Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | fully reversible redox-linked conformational changes in three forms of TauD. The hysteresis between the oxidation and reduction Nernstian NPSV profiles arises primarily from isomerization between two separate ferric/ferrous redox couples of the protein | Escherichia coli |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
taurine + 2-oxoglutarate + O2 | Escherichia coli | - |
sulfite + aminoacetaldehyde + succinate + CO2 | - |
? | |
taurine + 2-oxoglutarate + O2 | Escherichia coli K12 | - |
sulfite + aminoacetaldehyde + succinate + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | P37610 | - |
- |
Escherichia coli K12 | P37610 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
taurine + 2-oxoglutarate + O2 | - |
Escherichia coli | sulfite + aminoacetaldehyde + succinate + CO2 | - |
? | |
taurine + 2-oxoglutarate + O2 | - |
Escherichia coli K12 | sulfite + aminoacetaldehyde + succinate + CO2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
TauD | - |
Escherichia coli |
General Information | Comment | Organism |
---|---|---|
physiological function | the enzyme metabolizes taurine as a sulfur source for sulfur-starved cells. TauD activates taurine via hydrogen atom transfer to an Fe(IV)=O intermediate | Escherichia coli |