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Enzyme Nomenclature
Information on EC 1.14.14.5 - alkanesulfonate monooxygenase
for references in articles please use BRENDA:EC1.14.14.5
Word Map on EC 1.14.14.5
- 1.14.14.5
- flavin
-
desulfonation
- sulfur
-
two-component
- sulfite
- octanesulfonate
-
c4a-hydroperoxyflavin
-
tim-barrel
-
sulfonated
-
organosulfur
-
organosulfonate
-
carbon-sulfur
-
petroleum
-
oxygenolytic
-
homotetrameric
-
fluorimetric
-
peroxyflavin
-
draft
-
half-reaction
-
c4a-peroxyflavin
-
oilfield
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The expected taxonomic range for this enzyme is: Escherichia coli
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EC NUMBER 
COMMENTARY 
1.14.14.5
-
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RECOMMENDED NAME
GeneOntology No.
alkanesulfonate monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an alkanesulfonate + FMNH2 + O2 = an aldehyde + FMN + sulfite + H2O
absolutely dependent on oxygen
-
an alkanesulfonate + FMNH2 + O2 = an aldehyde + FMN + sulfite + H2O
catalysis by SsuD probably results in an unstable 1-hydroxysulfonate that spontaneously decomposes to the corresponding aldehyde and sulfite
-
an alkanesulfonate + FMNH2 + O2 = an aldehyde + FMN + sulfite + H2O
kinetic reaction mechanism, charge transfer complex formation with flavin mononucleotide reductase in the alkanesulfonate monooxygenase system; mechanism of flavin reduction in the alkanesulfonate monooxygenase system, overview
-
an alkanesulfonate + FMNH2 + O2 = an aldehyde + FMN + sulfite + H2O
mechanism of flavin reduction in the alkanesulfonate monooxygenase system, overview
-
an alkanesulfonate + FMNH2 + O2 = an aldehyde + FMN + sulfite + H2O
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
desulfonation
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
alkanesulfonate,FMNH2:oxygen oxidoreductase
The enzyme from Escherichia coli catalyses the desulfonation of a wide range of aliphatic sulfonates (unsubstituted C1- to C14-sulfonates as well as substituted C2-sulfonates). Does not desulfonate taurine (2-aminoethanesulfonate) or aromatic sulfonates. Does not use FMN as a bound cofactor. Instead, it uses reduced FMN (i.e., FMNH2) as a substrate. FMNH2 is provided by SsuE, the associated FMN reductase (EC 1.5.1.38).
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CAS REGISTRY NUMBER
COMMENTARY
54596-24-6
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
-
salt bridges between Arg297 and Glu20 or Asp111 are not critical to the desulfonation mechanism. The predicted role of residue Arg297 is to favorably interact with the phosphate group of the reduced flavin. Arg226 functions as a protection group shielding FMNOO- from bulk solvent and is more pronounced when both FMNOO- and octanesulfonate are bound
physiological function
-
optimal transfer of reduced flavin from NADPH-dependent FMN reductase SsuE to SsuD requires defined protein-protein interactions, but diffusion can occur under specified conditions. A SsuD variant containing substitutions of charged residues shows a 4fold decrease in coupled assays that include SsuE to provide reduced FMN, but there is no activity observed with an SsuD variant containing a deletion of the alpha-helix containing conserved charged amino acids
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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
-
-
-
-
?
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
-
-
-
-
?
octanesulfonic acid + FMNH2 + O2
octanal + FMN + sulfite + H2O
-
-
-
-
?
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
-
-
ir
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
-
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
-
-
-
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
-
-
-
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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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0312
octanesulfonate
-
wild-type, pH 7.5, temperature not specified in the publication
0.0322
octanesulfonate
-
mutant E20A, pH 7.5, temperature not specified in the publication
0.0363
octanesulfonate
-
mutant D111A, pH 7.5, temperature not specified in the publication
additional information
additional information
-
rapid reaction kinetic analysis of SsuE-catalyzed flavin reduction using NADPH; stopped-flow kinetics
-
additional information
additional information
-
kinetics of reaction of SsuD with FMNH2, rapid reaction and stopped flow kinetic analyses, dissociation constants for FMN and FMNH2, detailed overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.065
octanesulfonate
-
mutant E20A, pH 7.5, temperature not specified in the publication
0.675
octanesulfonate
-
mutant D111A, pH 7.5, temperature not specified in the publication
0.73
octanesulfonate
-
wild-type, pH 7.5, temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
18
octanesulfonate
-
mutant D111A, pH 7.5, temperature not specified in the publication; mutant E20A, pH 7.5, temperature not specified in the publication
23
octanesulfonate
-
wild-type, pH 7.5, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
molecular dynamics simulations for Ssud in substrate-free form, bound with FMNH2, bound with a C4a-peroxyflavin intermediate (FMNOO?), bound with octanesulfonate, cobound with FMNH2 and octanesulfonate, and cobound with FMNOO? and octanesulfonate
-
X-ray characterization, tetramer 96 A x 90 A x 66 A, comprises two homodimers, monomer 60A x 50 A x 40 A, TIM-barrel protein
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 15% glycerol, the activity increases slightly during the first 2 to 3 weeks of storage
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene ssuD, the alkanesulfonate monooxygenase system, expressed from the ssuEADCB operon, is comprised of a flavin reductase encoded by ssuE and monooxygenase encoded by ssuD, ssuD expressionin strain BL21(DE3)
-
ligated into pET21a plasmid containing the ssuD gene, wild-type and mutants expressed in Escherichia coli BL21(DE3) super-competent cells
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
C54A
-
has little effect on FMN or FMNH2 binding, kcat/Km value decreases 6fold relative to wild-type
C54S
-
has little effect on FMN or FMNH2 binding, kcat/Km value increases 3fold relative to wild-type. Is able to generate the C4a-(hydro)peroxyflavin, but the rate of formation is increased 10fold relative to wild-type
D251A/D252A/E253A
-
mutation of conserved charged amino acids, 4fold decrease in kcat/Km value
DELTA251-261
-
deletion of alpha-helix containing conserved charged amino acids, complete loss of activity
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LINKS TO OTHER DATABASES (specific for EC-Number 1.14.14.5)
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