Information on EC 1.14.14.5 - alkanesulfonate monooxygenase

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The expected taxonomic range for this enzyme is: Escherichia coli

EC NUMBER
COMMENTARY hide
1.14.14.5
-
RECOMMENDED NAME
GeneOntology No.
alkanesulfonate monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
an alkanesulfonate + FMNH2 + O2 = an aldehyde + FMN + sulfite + H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
desulfonation
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
two-component alkanesulfonate monooxygenase
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non-pathway related
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Sulfur metabolism
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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).
CAS REGISTRY NUMBER
COMMENTARY hide
54596-24-6
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
-
-
-
-
?
2-(4-pyridyl)ethanesulfonic acid + FMNH2 + O2
pyridin-4-ylacetaldehyde
show the reaction diagram
-
-
-
-
?
4-phenyl-1-butanesulfonic acid + FMNH2 + O2
4-phenylbutanol + FMN + sulfite + H2O
show the reaction diagram
-
-
-
-
?
an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
show the reaction diagram
an alkansulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
show the reaction diagram
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-
-
-
?
butanesulfonic acid + FMNH2 + O2
butanal + FMN + sulfite + H2O
show the reaction diagram
-
-
-
-
?
decanesulfonic acid + FMNH2 + O2
decanal + FMN + sulfite + H2O
show the reaction diagram
-
-
-
-
?
hexanesulfonic acid + FMNH2 + O2
hexanal + FMN + sulfite + H2O
show the reaction diagram
-
-
-
-
?
MOPS + FMNH2 + O2
?
show the reaction diagram
-
-
-
-
?
N-phenyltaurine + FMNH2 + O2
anilinoacetaldehyde + FMN + sulfite + H2O
show the reaction diagram
-
-
-
-
?
octanesulfonate + FMNH2 + O2
octanal + FMN + sulfite + H2O
show the reaction diagram
octanesulfonic acid + FMNH2 + O2
octanal + FMN + sulfite + H2O
show the reaction diagram
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-
-
-
?
pentanesulfonic acid + FMNH2 + O2
pentaldehyde + FMN + sulfite + H2O
show the reaction diagram
PIPES + FMNH2 + O2
?
show the reaction diagram
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-
-
-
?
R-CH2-SO3H + FMNH2 + O2
R-CHO + FMN + sulfite + H2O
show the reaction diagram
-
-
-
?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
show the reaction diagram
an alkansulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
show the reaction diagram
-
-
-
-
?
R-CH2-SO3H + FMNH2 + O2
R-CHO + FMN + sulfite + H2O
show the reaction diagram
-
-
-
?
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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.114
1,3-dioxo-2-isoindolineethanesulfonic acid
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0.139
2-(4-pyridyl)ethanesulfonic acid
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0.11
4-phenyl-1-butanesulfonic acid
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0.87
butanesulfonic acid
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0.035
decanesulfonic acid
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0.095
hexanesulfonic acid
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0.617
MOPS
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0.237
N-phenyltaurine
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0.0075 - 0.157
octanesulfonate
0.044
octanesulfonic acid
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0.189
pentanesulfonic acid
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1.11
PIPES
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additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.065 - 0.88
octanesulfonate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.005 - 63.3
octanesulfonate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
9.1
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in 10 mM Tris-HCl
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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assay at
30
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enzyme assay
PDB
SCOP
CATH
UNIPROT
ORGANISM
Escherichia coli (strain K12);
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
41200
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4 * 41200, SDS-PAGE
41605
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4 * 41605, mass spectrometry
181000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
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4 * 41200, SDS-PAGE
tetramer
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4 * 41605, mass spectrometry
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
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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
expressed in Escherichia coli
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expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
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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)
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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 hide
LITERATURE
C54A
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has little effect on FMN or FMNH2 binding, kcat/Km value decreases 6fold relative to wild-type
C54S
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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
D111A
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kcat/Km vlaue similar to wild-type
D251A/D252A/E253A
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mutation of conserved charged amino acids, 4fold decrease in kcat/Km value
DELTA251-261
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deletion of alpha-helix containing conserved charged amino acids, complete loss of activity
E20A
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kcat/Km vlaue similar to wild-type
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