1.14.14.5: alkanesulfonate monooxygenase
This is an abbreviated version!
For detailed information about alkanesulfonate monooxygenase, go to the full flat file.
Word Map on EC 1.14.14.5
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1.14.14.5
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flavin
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sulfur
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desulfonation
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two-component
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octanesulfonate
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sulfite
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c4a-hydroperoxyflavin
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organosulfonate
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petroleum
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oxygenolytic
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tim-barrel
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c4a-peroxyflavin
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organosulfur
- 1.14.14.5
- flavin
- sulfur
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desulfonation
-
two-component
- octanesulfonate
- sulfite
-
c4a-hydroperoxyflavin
-
organosulfonate
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petroleum
-
oxygenolytic
-
tim-barrel
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c4a-peroxyflavin
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organosulfur
Reaction
Synonyms
alkanesulfonate alpha-hydroxylase, alkanesulfonate monooxygenase, AOLE_19265, FMNH2-dependent alkanesulfonate monooxygenase, msuD, oxygenase, alkanesulfonate 1-mono-, Pfl01_3916, SsuD, SsuE, sulfate starvation-induced protein 6, YcbN
ECTree
1.14.14.5 alkanesulfonate monooxygenaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 1.14.14.5 - alkanesulfonate monooxygenase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
-
-
?
3-(N-morpholino)propanesulfonate + FMNH2 + O2
? + FMN + sulfite + H2O
MOPS
-
-
?
4-phenyl-1-butanesulfonic acid + FMNH2 + O2
4-phenylbutanol + 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
-
-
-
-
?
N-phenyltaurine + FMNH2 + O2
anilinoacetaldehyde + FMN + sulfite + H2O
-
-
-
-
?
octanesulfonate + FMNH2 + O2
octaldehyde + FMN + sulfite + H2O
-
-
-
?
octanesulfonic acid + FMNH2 + O2
octanal + FMN + sulfite + H2O
-
-
-
-
?
piperazine-N,N'-bis(2-ethanesulfonate) + FMNH2 + O2
? + FMN + sulfite + H2O
PIPES
-
-
?
2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonate + FMNH2 + O2
? + FMN + sulfite + H2O
HEPES
-
-
?
2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonate + FMNH2 + O2
? + FMN + sulfite + H2O
HEPES
-
-
?
an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
-
-
-
-
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
-
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
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-
ir
an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
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the enzyme system is involved in scavenging sulfur from alkanesulfonates under sulfur starvation, overview
-
-
?
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
-
-
-
?
an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
-
-
-
?
hexadecanesulfonate + FMNH2 + O2
hexadecanal + FMN + sulfite + H2O
-
-
-
?
hexadecanesulfonate + FMNH2 + O2
hexadecanal + FMN + sulfite + H2O
-
-
-
?
methanesulfonate + FMNH2 + O2
formaldehyde + FMN + sulfite + H2O
-
-
-
?
methanesulfonate + FMNH2 + O2
formaldehyde + 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
-
-
-
?
octanesulfonate + FMNH2 + O2
octanal + FMN + sulfite + H2O
-
-
-
?
pentanesulfonate + FMNH2 + O2
pentaldehyde + FMN + sulfite + H2O
-
-
-
?
pentanesulfonate + FMNH2 + O2
pentaldehyde + FMN + sulfite + H2O
62% of the activtiy with octanesulfonate
-
-
?
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
?
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-
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
-
-
?
additional information
?
-
when both the lid and C-terminus are ordered and bound in ternary-MsuD, the active site appears completely enclosed from bulk solvent. The apparent volume is larger than methanesulfonate (MS-), consistent with previously observed activity against larger sulfonate substrates. Therefore, molecular docking of substrates ranging in size from pentanesulfonate to PIPES is explored. Docking returns possible poses with the sulfonate moiety in a similar orientation as observed for MS-, but with variable positioning of alkyl groups. Molecular docking defines MsuD as a small- to medium-chain alkanesulfonate monooxygenase. Substrate binding structures for methanesulfonate (alkanesulfonate), FMNH2, and O2, involving the enzyme's C-terminuns, overview
-
-
-
additional information
?
-
-
when both the lid and C-terminus are ordered and bound in ternary-MsuD, the active site appears completely enclosed from bulk solvent. The apparent volume is larger than methanesulfonate (MS-), consistent with previously observed activity against larger sulfonate substrates. Therefore, molecular docking of substrates ranging in size from pentanesulfonate to PIPES is explored. Docking returns possible poses with the sulfonate moiety in a similar orientation as observed for MS-, but with variable positioning of alkyl groups. Molecular docking defines MsuD as a small- to medium-chain alkanesulfonate monooxygenase. Substrate binding structures for methanesulfonate (alkanesulfonate), FMNH2, and O2, involving the enzyme's C-terminuns, overview
-
-
-
additional information
?
-
when both the lid and C-terminus are ordered and bound in ternary-MsuD, the active site appears completely enclosed from bulk solvent. The apparent volume is larger than methanesulfonate (MS-), consistent with previously observed activity against larger sulfonate substrates. Therefore, molecular docking of substrates ranging in size from pentanesulfonate to PIPES is explored. Docking returns possible poses with the sulfonate moiety in a similar orientation as observed for MS-, but with variable positioning of alkyl groups. Molecular docking defines MsuD as a small- to medium-chain alkanesulfonate monooxygenase. Substrate binding structures for methanesulfonate (alkanesulfonate), FMNH2, and O2, involving the enzyme's C-terminuns, overview
-
-
-
