| 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 | calculations using large cluster models that include key hydrogen bonding interactions in the substrate binding pocket and His70 protonated reproduce experimental rates and selectivity excellently and give a dominant C1-hydroxylation channel leading to R-1-hydroxytaurine products. This is triggered by charged active site residues including a protonated His70 group | Escherichia coli | sulfite + aminoacetaldehyde + succinate + CO2 | - |
? | |
| taurine + 2-oxoglutarate + O2 | - |
Escherichia coli K12 | sulfite + aminoacetaldehyde + succinate + CO2 | - |
? | |
| taurine + 2-oxoglutarate + O2 | calculations using large cluster models that include key hydrogen bonding interactions in the substrate binding pocket and His70 protonated reproduce experimental rates and selectivity excellently and give a dominant C1-hydroxylation channel leading to R-1-hydroxytaurine products. This is triggered by charged active site residues including a protonated His70 group | Escherichia coli K12 | sulfite + aminoacetaldehyde + succinate + CO2 | - |
? |
| Synonyms | Comment | Organism |
|---|---|---|
| TauD | - |
Escherichia coli |
| taurine/alpha-ketoglutarate dioxygenase | - |
Escherichia coli |