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Information on EC 1.14.14.5 - alkanesulfonate monooxygenase
for references in articles please use BRENDA:EC1.14.14.5
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EC Tree 1 Oxidoreductases
1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
1.14.14.5 alkanesulfonate monooxygenase
IUBMB Comments
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).
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 1.14.14.5
- flavin
- sulfur
-
desulfonation
-
two-component
- octanesulfonate
- sulfite
-
c4a-hydroperoxyflavin
-
organosulfonate
-
petroleum
-
oxygenolytic
-
tim-barrel
-
c4a-peroxyflavin
-
organosulfur
showSynonyms
alkanesulfonate monooxygenase, fmnh2-dependent alkanesulfonate monooxygenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alkanesulfonate alpha-hydroxylase
-
-
-
-
alkanesulfonate monooxygenase
AOLE_19265
msuD
oxygenase, alkanesulfonate 1-mono-
-
-
-
-
Pfl01_3916
SsuD
sulfate starvation-induced protein 6
-
-
-
-
SsuD
-
-
-
-
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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
-
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
proposed mechanism for two-component flavin-dependent alkanesulfonate monooxygenases based on the ternary-MsuD structure, overview
an alkanesulfonate + FMNH2 + O2 = an aldehyde + FMN + sulfite + H2O
proposed mechanism for two-component flavin-dependent alkanesulfonate monooxygenases based on the ternary-MsuD structure, 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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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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
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
-
Substrates: -
Products: -
Products: -
?
2-(4-pyridyl)ethanesulfonic acid + FMNH2 + O2
pyridin-4-ylacetaldehyde
-
Substrates: -
Products: -
Products: -
?
3-(N-morpholino)propanesulfonate + FMNH2 + O2
? + FMN + sulfite + H2O
Substrates: MOPS
Products: -
Products: -
?
4-phenyl-1-butanesulfonic acid + FMNH2 + O2
4-phenylbutanol + FMN + sulfite + H2O
-
Substrates: -
Products: -
Products: -
?
an alkansulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
-
Substrates: -
Products: -
Products: -
?
butanesulfonic acid + FMNH2 + O2
butanal + FMN + sulfite + H2O
-
Substrates: -
Products: -
Products: -
?
decanesulfonic acid + FMNH2 + O2
decanal + FMN + sulfite + H2O
-
Substrates: -
Products: -
Products: -
?
hexanesulfonic acid + FMNH2 + O2
hexanal + FMN + sulfite + H2O
-
Substrates: -
Products: -
Products: -
?
N-phenyltaurine + FMNH2 + O2
anilinoacetaldehyde + FMN + sulfite + H2O
-
Substrates: -
Products: -
Products: -
?
octanesulfonic acid + FMNH2 + O2
octanal + FMN + sulfite + H2O
-
Substrates: -
Products: -
Products: -
?
pentanesulfonic acid + FMNH2 + O2
pentaldehyde + FMN + sulfite + H2O
-
Substrates: -
Products: -
Products: -
?
piperazine-N,N'-bis(2-ethanesulfonate) + FMNH2 + O2
? + FMN + sulfite + H2O
Substrates: PIPES
Products: -
Products: -
?
R-CH2-SO3H + FMNH2 + O2
R-CHO + FMN + sulfite + H2O
-
Substrates: -
Products: -
Products: -
?
2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonate + FMNH2 + O2
? + FMN + sulfite + H2O
Substrates: HEPES
Products: -
Products: -
?
2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonate + FMNH2 + O2
? + FMN + sulfite + H2O
Substrates: HEPES
Products: -
Products: -
?
an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
-
Substrates: 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
Products: -
Products: -
ir
an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
-
Substrates: the enzyme is involved in scavenging sulfur from alkanesulfonates under sulfur starvation
Products: -
Products: -
?
an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
-
Substrates: -
Products: -
Products: -
ir
an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
-
Substrates: -
Products: -
Products: -
?
an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
-
Substrates: the enzyme system is involved in scavenging sulfur from alkanesulfonates under sulfur starvation, overview
Products: -
Products: -
?
an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
-
Substrates: 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
Products: -
Products: -
?
an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
Substrates: -
Products: -
Products: -
?
an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
Substrates: -
Products: -
Products: -
?
hexadecanesulfonate + FMNH2 + O2
hexadecanal + FMN + sulfite + H2O
D8JJB2
Substrates: -
Products: -
Products: -
?
hexadecanesulfonate + FMNH2 + O2
hexadecanal + FMN + sulfite + H2O
D8JJB2
Substrates: -
Products: -
Products: -
?
methanesulfonate + FMNH2 + O2
formaldehyde + FMN + sulfite + H2O
Substrates: -
Products: -
Products: -
?
methanesulfonate + FMNH2 + O2
formaldehyde + FMN + sulfite + H2O
Substrates: -
Products: -
Products: -
?
octanesulfonate + FMNH2 + O2
octaldehyde + FMN + sulfite + H2O
Substrates: -
Products: -
Products: -
?
octanesulfonate + FMNH2 + O2
octaldehyde + FMN + sulfite + H2O
Substrates: -
Products: -
Products: -
?
octanesulfonate + FMNH2 + O2
octanal + FMN + sulfite + H2O
-
Substrates: SsuD shows a clear preference for FMNH2, reaction via C4a-(hydro)peroxyflavin intermediate
Products: -
Products: -
?
octanesulfonate + FMNH2 + O2
octanal + FMN + sulfite + H2O
-
Substrates: -
Products: -
Products: -
?
octanesulfonate + FMNH2 + O2
octanal + FMN + sulfite + H2O
Substrates: -
Products: -
Products: -
?
octanesulfonate + FMNH2 + O2
octanal + FMN + sulfite + H2O
Substrates: -
Products: -
Products: -
?
pentanesulfonate + FMNH2 + O2
pentaldehyde + FMN + sulfite + H2O
Substrates: -
Products: -
Products: -
?
pentanesulfonate + FMNH2 + O2
pentaldehyde + FMN + sulfite + H2O
Substrates: 62% of the activtiy with octanesulfonate
Products: -
Products: -
?
pentanesulfonate + FMNH2 + O2
pentaldehyde + FMN + sulfite + H2O
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: further substrates: sulfoacetate, ethanesulfate, propanesulfonate, 2-hydroxyethanesulfonic acid, 3-aminopropanesulfate, no substrate: taurine
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: Cys54 in SsuD may be either directly or indirectly involved in stabilizing the C4a-(hydro)peroxyflavin intermediate formed during catalysis through hydrogen bonding interactions
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
an alkansulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
-
Substrates: -
Products: -
Products: -
?
R-CH2-SO3H + FMNH2 + O2
R-CHO + FMN + sulfite + H2O
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
-
Substrates: 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
Products: -
Products: -
ir
an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
-
Substrates: the enzyme is involved in scavenging sulfur from alkanesulfonates under sulfur starvation
Products: -
Products: -
?
an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
-
Substrates: the enzyme system is involved in scavenging sulfur from alkanesulfonates under sulfur starvation, overview
Products: -
Products: -
?
an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
Substrates: -
Products: -
Products: -
?
an alkanesulfonate + FMNH2 + O2
an aldehyde + FMN + sulfite + H2O
Substrates: -
Products: -
Products: -
?
methanesulfonate + FMNH2 + O2
formaldehyde + FMN + sulfite + H2O
Substrates: -
Products: -
Products: -
?
methanesulfonate + FMNH2 + O2
formaldehyde + FMN + sulfite + H2O
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FMNH2
dependent on, not permanently enzyme bound, binding structure, overview
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Starvation
Catalytic importance of the substrate binding order for the FMNH2-dependent alkanesulfonate monooxygenase enzyme.
Starvation
Detection of protein-protein interactions in the alkanesulfonate monooxygenase system from Escherichia coli.
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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
-
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 E20A, pH 7.5, temperature not specified in the publication
18
octanesulfonate
mutant D111A, 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
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
additional information
evolution
the enzymes SfnG, MsuC, and MsuD are members of a small subset of flavin-dependent monooxygenases that are characterized by their use of reduced flavin as a cosubstrate rather than a cofactor. Termed two-component flavin-dependent monooxygenases, members of this family lack an NAD(P)H-binding site and therefore require a separate reduced NAD(P)H:oxidized flavin mononucleotide (FMN) oxidoreductase to provide the FMNH- cosubstrate
evolution
-
the enzymes SfnG, MsuC, and MsuD are members of a small subset of flavin-dependent monooxygenases that are characterized by their use of reduced flavin as a cosubstrate rather than a cofactor. Termed two-component flavin-dependent monooxygenases, members of this family lack an NAD(P)H-binding site and therefore require a separate reduced NAD(P)H:oxidized flavin mononucleotide (FMN) oxidoreductase to provide the FMNH- cosubstrate
-
metabolism
small- to medium-chain alkanesulfonate monooxygenase enzyme MsuD plays a role in the sulfur assimilation pathway. The flavin-dependent monooxygenases SfnG, MsuC, and MsuD convert DMSO2 to sulfite. SfnG converts DMSO2 to methanesulfinate (MSI-), MsuC oxidizes MSI- to methanesulfonate (MS-), and MsuD catalyzes the conversion of MS- to sulfite. Together SfnG and MsuD are responsible for sequential cleavage of the two C-S bonds of DMSO2, and each methyl group is presumed to be oxidized to formaldehyde
metabolism
-
small- to medium-chain alkanesulfonate monooxygenase enzyme MsuD plays a role in the sulfur assimilation pathway. The flavin-dependent monooxygenases SfnG, MsuC, and MsuD convert DMSO2 to sulfite. SfnG converts DMSO2 to methanesulfinate (MSI-), MsuC oxidizes MSI- to methanesulfonate (MS-), and MsuD catalyzes the conversion of MS- to sulfite. Together SfnG and MsuD are responsible for sequential cleavage of the two C-S bonds of DMSO2, and each methyl group is presumed to be oxidized to formaldehyde
-
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
physiological function
D8JJB2
genes SsuD and TauD, which encode an alkanesulfonate monooxygenase and a taurine dioxygenase, respectively, are both required to protect cells against oxidative stress, including that generated by n-hexadecane degradation and H2O2 exposure. Both the SsuD and TauD knockout strains exhibit increased sensitivity to H2O2 compared to the wild-type strain
physiological function
bacterial two-component flavin-dependent monooxygenases cleave the stable C-S bond of environmental and anthropogenic organosulfur compounds. The monooxygenase MsuD converts methanesulfonate (MS-) to sulfite, completing the sulfur assimilation process during sulfate starvation
physiological function
-
bacterial two-component flavin-dependent monooxygenases cleave the stable C-S bond of environmental and anthropogenic organosulfur compounds. The monooxygenase MsuD converts methanesulfonate (MS-) to sulfite, completing the sulfur assimilation process during sulfate starvation
-
physiological function
-
genes SsuD and TauD, which encode an alkanesulfonate monooxygenase and a taurine dioxygenase, respectively, are both required to protect cells against oxidative stress, including that generated by n-hexadecane degradation and H2O2 exposure. Both the SsuD and TauD knockout strains exhibit increased sensitivity to H2O2 compared to the wild-type strain
-
additional information
molecular docking, structure-function analysis, roles of the active site lid, the protein C terminus, and an active site loop in flavin and/or alkanesulfonate binding, overview. These structures position MS- closest to the flavin N5 position, consistent with an N5-(hydro)peroxyflavin mechanism rather than a classical C4a-(hydro)peroxyflavin mechanism. A fully enclosed active site is observed in the ternary complex, mediated by interchain interaction of the C-terminus at the tetramer interface identifying a function of the protein C-terminus in this protein family in stabilizing tetramer formation and the alkanesulfonate-binding site. The structures of MsuD with and without ligands support ordered binding for FMNH- and MS-, and the preferential binding of FMN first within chains A/C and E/G is suggestive of possible cooperativity. Without ligands, the active site lid, the sulfonate-binding loop, and the protein C terminus are disordered
additional information
-
molecular docking, structure-function analysis, roles of the active site lid, the protein C terminus, and an active site loop in flavin and/or alkanesulfonate binding, overview. These structures position MS- closest to the flavin N5 position, consistent with an N5-(hydro)peroxyflavin mechanism rather than a classical C4a-(hydro)peroxyflavin mechanism. A fully enclosed active site is observed in the ternary complex, mediated by interchain interaction of the C-terminus at the tetramer interface identifying a function of the protein C-terminus in this protein family in stabilizing tetramer formation and the alkanesulfonate-binding site. The structures of MsuD with and without ligands support ordered binding for FMNH- and MS-, and the preferential binding of FMN first within chains A/C and E/G is suggestive of possible cooperativity. Without ligands, the active site lid, the sulfonate-binding loop, and the protein C terminus are disordered
additional information
-
molecular docking, structure-function analysis, roles of the active site lid, the protein C terminus, and an active site loop in flavin and/or alkanesulfonate binding, overview. These structures position MS- closest to the flavin N5 position, consistent with an N5-(hydro)peroxyflavin mechanism rather than a classical C4a-(hydro)peroxyflavin mechanism. A fully enclosed active site is observed in the ternary complex, mediated by interchain interaction of the C-terminus at the tetramer interface identifying a function of the protein C-terminus in this protein family in stabilizing tetramer formation and the alkanesulfonate-binding site. The structures of MsuD with and without ligands support ordered binding for FMNH- and MS-, and the preferential binding of FMN first within chains A/C and E/G is suggestive of possible cooperativity. Without ligands, the active site lid, the sulfonate-binding loop, and the protein C terminus are disordered
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oligomer
additional information
oligomer
the ligand free enzyme forms a dimer-of-dimers structure in cyrstals, while the liganded enzyme froms a dimer-of-tetramers, overview
oligomer
-
the ligand free enzyme forms a dimer-of-dimers structure in cyrstals, while the liganded enzyme froms a dimer-of-tetramers, overview
-
additional information
MsuD adopts a classic (beta/alpha)8 TIM barrel fold with four insertion segments (ISs) to the (beta/alpha)8 core of MsuD: IS-1 includes two beta-strands (labeled beta1a/b), IS-2 includes an alpha-helix (labeled alpha4a), IS-3 includes a beta-hairpin (labeled beta4a/b); and IS-4 includes three alpha-helices (labeled alpha7a/b/c), a 310 helix (labeled nu7d), and three short beta-strands (labeled beta7a/b/c). In addition, MsuD contains an extended protein C-terminus involved in catalysis
additional information
-
MsuD adopts a classic (beta/alpha)8 TIM barrel fold with four insertion segments (ISs) to the (beta/alpha)8 core of MsuD: IS-1 includes two beta-strands (labeled beta1a/b), IS-2 includes an alpha-helix (labeled alpha4a), IS-3 includes a beta-hairpin (labeled beta4a/b); and IS-4 includes three alpha-helices (labeled alpha7a/b/c), a 310 helix (labeled nu7d), and three short beta-strands (labeled beta7a/b/c). In addition, MsuD contains an extended protein C-terminus involved in catalysis
additional information
-
MsuD adopts a classic (beta/alpha)8 TIM barrel fold with four insertion segments (ISs) to the (beta/alpha)8 core of MsuD: IS-1 includes two beta-strands (labeled beta1a/b), IS-2 includes an alpha-helix (labeled alpha4a), IS-3 includes a beta-hairpin (labeled beta4a/b); and IS-4 includes three alpha-helices (labeled alpha7a/b/c), a 310 helix (labeled nu7d), and three short beta-strands (labeled beta7a/b/c). In addition, MsuD contains an extended protein C-terminus involved in catalysis
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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
molecular dynamics simulations of wild-type SsuD and variant enzymes bound with different combinations of FMNH2, C4a-peroxyflavin intermediate FMNOO-, and octanesulfonate. Mobile loop conformations are open, closed, and semiclosed. The substrate-free SsuD system has a wide opening capable of providing full access for substrates to enter the active site. Upon binding FMNH2, SsuD adopts a closed conformation. Salt bridges, Asp111-Arg263 and Glu205-Arg271, are particularly important in maintaining the closed conformation. With both FMNH2 and octanesulfonate bound in SsuD, a second conformation is formed dependent upon a favorable pi-pi interaction between residues His124 and Phe261
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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alkanesulfonate monooxygenase unliganded and with a bound flavin and alkanesulfonate, co-crystallization with greater than 5fold molar excess of both ligands, sitting drop vapor diffusion, mixing of 0.001 ml of 8 mg/ml protein solution with 0.001 ml of reservoir solution containing 12-18% w/v PEG 3350, and either 0.14-0.20 M succinate or 0.2-0.3 M sodium acetate set up at room temperature, equilibration againt 0.6 ml of reservoir solution, soaking of crystals in 0.002 ml of reservoir solution supplemented with 2 mM FMN and 2 mM methanesulfonate and 0.001 ml containing MsuD crystals and incubated for over 16 h at 18°C, X-ray diffraction structure determination and analysis at 2.4-2.8 A resolution, ternary-MsuD crystallized in the space group P61 with four MsuD chains per asymmetric unit, arranged as a dimer-of-dimers. In the absence of ligands, MsuD crystallizes in space group P21 with two MsuD tetramers (chains A/B/C/D and E/F/G/H) per asymmetric unit. The active site of MsuD is solvent exposed without FMN bound. Molecular replacement of the unliganded MsuD dataset using the structure of homologue SsuD from Escherichia coli strain K12 (PDB ID 1NQK) as template, modeling
structures of MsuD in different liganded states. The active site of MsuD is solvent exposed without FMN bound. Substrate methanesulfonate is positioned closest to the flavin N5 position, consistent with an N5-(hydro)peroxyflavin mechanism rather than a classical C4a-(hydro)peroxyflavin mechanism. A fully enclosed active site is observed in the ternary complex, mediated by interchain interaction of the C terminus at the tetramer interface. The protein C terminus functions in stabilizing tetramer formation and the alkanesulfonate-binding site. MsuD is a small- to medium-chain alkanesulfonate monooxygenase
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PROTEIN VARIANTS
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
R271A
mutation does not alter the catalytic activity, but in the presence of reduced flavin the variant is more susceptible to proteolytic digestion compared to wild-type
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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
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene msuD, genetic structure, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
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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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of SsuD and TauD occurs under sulfate-limited conditions generated during n-hexadecane degradation. Regulator Cbl is responsible for the expression
expression of SsuD and TauD occurs under sulfate-limited conditions generated during n-hexadecane degradation. Regulator Cbl is responsible for the expression
D8JJB2
expression of SsuD and TauD occurs under sulfate-limited conditions generated during n-hexadecane degradation. Regulator Cbl is responsible for the expression
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Park, C.; Shin, B.; Park, W.
Protective role of bacterial alkanesulfonate monooxygenase under oxidative stress
Appl. Environ. Microbiol.
86
e00692
2020
Acinetobacter oleivorans (D8JJB2), Acinetobacter oleivorans DR1 (D8JJB2), Acinetobacter oleivorans DR1
brenda
Thakur, A.; Somai, S.; Yue, K.; Ippolito, N.; Pagan, D.; Xiong, J.; Ellis, H.R.; Acevedo, O.
Substrate-dependent mobile loop conformational changes in alkanesulfonate monooxygenase from accelerated molecular dynamics
Biochemistry
59
3582-3593
2020
Escherichia coli (P80645)
brenda
Liew, J.J.M.; El Saudi, I.M.; Nguyen, S.V.; Wicht, D.K.; Dowling, D.P.
Structures of the alkanesulfonate monooxygenase MsuD provide insight into C-S bond cleavage, substrate scope, and an unexpected role for the tetramer
J. Biol. Chem.
297
100823
2021
Pseudomonas fluorescens (Q3K9A1), Pseudomonas fluorescens, Pseudomonas fluorescens Pf0-1 (Q3K9A1)
brenda
EXTERNAL LINKS (specific for EC-Number 1.14.14.5)
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