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Recombinant E. coli, Taurine Dioxygenase (TauD)
TauD, 2-aminoethanesulfonate dioxygenase, Sulfate starvation-induced protein 3, SSI3
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P37610 |
|---|---|
| Concentration | 1.5 mg/ml |
| Calculated MW | 34.3 kDa |
| Gene ID | 945021 |
|---|---|
| Other Names | TauD, 2-aminoethanesulfonate dioxygenase, Sulfate starvation-induced protein 3, SSI3 |
| Gene Source | E. coli |
| Source | E. Coli |
| Assay&Purity | SDS-PAGE;≥90% |
| Recombinant | Yes |
| Target/Specificity | tauD |
| Format | Liquid |
| Storage | -20°C;50 mM Sodium phosphate, pH 7.0 and 30% glycerol |
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Provided below are standard protocols that you may find useful for product applications.
Background
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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