |
FNR reduced in the presence of NADPH is slowly inactivated under all conditions. Reactivity towards flavodoxin is lost most rapidly (kinact of 0.031 per min) with less than 10% of the original activity remaining after 30 min, reactivity towards ferredoxin is not as rapidly affected (kinact of 0.0065 per min) with 80% of the original activity remaining after 30 min | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
enzyme catalyzes reactions of both EC 1.18.1.2 and EC 1.19.1.1 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
reduced 2,6-dichlorophenolindophenol + NADP+ | - |
Escherichia coli | oxidized 2,6-dichlorophenolindophenol + NADPH + H+ | - |
? | |
reduced flavodoxin + NADP+ | - |
Escherichia coli | oxidized flavodoxin + NADPH + H+ | - |
? |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
reduced FNR is subject to inactivation due to unfolding of the protein and dissociation of the FADH2 cofactor | Escherichia coli |
41 | - |
melting temperature,reduced FNR in presence of dithiothreitol | Escherichia coli |
66 | - |
melting temperature,oxidized FNR in presence of dithiothreitol | Escherichia coli |