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Literature summary extracted from
- Detection of protein-protein interactions in the alkanesulfonate monooxygenase system from Escherichia coli (2006), J. Bacteriol., 188, 8153-8159.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.14.5 | expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) | Escherichia coli |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.14.5 | additional information | - |
additional information | steady-state kinetics | Escherichia coli |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 1.5.1.38 | additional information | - |
formation of a stable complex between the flavin mononucleotide (FMN) reductase (SsuE) and monooxygenase (SsuD) of the alkanesulfonate monooxygenase system. The stoichiometry for protein-protein interactions is proposed to involve a 1:1 monomeric association of SsuE with SsuD. Interactions between the two proteins do not lead to overall conformational changes in protein structure | 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 | an alkanesulfonate + FMNH2 + O2 | Escherichia coli | 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 | an aldehyde + FMN + sulfite + H2O | - |
ir |  |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.5.1.38 | Escherichia coli | - |
- |
- |
| 1.14.14.5 | Escherichia coli | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 1.14.14.5 | recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Escherichia coli |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.5 | an alkanesulfonate + FMNH2 + O2 | - |
Escherichia coli | an aldehyde + FMN + sulfite + H2O | - |
ir | |
| 1.14.14.5 | an alkanesulfonate + FMNH2 + O2 | 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 | Escherichia coli | an aldehyde + FMN + sulfite + H2O | - |
ir | |
| 1.14.14.5 | 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 | Escherichia coli | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.5.1.38 | SsuE | - |
Escherichia coli |
| 1.14.14.5 | SsuD | - |
Escherichia coli |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.14.5 | FMNH2 | - |
Escherichia coli | |
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