Recombinant E. coli, Taurine Dioxygenase (TauD)
TauD, 2-aminoethanesulfonate dioxygenase, Sulfate starvation-induced protein 3, SSI3
|Calculated MW||34.3 kDa|
|Other Names||TauD, 2-aminoethanesulfonate dioxygenase, Sulfate starvation-induced protein 3, SSI3|
|Gene Source||E. coli|
|Storage||-20°C;50 mM Sodium phosphate, pH 7.0 and 30% glycerol|
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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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