EC Number   |
BRENDA No. |
Title |
Journal  |
Volume |
Pages |
Year |
Organism |
PubMed ID |
|---|
    1.14.11.17 | 680611 |
Characterization of a sulfur-regulated oxygenative alkylsulfatase from Pseudomonas putida S-313 |
J. Biol. Chem. |
275 |
31661-31667 |
2000 |
Pseudomonas putida S-313 |
10913158 |
| 1.14.11.17 | 285263 |
Characterization of alpha-ketoglutarate-dependent taurine dioxygenase from Escherichia coli |
J. Biol. Chem. |
272 |
23031-23036 |
1997 |
Escherichia coli |
9287300 |
| 1.14.11.17 | 674930 |
Self-hydroxylation of taurine/alpha-ketoglutarate dioxygenase: evidence for more than one oxygen activation mechanism |
J. Biol. Inorg. Chem. |
11 |
63-72 |
2006 |
Escherichia coli |
16320009 |
| 1.14.11.17 | 765089 |
The Irving-Williams series and the 2-His-1-carboxylate facial triad a thermodynamic study of Mn2+, Fe2+, and Co2+ binding to taurine/?-ketoglutarate dioxygenase (TauD) |
J. Biol. Inorg. Chem. |
23 |
785-793 |
2018 |
Escherichia coli |
29923040 |
| 1.14.11.17 | 765089 |
The Irving-Williams series and the 2-His-1-carboxylate facial triad a thermodynamic study of Mn2+, Fe2+, and Co2+ binding to taurine/?-ketoglutarate dioxygenase (TauD) |
J. Biol. Inorg. Chem. |
23 |
785-793 |
2018 |
Escherichia coli K12 |
29923040 |
| 1.14.11.17 | 688192 |
Metal ligand substitution and evidence for quinone formation in taurine/alpha-ketoglutarate dioxygenase |
J. Inorg. Biochem. |
101 |
797-808 |
2007 |
Escherichia coli |
17350690 |
| 1.14.11.17 | 688611 |
Comparative quantum mechanics/molecular mechanics (QM/MM) and density functional theory calculations on the oxo-iron species of taurine/alpha-ketoglutarate dioxygenase |
J. Phys. Chem. A |
112 |
2464-2468 |
2008 |
Escherichia coli |
18237159 |
| 1.14.11.17 | 743152 |
Atom tunneling in the hydroxylation process of taurine/alpha-ketoglutarate dioxygenase identified by quantum mechanics/molecular mechanics simulations |
J. Phys. Chem. B |
121 |
5347-5354 |
2017 |
Escherichia coli |
28490178 |
| 1.14.11.17 | 725787 |
Measuring the orientation of taurine in the active site of the non-heme Fe(II)/alpha-ketoglutarate-dependent taurine hydroxylase (TauD) using electron spin echo envelope modulation (ESEEM) spectroscopy |
J. Phys. Chem. B |
117 |
10384-10394 |
2013 |
Escherichia coli |
23937570 |
| 1.14.11.17 | 765270 |
Strongly coupled redox-linked conformational switching at the active site of the non-heme iron-dependent dioxygenase, TauD |
J. Phys. Chem. B |
123 |
7785-7793 |
2019 |
Escherichia coli |
31433947 |
