EC Number   |
General Information |
Reference |
|---|
    1.14.11.17 | more |
development of a colorimetric assay method, based on the measurement of sulfite using Ellman's reagent, i.e. 2.5 mM 5,5'-dithiobis(2-nitrobenzoic acid), for determination of taurine in commercially available beverages and some biological samples, overview |
723940 |
| 1.14.11.17 | more |
metal-to-ligand charge-transfer transition involving the 2-oxoglutarate ligand with a six-coordinate metal center. Taurine does not coordinate the Fe(II) ion, but binds in its close vicinity, leading to loss of the coordinating water molecule. This change of the six-coordinate to five-coordinate Fe(II) center causes a small perturbation of the absorption spectrum |
-, 724974 |
| 1.14.11.17 | more |
structure-activity analysis, modeling and simulations, overview. Modeling of TauD-(Fe-NO) complex and spectral analysis |
725787 |
| 1.14.11.17 | physiological function |
cysteine metabolism |
697475 |
| 1.14.11.17 | physiological function |
important in antibiotic biosynthesis, oxygen sensing, DNA repair, biodegradation of anthropogenic compounds |
701264 |
| 1.14.11.17 | physiological function |
nonheme iron enzyme, activation of C-H bonds |
697518 |
| 1.14.11.17 | physiological function |
the enzyme catalyzes the hydroxylation of taurine eventually leading to sulfite production in Escherichia coli |
-, 765089 |
| 1.14.11.17 | physiological function |
the enzyme is responsible for the microbial catabolism of taurine initiated by hydroxylation of C1 |
-, 764167 |
| 1.14.11.17 | physiological function |
the enzyme metabolizes taurine as a sulfur source for sulfur-starved cells. TauD activates taurine via hydrogen atom transfer to an Fe(IV)=O intermediate |
-, 765270 |
