Taurine dioxygenase (TauD) is a Fe(II) and α-ketoglutaric acid-dependent dioxygenase, which enables E.coli to use taurine as a sulfur source. The oligomeric state of the enzyme from E.coli is reported both as a dimer and tetramer. It contains a 2-His, 1 carboxylate facial triad, which is present in most members of the family of Fe(II)? α-KG-dependent enzymes. TauD catalyzes the conversion of the amino acid taurine (2-aminoethane-1-sulfonic acid) to sulfite and aminoacetaldehyde. MW: 34.3 kDa. Purity ≥90%
Size
2000 μg
Concentration
1.5 mg/ml
Applications
RUO
Other Names
TauD, 2-aminoethanesulfonate dioxygenase, Sulfate starvation-induced protein 3, SSI5