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Literature summary extracted from
- Exploring the catalytic mechanism of alkanesulfonate monooxygenase using molecular dynamics (2014), Biochemistry, 53, 3308-3317 .
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.14.14.5 | 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 | Escherichia coli |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 1.14.14.5 | D111A | kcat/Km vlaue similar to wild-type | Escherichia coli |
| 1.14.14.5 | E20A | kcat/Km vlaue similar to wild-type | Escherichia coli |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.14.5 | 0.0312 | - |
octanesulfonate | wild-type, pH 7.5, temperature not specified in the publication | Escherichia coli |  |
| 1.14.14.5 | 0.0322 | - |
octanesulfonate | mutant E20A, pH 7.5, temperature not specified in the publication | Escherichia coli | |
| 1.14.14.5 | 0.0363 | - |
octanesulfonate | mutant D111A, pH 7.5, temperature not specified in the publication | Escherichia coli | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.14.5 | Escherichia coli | P80645 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.14.5 | octanesulfonate + FMNH2 + O2 | - |
Escherichia coli | octanal + FMN + sulfite + H2O | - |
? | |
Turnover Number [1/s]
| EC Number | Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 1.14.14.5 | 0.065 | - |
octanesulfonate | mutant E20A, pH 7.5, temperature not specified in the publication | Escherichia coli | |
| 1.14.14.5 | 0.675 | - |
octanesulfonate | mutant D111A, pH 7.5, temperature not specified in the publication | Escherichia coli | |
| 1.14.14.5 | 0.73 | - |
octanesulfonate | wild-type, pH 7.5, temperature not specified in the publication | Escherichia coli | |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.14.14.5 | 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 | 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 |
|---|---|---|---|---|---|---|
| 1.14.14.5 | 18 | - |
octanesulfonate | mutant D111A, pH 7.5, temperature not specified in the publication | Escherichia coli | |
| 1.14.14.5 | 18 | - |
octanesulfonate | mutant E20A, pH 7.5, temperature not specified in the publication | Escherichia coli | |
| 1.14.14.5 | 23 | - |
octanesulfonate | wild-type, pH 7.5, temperature not specified in the publication | Escherichia coli | |
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