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Literature summary for 1.5.1.38 extracted from
- Transformation of a flavin-free FMN reductase to a canonical flavoprotein through modification of the Pi-helix (2016), Biochemistry, 55, 6389-6394 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene ssueE, recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| Y118A | site-directed mutagenesis, the SsuE variant converts the typically flavin-free enzyme to a flavin-bound form. The Y118A SsuE FMN cofactor is reduced with approximately 1 equiv of NADPH in anaerobic titration experiments, and the flavin remains bound following reduction. No measurable sulfite product is formed in a coupled assays with the Y118A SsuE variant and SsuD, demonstrating that flavin transfer is no longer supported | Escherichia coli |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | steady-state kinetic analysis of wild-type and mutant enzymes, kinetics of FMN binding, overview | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| FMNH2 + NADP+ | Escherichia coli | - |
FMN + NADPH + H+ | - |
r |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P80644 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3) | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| FMNH2 + NADP+ | - |
Escherichia coli | FMN + NADPH + H+ | - |
r | |
| additional information | electron transfer to ferricyanide is performed with FMN-bound Y118A SsuE mutant varying concentrations of NADPH, and ferricyanide, the ferricyanide concentration is saturating to maintain pseudo-first-order kinetic conditions at varying NADPH concentrations | Escherichia coli | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| FMN reductase | - |
Escherichia coli |
| NAD(P)H:FMN reductase | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 25 | - |
assay at | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Escherichia coli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADP+ | - |
Escherichia coli | |
| NADPH | - |
Escherichia coli | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the flavin reductase of the alkanesulfonate monooxygenase system (SsuE) contains a conserved Pi-helix located at the tetramer interface that originates from the insertion of Tyr118 into helix alpha4 of SsuE, the presence of Pi-helices provides an evolutionary gain of function. Residue Tyr118 residue generates the Pi-helix in SsuE | Escherichia coli |
| physiological function | the Pi-helix enables SsuE to effectively utilize flavin as a substrate in the two-component monooxygenase system of SsueE with SsueD, overview | Escherichia coli |
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