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1,3-dioxo-2-isoindolineethanesulfonic acid + FMNH2 + O2
(1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)acetaldehyd + FMN + sulfite + H2O
-
-
-
-
?
2-(4-pyridyl)ethanesulfonic acid + FMNH2 + O2
pyridin-4-ylacetaldehyde
-
-
-
-
?
4-phenyl-1-butanesulfonic acid + FMNH2 + O2
4-phenylbutanol + FMN + sulfite + H2O
-
-
-
-
?
an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
an alkansulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
-
-
-
-
?
butanesulfonic acid + FMNH2 + O2
butanal + FMN + sulfite + H2O
-
-
-
-
?
decanesulfonic acid + FMNH2 + O2
decanal + FMN + sulfite + H2O
-
-
-
-
?
hexanesulfonic acid + FMNH2 + O2
hexanal + FMN + sulfite + H2O
-
-
-
-
?
MOPS + FMNH2 + O2
?
-
-
-
-
?
N-phenyltaurine + FMNH2 + O2
anilinoacetaldehyde + FMN + sulfite + H2O
-
-
-
-
?
octanesulfonate + FMNH2 + O2
octanal + FMN + sulfite + H2O
octanesulfonic acid + FMNH2 + O2
octanal + FMN + sulfite + H2O
-
-
-
-
?
pentanesulfonic acid + FMNH2 + O2
pentaldehyde + FMN + sulfite + H2O
PIPES + FMNH2 + O2
?
-
-
-
-
?
R-CH2-SO3H + FMNH2 + O2
R-CHO + FMN + sulfite + H2O
-
-
-
?
additional information
?
-
an alkanesulfonate + FMNH2 + O2

an aldehyde + FMN + sulfite + H2O
-
mechanism of flavin reduction in the alkanesulfonate monooxygenase system, the FMN reductase, SsuE, catalyzes the reduction of FMN by NADPH, and the reduced flavin is transferred to the monooxygenase, SsuD, overview
-
-
?
an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
-
the enzyme system is involved in scavenging sulfur from alkanesulfonates under sulfur starvation, overview
-
-
?
an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
-
the two-component alkanesulfonate monooxygenase system, with the flavin mononucleotide reductase, SsuE, being a part of it besides SsuD, utilizes reduced flavin as a substrate to catalyze a unique desulfonation reaction during times of sulfur starvation, protein-protein interactions are important in the mechanism of flavin transfer
-
-
ir
an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
-
the enzyme is involved in scavenging sulfur from alkanesulfonates under sulfur starvation
-
-
?
an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
-
-
-
-
ir
an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
-
-
-
-
?
octanesulfonate + FMNH2 + O2

octanal + FMN + sulfite + H2O
-
-
-
-
?
octanesulfonate + FMNH2 + O2
octanal + FMN + sulfite + H2O
-
SsuD shows a clear preference for FMNH2, reaction via C4a-(hydro)peroxyflavin intermediate
-
-
?
octanesulfonate + FMNH2 + O2
octanal + FMN + sulfite + H2O
-
-
-
?
pentanesulfonic acid + FMNH2 + O2

pentaldehyde + FMN + sulfite + H2O
-
-
-
-
?
pentanesulfonic acid + FMNH2 + O2
pentaldehyde + FMN + sulfite + H2O
-
-
-
?
additional information

?
-
-
further substrates: sulfoacetate, ethanesulfate, propanesulfonate, 2-hydroxyethanesulfonic acid, 3-aminopropanesulfate, no substrate: taurine
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
Cys54 in SsuD may be either directly or indirectly involved in stabilizing the C4a-(hydro)peroxyflavin intermediate formed during catalysis through hydrogen bonding interactions
-
-
?
additional information
?
-
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
-
-
?
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an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
an alkansulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
-
-
-
-
?
R-CH2-SO3H + FMNH2 + O2
R-CHO + FMN + sulfite + H2O
-
-
-
?
additional information
?
-
-
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
-
-
?
an alkanesulfonate + FMNH2 + O2

an aldehyde + FMN + sulfite + H2O
-
the enzyme is involved in scavenging sulfur from alkanesulfonates under sulfur starvation
-
-
?
an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
-
the two-component alkanesulfonate monooxygenase system, with the flavin mononucleotide reductase, SsuE, being a part of it besides SsuD, utilizes reduced flavin as a substrate to catalyze a unique desulfonation reaction during times of sulfur starvation, protein-protein interactions are important in the mechanism of flavin transfer
-
-
ir
an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
-
the enzyme system is involved in scavenging sulfur from alkanesulfonates under sulfur starvation, overview
-
-
?
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Eichhorn, E.; van der Ploeg, J.R.; Leisinger, T.
Deletion analysis of the Escherichia coli taurine and alkanesulfonate transport systems
J. Bacteriol.
182
2687-2795
2000
Escherichia coli
brenda
Eichhorn, E.; van der Ploeg, J.R.; Leisinger, T.
Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coli
J. Biol. Chem.
274
26639-26646
1999
Escherichia coli
brenda
Van der Ploeg, J.R.; Eichhorn, E.; Leisinger, T.
Sulfonate-sulfur metabolism and its regulation in Escherichia coli
Arch. Microbiol.
176
1-8
2001
Escherichia coli
brenda
Eichhorn, E.; Davey, C.A.; Sargent, D.F.; Leisinger, T.
Monooxygenase SsuD
J. Mol. Biol.
324
457-468
2002
Escherichia coli
brenda
Gao, B.; Ellis, H.R.
Altered mechanism of the alkanesulfonate FMN reductase with the monooxygenase enzyme
Biochem. Biophys. Res. Commun.
331
1137-1145
2005
Escherichia coli
brenda
Gao, B.; Ellis, H.R.
Mechanism of flavin reduction in the alkanesulfonate monooxygenase system
Biochim. Biophys. Acta
1774
359-367
2007
Escherichia coli
brenda
Abdurachim, K.; Ellis, H.R.
Detection of protein-protein interactions in the alkanesulfonate monooxygenase system from Escherichia coli
J. Bacteriol.
188
8153-8159
2006
Escherichia coli
brenda
Zhan, X.; Carpenter, R.A.; Ellis, H.R.
Catalytic importance of the substrate binding order for the FMNH2-dependent alkanesulfonate monooxygenase enzyme
Biochemistry
47
2221-2230
2008
Escherichia coli
brenda
Carpenter, R.A.; Zhan, X.; Ellis, H.R.
Catalytic role of a conserved cysteine residue in the desulfonation reaction by the alkanesulfonate monooxygenase enzyme
Biochim. Biophys. Acta
1804
97-105
2010
Escherichia coli
brenda
Robbins, J.; Ellis, H.
Steady-state kinetic isotope effects support a complex role of Arg226 in the proposed desulfonation mechanism of alkanesulfonate monooxygenase
Biochemistry
53
161-168
2014
Escherichia coli (P80645)
brenda
Armacost, K.; Musila, J.; Gathiaka, S.; Ellis, H.R.; Acevedo, O.
Exploring the catalytic mechanism of alkanesulfonate monooxygenase using molecular dynamics
Biochemistry
53
3308-3317
2014
Escherichia coli (P80645)
brenda
Dayal, P.V.; Singh, H.; Busenlehner, L.S.; Ellis, H.R.
Exposing the alkanesulfonate monooxygenase protein-protein interaction sites
Biochemistry
54
7531-7538
2015
Escherichia coli (P80645)
brenda