EC Number   |
Metals/Ions |
Reference |
|---|
    1.14.11.17 | Co2+ |
isothermal titration calorimetry and related biophysical techniques are used to generate complete thermodynamic profiles of Mn2+ and Co2+ binding to the 2-His-1-carboxylate facial triad of TauD |
765089 |
| 1.14.11.17 | Cr2+ |
Cr(II) replaces Fe2+ and binds stoichiometrically with 2-oxoglutarate to the Fe(II)/2-oxoglutarate binding site of the protein, with additional Cr(II) used to generate a chromophore attributed to a Cr(III)-semiquinone in a small percentage of the sample. Formation of the semiquinone requires the dihydroxyphenylalanine quinone form of Y73, generated by intracellular self-hydroxylation |
687079 |
| 1.14.11.17 | Fe |
catalyzes the hydroxylation of taurine to generate sulfite and aminoacetaldehyde in the presence of O2, alpha-ketoglutarate, and Fe(II) |
674930 |
| 1.14.11.17 | Fe |
the enzyme contains a central iron atom that is held in position by interactions with the side chains of two histidine and an aspartic acid residue |
673044 |
| 1.14.11.17 | Fe2+ |
- |
687079 |
| 1.14.11.17 | Fe2+ |
binding structure and role in the kinetic mechanism, overview |
712249 |
| 1.14.11.17 | Fe2+ |
dependent on, mononuclear non-heme iron center, binding structure and kinetics, spectral analysis, overview |
724974 |
| 1.14.11.17 | Fe2+ |
dependent on, non-heme mononuclear Fe(II) center |
725787 |
| 1.14.11.17 | Fe2+ |
fully reversible redox-linked conformational changes in three forms of TauD. The hysteresis between the oxidation and reduction Nernstian NPSV profiles arises primarily from isomerization between two separate ferric/ferrous redox couples of the protein |
765270 |
| 1.14.11.17 | Fe2+ |
maximal activation between 0.005 and 0.150 mM |
285263 |
