Cloned (Comment) | Organism |
---|---|
gene ssueE, phylogenetic tree, recombinant expression | Escherichia coli |
Crystallization (Comment) | Organism |
---|---|
purified recombinant enzyme in apoform, or complexed with FMN or FMNH2, hanging drop vapour diffusion method, mixing 0.004 ml of 10 mg/ml of protein in 10 mM HEPES, pH 7.0, with 0.002 ml of reservoir solution containing 7.5% w/v PEG 3350 and 0.1 M sodium citrate, at room temperature, for complexed protein, the crystals are soaked in an AML containing 1 mM FMN solution, X-ray diffraction structure determination and analysis at 1.9-2.3 A resolution | Escherichia coli |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
40900 | - |
dimeric SsueE in presence of flavin, analytical ultracentrifugation | Escherichia coli |
73100 | - |
tetrameric SsuE enzyme in the absence of flavin, analytical ultracentrifugation | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
FMNH2 + NADP+ | Escherichia coli | - |
FMN + NADPH + H+ | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P80644 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant enzyme | Escherichia coli |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
FMNH2 + NADP+ = FMN + NADPH + H+ | reaction mechanism, overview | Escherichia coli |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
FMNH2 + NADP+ | - |
Escherichia coli | FMN + NADPH + H+ | - |
r | |
additional information | FMN binds tightly in a deeply held site, which makes available a second binding site, in which either a second FMN or the nicotinamide of NADPH can bind. The FMNH2-bound structure shows subtle changes consistent with its binding being weaker than that of FMN | Escherichia coli | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | analytical ultracentrifugation studies of SsuE confirm a dimer-tetramer equilibrium exists in solution, with FMN binding favoring the dimer. The active site includes residues from both subunits | Escherichia coli |
tetramer | dimer of dimers, 4 * 21300, analytical ultracentrifugation | Escherichia coli |
Synonyms | Comment | Organism |
---|---|---|
(NADPH)-dependent flavin mononucleotide reductase | - |
Escherichia coli |
(NADPH)-dependent FMN reductase | - |
Escherichia coli |
FMN reductase | - |
Escherichia coli |
SsuE | - |
Escherichia coli |
ssueE | - |
Escherichia coli |
ycbP | - |
Escherichia coli |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADP+ | - |
Escherichia coli | |
NADPH | - |
Escherichia coli |
General Information | Comment | Organism |
---|---|---|
evolution | enzyme SsuE is part of the flavodoxin-like superfamily. A Pi-helix present at the tetramer building interface of enzyme Ssue is unique to the reductases from two-component monooxygenase systems | Escherichia coli |
metabolism | a general catalytic cycle is proposed for two-component reductases of the flavodoxin-like superfamily, by which the enzyme can potentially provide FMNH2 to its partner monooxygenase by different routes depending on the FMN concentration and the presence of a partner monooxygenase SsueD, overview | Escherichia coli |
additional information | at least a dimeric association is required for the function of enzyme SsuE, FMN binding site structure, overview | Escherichia coli |