EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
  1.5.1.38 | 2-thioFMN + NADPH + H+ |
the holoenzyme reconstituted with 2-thioFMN is catalytically active in using either FMN or 2-thioFMN as a substrate |
Vibrio harveyi |
2-thioFMNH2 + NADP+ |
- |
? |
| 1.5.1.38 | FAD + NADPH + H+ |
- |
Vibrio harveyi |
FADH2 + NADP+ |
- |
? |
| 1.5.1.38 | FAD + NADPH + H+ |
FMN is the preferred flavin substrate of SsuE but FAD and riboflavin are also reduced at significant rates, whereas lumiflavin is not |
Escherichia coli |
FADH2 + NADP+ |
- |
? |
| 1.5.1.38 | FAD + NADPH + H+ |
Vmax/KM for riboflavin is 6fold lower compared to Vmax/Km for FMN |
Vibrio harveyi |
FADH2 + NADP+ |
- |
? |
| 1.5.1.38 | FAD + NADPH + H+ |
- |
Vibrio harveyi No. 392 |
FADH2 + NADP+ |
- |
? |
| 1.5.1.38 | FMN + NADH + H+ |
when NADH is the pyrimidinic substrate, a distinct activity maximum is obtained at an FMN concentration of 0.5 mM, whereas concentrations higher than 2.5 mM led to more than 60% decrease in specific activity |
Escherichia coli |
FMNH2 + NAD+ |
- |
? |
| 1.5.1.38 | FMN + NADPH + H+ |
- |
Escherichia coli |
FMNH2 + NADP+ |
- |
? |
| 1.5.1.38 | FMN + NADPH + H+ |
- |
Vibrio harveyi |
FMNH2 + NADP+ |
- |
? |
| 1.5.1.38 | FMN + NADPH + H+ |
FMN is the preferred flavin substrate of SsuE but FAD and riboflavin are also reduced at significant rates, whereas lumiflavin is not. When NADPH is supplied as pyrimidinic substrate, maximal reductase activity is obtained with 2.5-10 mM FMN, while higher FMN concentration leads to 15% decrease in SsuE activity. When NADH is the pyrimidinic substrate, a distinct activity maximum is obtained at an FMN concentration of 0.5 mM, whereas concentrations higher than 2.5 mM led to more than 60% decrease in specific activity |
Escherichia coli |
FMNH2 + NADP+ |
- |
? |
| 1.5.1.38 | FMN + NADPH + H+ |
results from single-wavelength analyses at 450 and 550 nm show that reduction of FMN occurs in three distinct phases. Following a possible rapid equilibrium binding of FMN and NADPH to SsuE (MC-1) that occurs before the first detectable step, an initial fast phase (241 s-1) corresponds to the interaction of NADPH with FMN (CT-1). The second phase is a slow conversion (11 s-1) to form a charge-transfer complex of reduced FMNH2 with NADP+ (CT-2), and represents electron transfer from the pyridine nucleotide to the flavin. The third step (19 s-1) is the decay of the charge-transfer complex to SsuE with bound products (MC-2) or product release from the CT-2 complex. Results from isotope studies with [(4R)-2H]NADPH demonstrates a rate-limiting step in electron transfer from NADPH to FMN |
Escherichia coli |
FMNH2 + NADP+ |
- |
? |
