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Literature summary extracted from

  • Driggers, C.; Dayal, P.; Ellis, H.; Andrew Karplus, P.
    Crystal structure of Escherichia coli SsuE defining a general catalytic cycle for FMN reductases of the flavodoxin-like superfamily (2014), Biochemistry, 53, 3509-3519 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.1.38 gene ssueE, phylogenetic tree, recombinant expression Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.5.1.38 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]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.5.1.38 40900
-
 dimeric SsueE in presence of flavin, analytical ultracentrifugation Escherichia coli
1.5.1.38 73100
-
 tetrameric SsuE enzyme in the absence of flavin, analytical ultracentrifugation Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.1.38 FMNH2 + NADP+ Escherichia coli
-
 FMN + NADPH + H+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.5.1.38 Escherichia coli P80644
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.5.1.38 recombinant enzyme Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
1.5.1.38 FMNH2 + NADP+ = FMN + NADPH + H+ reaction mechanism, overview Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.1.38 FMNH2 + NADP+
-
 Escherichia coli FMN + NADPH + H+
-
 r
1.5.1.38 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

EC Number Subunits Comment Organism
1.5.1.38 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
1.5.1.38 tetramer dimer of dimers, 4 * 21300, analytical ultracentrifugation Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
1.5.1.38 (NADPH)-dependent flavin mononucleotide reductase
-
 Escherichia coli
1.5.1.38 (NADPH)-dependent FMN reductase
-
 Escherichia coli
1.5.1.38 FMN reductase
-
 Escherichia coli
1.5.1.38 SsuE
-
 Escherichia coli
1.5.1.38 ssueE
-
 Escherichia coli
1.5.1.38 ycbP
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.5.1.38 NADP+
-
 Escherichia coli
1.5.1.38 NADPH
-
 Escherichia coli

General Information

EC Number General Information Comment Organism
1.5.1.38 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
1.5.1.38 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
1.5.1.38 additional information at least a dimeric association is required for the function of enzyme SsuE, FMN binding site structure, overview Escherichia coli