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.
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