EC Number   |
Substrates |
Organism |
Products  |
Reversibility |
|---|
    1.14.14.5 | 1,3-dioxo-2-isoindolineethanesulfonic acid + FMNH2 + O2 |
- |
Escherichia coli |
(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)acetaldehyd + FMN + sulfite + H2O |
- |
? |
| 1.14.14.5 | 4-phenyl-1-butanesulfonic acid + FMNH2 + O2 |
- |
Escherichia coli |
4-phenylbutanol + FMN + sulfite + H2O |
- |
? |
| 1.14.14.5 | MOPS + FMNH2 + O2 |
- |
Escherichia coli |
? |
- |
? |
| 1.14.14.5 | more |
further substrates: sulfoacetate, ethanesulfate, propanesulfonate, 2-hydroxyethanesulfonic acid, 3-aminopropanesulfate, no substrate: taurine |
Escherichia coli |
? |
- |
? |
| 1.14.14.5 | more |
no substrates are taurine, methanesulfonic acid, benzenesulfonic acid, L-cysteic acid, ethanedisulfonic acid, toluene-4-sulfonic acid, p-sulfobenzoic acid, benzenesulfonic acid, 4-hydroxybenzenesulfonic acid, SsuD is able to desulfonate C-2 to C-10 unsubstituted alkanesulfonates, substituted ethanesulfonic acids and HEPES, the catalytic efficiency increases with increasing chain length up to decanesulfonic acid |
Escherichia coli |
? |
- |
? |
| 1.14.14.5 | more |
mechanism of flavin reduction in the alkanesulfonate monooxygenase system, consisting of the alkanesulfonate monooxygenase and the flavin mononucleotide reductase, which catalyzes the reduction of FMN by NADPH, overview |
Escherichia coli |
? |
- |
? |
| 1.14.14.5 | more |
the enzyme interacts with the flavin mononucleotide reductase, SsuE, in a 1:1 monomeric association, mechanism of protein-protein interaction not leading to overall conformational changes in protein structure, overview |
Escherichia coli |
? |
- |
? |
| 1.14.14.5 | more |
the two-component alkanesulfonate monooxygenase system from Escherichia coli includes an FMN reductase, SsuE, and an FMNH2-dependent alkanesulfonate monooxygenase, SsuD, involved in the acquisition of sulfur from alkanesulfonates during sulfur starvation, overview |
Escherichia coli |
? |
- |
? |
| 1.14.14.5 | more |
Cys54 in SsuD may be either directly or indirectly involved in stabilizing the C4a-(hydro)peroxyflavin intermediate formed during catalysis through hydrogen bonding interactions |
Escherichia coli |
? |
- |
? |
| 1.14.14.5 | more |
residues Arg226 donates a proton to the FMN-O? intermediate, triggering a conformational change that opens the enzyme to solvation and promotes product release, solvent and kinetic isotope studies |
Escherichia coli |
? |
- |
? |
