Any feedback?
Literature summary extracted from
- Characterization of a two-component alkanesulfonate monooxygenase from Escherichia coli (1999), J. Biol. Chem., 274, 26639-26646.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.5.1.38 | - |
Escherichia coli |
| 1.14.14.5 | expressed in Escherichia coli | Escherichia coli |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.5.1.38 | FMN | when NADPH is supplied as pyrimidinic substrate, maximal reductase activity is obtained with 2.5-10 mM FMN, while higher FMN concentration led to 15% decrease in SsuE activity. When NADH is the pyrimidinic substrate, a distinct activity maximum is obtained at an FMN concentration of 0.5 mM, whereas concentrations higher than 2.5 mM led to more than 60% decrease in specific activity | Escherichia coli |  |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.5.1.38 | 0.000054 | - |
FMN | pH 7.9, 30°C | Escherichia coli | |
| 1.5.1.38 | 0.0027 | - |
FAD | pH 7.9, 30°C | Escherichia coli | |
| 1.5.1.38 | 0.046 | - |
NADPH | pH 7.9, 30°C, 0.003 mM FMN | Escherichia coli | |
| 1.5.1.38 | 0.5555 | - |
NADH | pH 7.9, 30°C, 0.0005 mM FMN | Escherichia coli | |
| 1.14.14.5 | 0.035 | - |
decanesulfonic acid | - |
Escherichia coli | |
| 1.14.14.5 | 0.044 | - |
octanesulfonic acid | - |
Escherichia coli | |
| 1.14.14.5 | 0.095 | - |
hexanesulfonic acid | - |
Escherichia coli | |
| 1.14.14.5 | 0.11 | - |
4-phenyl-1-butanesulfonic acid | - |
Escherichia coli | |
| 1.14.14.5 | 0.114 | - |
1,3-dioxo-2-isoindolineethanesulfonic acid | - |
Escherichia coli | |
| 1.14.14.5 | 0.139 | - |
2-(4-pyridyl)ethanesulfonic acid | - |
Escherichia coli | |
| 1.14.14.5 | 0.189 | - |
pentanesulfonic acid | - |
Escherichia coli | |
| 1.14.14.5 | 0.237 | - |
N-phenyltaurine | - |
Escherichia coli | |
| 1.14.14.5 | 0.617 | - |
MOPS | - |
Escherichia coli | |
| 1.14.14.5 | 0.87 | - |
butanesulfonic acid | - |
Escherichia coli | |
| 1.14.14.5 | 1.11 | - |
PIPES | - |
Escherichia coli | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.5.1.38 | 23700 | - |
2 * 23700, calculated from sequence | Escherichia coli |
| 1.5.1.38 | 25400 | - |
2 * 25400, SDS-PAGE | Escherichia coli |
| 1.5.1.38 | 58400 | - |
gel filtration | Escherichia coli |
| 1.14.14.5 | 41200 | - |
4 * 41200, SDS-PAGE | Escherichia coli |
| 1.14.14.5 | 181000 | - |
gel filtration | Escherichia coli |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.5 | R-CH2-SO3H + FMNH2 + O2 | Escherichia coli | - |
R-CHO + FMN + sulfite + H2O | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.5.1.38 | Escherichia coli | P80644 | - |
- |
| 1.14.14.5 | Escherichia coli | - |
EC1250, chromosomal gene cluster ssuEADCB | - |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.5.1.38 | SsuE is purified to homogeneity as an N-terminal histidine-tagged fusion protein | Escherichia coli |
| 1.14.14.5 | - |
Escherichia coli |
Reaction
| EC Number | Reaction | Comment | Organism | Reaction ID |
|---|---|---|---|---|
| 1.14.14.5 | an alkanesulfonate + FMNH2 + O2 = an aldehyde + FMN + sulfite + H2O | absolutely dependent on oxygen | Escherichia coli |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 1.14.14.5 | 2.5 | - |
- |
Escherichia coli |
Storage Stability
| EC Number | Storage Stability | Organism |
|---|---|---|
| 1.14.14.5 | -20°C, 15% glycerol, the activity increases slightly during the first 2 to 3 weeks of storage | Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.5.1.38 | FAD + NADPH + H+ | FMN is the preferred flavin substrate of SsuE but FAD and riboflavin are also reduced at significant rates, whereas lumiflavin is not | Escherichia coli | FADH2 + NADP+ | - |
? | |
| 1.5.1.38 | FMN + NADH + H+ | when NADH is the pyrimidinic substrate, a distinct activity maximum is obtained at an FMN concentration of 0.5 mM, whereas concentrations higher than 2.5 mM led to more than 60% decrease in specific activity | Escherichia coli | FMNH2 + NAD+ | - |
? | |
| 1.5.1.38 | FMN + NADPH + H+ | FMN is the preferred flavin substrate of SsuE but FAD and riboflavin are also reduced at significant rates, whereas lumiflavin is not. When NADPH is supplied as pyrimidinic substrate, maximal reductase activity is obtained with 2.5-10 mM FMN, while higher FMN concentration leads to 15% decrease in SsuE activity. When NADH is the pyrimidinic substrate, a distinct activity maximum is obtained at an FMN concentration of 0.5 mM, whereas concentrations higher than 2.5 mM led to more than 60% decrease in specific activity | Escherichia coli | FMNH2 + NADP+ | - |
? | |
| 1.5.1.38 | riboflavin + NADPH + H+ | FMN is the preferred flavin substrate of SsuE but FAD and riboflavin are also reduced at significant rates, whereas lumiflavin is not | Escherichia coli | reduced riboflavin + NADP+ | - |
? | |
| 1.14.14.5 | 1,3-dioxo-2-isoindolineethanesulfonic acid + FMNH2 + O2 | - |
Escherichia coli | (1,3-dioxo-1,3-dihydro-2H-isoindol-2-yl)acetaldehyd + FMN + sulfite + H2O | - |
? | |
| 1.14.14.5 | 2-(4-pyridyl)ethanesulfonic acid + FMNH2 + O2 | - |
Escherichia coli | pyridin-4-ylacetaldehyde | - |
? | |
| 1.14.14.5 | 4-phenyl-1-butanesulfonic acid + FMNH2 + O2 | - |
Escherichia coli | 4-phenylbutanol + FMN + sulfite + H2O | - |
? | |
| 1.14.14.5 | butanesulfonic acid + FMNH2 + O2 | - |
Escherichia coli | butanal + FMN + sulfite + H2O | - |
? | |
| 1.14.14.5 | decanesulfonic acid + FMNH2 + O2 | - |
Escherichia coli | decanal + FMN + sulfite + H2O | - |
? | |
| 1.14.14.5 | hexanesulfonic acid + FMNH2 + O2 | - |
Escherichia coli | hexanal + FMN + sulfite + H2O | - |
? | |
| 1.14.14.5 | MOPS + FMNH2 + O2 | - |
Escherichia coli | ? | - |
? | |
| 1.14.14.5 | 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 | Escherichia coli | ? | - |
? | |
| 1.14.14.5 | N-phenyltaurine + FMNH2 + O2 | - |
Escherichia coli | anilinoacetaldehyde + FMN + sulfite + H2O | - |
? | |
| 1.14.14.5 | octanesulfonic acid + FMNH2 + O2 | - |
Escherichia coli | octanal + FMN + sulfite + H2O | - |
? | |
| 1.14.14.5 | pentanesulfonic acid + FMNH2 + O2 | - |
Escherichia coli | pentaldehyde + FMN + sulfite + H2O | - |
? | |
| 1.14.14.5 | PIPES + FMNH2 + O2 | - |
Escherichia coli | ? | - |
? | |
| 1.14.14.5 | R-CH2-SO3H + FMNH2 + O2 | - |
Escherichia coli | R-CHO + FMN + sulfite + H2O | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.5.1.38 | homodimer | 2 * 23700, calculated from sequence | Escherichia coli |
| 1.5.1.38 | homodimer | 2 * 25400, SDS-PAGE | Escherichia coli |
| 1.14.14.5 | homotetramer | 4 * 41200, SDS-PAGE | Escherichia coli |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.5.1.38 | SsuE | - |
Escherichia coli |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 1.5.1.38 | 30 | - |
assay at | Escherichia coli |
| 1.14.14.5 | 30 | - |
enzyme assay | Escherichia coli |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 1.5.1.38 | 7.9 | - |
assay at | Escherichia coli |
| 1.14.14.5 | 9.1 | - |
in 10 mM Tris-HCl | Escherichia coli |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.5.1.38 | additional information | the enzyme does not contain any bound flavin cofactor | Escherichia coli | |
| 1.5.1.38 | NADH | kcat/KM for NADPH is 335fold higher compared to kcat/KM for NADH | Escherichia coli | |
| 1.5.1.38 | NADPH | kcat/KM for NADPH is 335fold higher compared kcat/KM for NADH | Escherichia coli | |
| 1.14.14.5 | FMNH2 | - |
Escherichia coli | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.5.1.38 | physiological function | SsuD is a monooxygenase that catalyzes the desulfonation of alkanesulfonates and requires reduced FMN, which is provided by the NAD(P)H:flavin oxidoreductase SsuE | Escherichia coli |
kcat/KM [mM/s]
| EC Number | kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.5.1.38 | 0.00167 | - |
NADH | pH 7.9, 30°C, 0.0005 mM FMN | Escherichia coli | |
| 1.5.1.38 | 0.0079 | - |
FMN | pH 7.9, 30°C | Escherichia coli | |
| 1.5.1.38 | 0.28 | - |
FAD | pH 7.9, 30°C | Escherichia coli | |
| 1.5.1.38 | 0.56 | - |
NADPH | pH 7.9, 30°C, 0.003 mM FMN | Escherichia coli | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
