Protein Variants | Comment | Organism |
---|---|---|
D251A/D252A/E253A | mutation of conserved charged amino acids, 4fold decrease in kcat/Km value | Escherichia coli |
DELTA251-261 | deletion of alpha-helix containing conserved charged amino acids, complete loss of activity | Escherichia coli |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.043 | - |
octanesulfonate | wild-type, pH 7.5, 25°C | Escherichia coli | |
0.157 | - |
octanesulfonate | mutant D251A/D252A/E253A, pH 7.5, 25°C | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P80645 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
octanesulfonate + FMNH2 + O2 | - |
Escherichia coli | octanal + FMN + sulfite + H2O | - |
? |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.85 | - |
octanesulfonate | mutant D251A/D252A/E253A, pH 7.5, 25°C | Escherichia coli | |
0.88 | - |
octanesulfonate | wild-type, pH 7.5, 25°C | Escherichia coli |
General Information | Comment | Organism |
---|---|---|
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 | Escherichia coli |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.005 | - |
octanesulfonate | mutant D251A/D252A/E253A, pH 7.5, 25°C | Escherichia coli | |
0.02 | - |
octanesulfonate | wild-type, pH 7.5, 25°C | Escherichia coli |